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1
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Ayub M, Kaminoff L, Maity A, Ali Z. Detailed primary localised cutaneous nodular amyloidosis clinical and pathological workup. BMJ Case Rep 2024; 17:e262126. [PMID: 39532322 DOI: 10.1136/bcr-2024-262126] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/16/2024] Open
Abstract
Primary localised cutaneous nodular amyloidosis is a rare form of amyloidosis characterised by amyloid deposition in the skin but a lack of further organ involvement; therefore, it is not a systemic disease that progresses to complication. Limited knowledge exists on the causes and outcomes of long-term cutaneous nodular amyloidosis patients. This study reports a case of a woman in her late 80s presenting with a primary cutaneous nodular amyloidosis, with yellow, white plaques and a focal area of violaceous nodules along the inferior lumbar spine. Notably, this rash has been present for nearly 40 years. Histopathological examination revealed amyloid deposits, but further examination showed no amyloid systemic involvement. Recognition of primary nodular amyloidosis through skin biopsy is essential, and current clinical recommendations are to perform pathology examinations to make the diagnosis.
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Affiliation(s)
- Mahaa Ayub
- Thomas Jefferson University Sidney Kimmel Medical College, Philadelphia, Pennsylvania, USA
- Oncology, Lankenau Medical Center, Wynnewood, Pennsylvania, USA
| | - Lizabeth Kaminoff
- Thomas Jefferson University Sidney Kimmel Medical College, Philadelphia, Pennsylvania, USA
| | - Alisha Maity
- Hematology and Oncology, Lankenau Medical Center, Wynnewood, Pennsylvania, USA
| | - Zonera Ali
- Hematology and Oncology, Lankenau Medical Center, Wynnewood, Pennsylvania, USA
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2
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Zhang Y, Le Y, Guo J, Wu F, Li Q, Lu P. Barrier function and ultrastructure characteristics of epidermis in patients with primary cutaneous amyloidosis. J Dermatol 2023. [PMID: 37157942 DOI: 10.1111/1346-8138.16819] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [Grants] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 01/02/2023] [Revised: 03/21/2023] [Accepted: 04/18/2023] [Indexed: 05/10/2023]
Abstract
Previous studies on primary cutaneous amyloidosis (PCA) have mainly focused on exploring genetic mutation and components of amyloid in patients with PCA. However, studies on skin barrier function in PCA patients are scarce. Here, we detected the skin barrier function in PCA patients and healthy people by using noninvasive techniques and characterized ultrastructural features of PCA lesions compared with healthy people using transmission electron microscopy (TEM). The expression of proteins related to skin barrier function was examined by immunohistochemistry staining. A total of 191 patients with clinically diagnosed PCA and 168 healthy individuals were enrolled in the study. Our analysis revealed that all investigated lesion areas displayed higher transepidermal water loss and pH values, and lower Sebum levels and stratum corneum hydration levels in PCA patients compared with the same site area in healthy individuals. The TEM results showed that the intercellular spaces between the basal cells were enlarged and the number of hemidesmosomes decreased in PCA lesions. Immunohistochemical staining showed that the expression of integrin α6 and E-cadherin in PCA patients was less than that in healthy controls, while no differences in the expression of loricrin and filaggrin were observed. Our study revealed that individuals with PCA displayed skin barrier dysfunction, which may be related to alterations in epidermal ultrastructure and a decrease in the skin barrier-related protein E-cadherin. However, the molecular mechanisms underlying skin barrier dysfunction in PCA remain to be elucidated.
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Affiliation(s)
- Yuling Zhang
- Dermatology Hospital, Southern Medical University, Guangzhou, China
- Department of Dermatology, The First Hospital of Jilin University, Changchun, China
| | - Ya Le
- Dermatology Hospital, Southern Medical University, Guangzhou, China
| | - Junyi Guo
- Dermatology Hospital, Southern Medical University, Guangzhou, China
| | - Fangfang Wu
- Dermatology Hospital, Southern Medical University, Guangzhou, China
| | - Qing Li
- Dermatology Hospital, Southern Medical University, Guangzhou, China
| | - Ping Lu
- Dermatology Hospital, Southern Medical University, Guangzhou, China
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3
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Kobayashi K, Iwaide S, Sakai H, Kametani F, Murakami T. Keratinic amyloid deposition in canine hair follicle tumors. Vet Pathol 2023; 60:60-68. [PMID: 36219102 DOI: 10.1177/03009858221128924] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 01/31/2023]
Abstract
Keratinic primary localized cutaneous amyloidosis is a disease in humans; however, no similar condition has been reported in animals. This study aimed to investigate cutaneous keratinic amyloid deposition in dogs and elucidate its etiology. Canine hair follicle tumor tissues were histopathologically analyzed. Immunohistochemistry and mass spectrometry-based proteomic analyses were performed to identify precursor protein candidates. Structural prediction and in vitro fibrillization analyses were conducted to determine the amyloidogenic region and gene sequencing analysis was performed to assess mutations. Of the 266 samples, 16 had amyloid deposition. Amyloid deposits were found in the stroma of tumors and in the margins of keratin debris and around normal hair follicles. Cytokeratin 5 (CK5) was identified as a precursor protein candidate. C-terminal truncation of CK5 was observed in amyloid deposits, and the truncation sites varied depending on the deposition pattern. There was a significantly higher incidence of amyloid deposition in Shiba dogs, and CK5 amino acid polymorphisms were identified in these dogs. A part of the C-terminal region of both canine and human CK5 exhibited highly amyloidogenic properties in vitro. This study revealed the existence of cutaneous keratinic amyloid deposition in animals and identified CK5 as an amyloid precursor protein, providing novel insights into understanding the etiology of cutaneous amyloidosis.
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Affiliation(s)
- Kyoko Kobayashi
- Tokyo University of Agriculture and Technology, Fuchu-shi, Japan
| | - Susumu Iwaide
- Tokyo University of Agriculture and Technology, Fuchu-shi, Japan
| | | | - Fuyuki Kametani
- Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Japan
| | - Tomoaki Murakami
- Tokyo University of Agriculture and Technology, Fuchu-shi, Japan
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Bilton SE, Shah N, Dougherty D, Simpson S, Holliday A, Sahebjam F, Grider DJ. Persistent diarrhea with petechial rash - unusual pattern of light chain amyloidosis deposition on skin and gastrointestinal biopsies: A case report. World J Clin Cases 2022; 10:10252-10259. [PMID: 36246794 PMCID: PMC9561598 DOI: 10.12998/wjcc.v10.i28.10252] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Received: 04/29/2022] [Revised: 05/31/2022] [Accepted: 08/05/2022] [Indexed: 02/05/2023] Open
Abstract
BACKGROUND Amyloidosis is a rare disease characterized by extracellular deposition of misfolded protein aggregated into insoluble fibrils. Gastrointestinal involvement in systemic amyloidosis is common, but is often subclinical or presents as vague and nonspecific symptoms. It is rare for gastrointestinal symptoms to be the main presenting symptom in patients with systemic amyloidosis, causing it to be undiagnosed until late-stage disease.
CASE SUMMARY A 53 year-old man with diarrhea, hematochezia, and weight loss presented to a community hospital. Colonoscopy with biopsy at that time was suspicious for Crohn disease. Due to worsening symptoms including nausea, vomiting, and a new petechial rash, an abdominal fat pad biopsy was done. The biopsy showed papillary and adnexal dermal amyloid deposition, in a pattern usually seen with cutaneous amyloidosis. However, Cytokeratin 5/6 was negative, excluding cutaneous amyloidosis. The patterns of nodular amyloidosis, subcutaneous amyloid deposits and perivascular amyloid were not seen. Periodic Acid-Schiff stain was negative for lipoid proteinosis, Congo red was positive for apple green birefringence on polarization and amyloid typing confirmed amyloid light chain amyloidosis. Repeat endoscopic biopsies of the gastrointestinal tract showed amyloid deposition from the esophagus to the rectum, in a pattern usually seen in serum amyloid A in the setting of chronic inflammatory diseases, including severe inflammatory bowel disease. Bone marrow biopsy showed kappa-restricted plasma cell neoplasm.
CONCLUSION Described is an unusual presentation of primary systemic amyloidosis, highlighting the risk of misdiagnosis with subsequent significant organ dysfunction and high mortality.
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Affiliation(s)
- Shawna E Bilton
- Department of Basic Science Education, Virginia Tech Carilion School of Medicine, Roanoke, VA 24016, United States
| | - Nikhil Shah
- Department of Internal Medicine, Carilion Clinic, Roanoke, VA 24016, United States
| | - Diana Dougherty
- Gastroenterology and Hepatology Section, Department of Internal Medicine, Carilion Clinic, Roanoke, VA 24016, United States
| | - Sarah Simpson
- Dermatology Section, Department of Internal Medicine, Carilion Clinic, Roanoke, VA 24016, United States
| | - Alex Holliday
- Dermatology Section, Department of Internal Medicine, Carilion Clinic, Roanoke, VA 24016, United States
| | - Farhad Sahebjam
- Department of Basic Science Education, Virginia Tech Carilion School of Medicine, Roanoke, VA 24016, United States
- Gastroenterology and Hepatology Section, Department of Internal Medicine, Carilion Clinic, Roanoke, VA 24016, United States
| | - Douglas J Grider
- Department of Basic Science Education, Virginia Tech Carilion School of Medicine, Roanoke, VA 24016, United States
- Pathology, Dominion Pathology Associates, Roanoke, VA 24018, United States
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5
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Anosacral Amyloidosis in a Chinese-Caribbean Male. JAAD Case Rep 2022; 21:46-48. [PMID: 35146100 PMCID: PMC8818804 DOI: 10.1016/j.jdcr.2021.12.003] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 12/04/2022] Open
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Khan NAJ, Nellhaus E, Griswold D, Jamil MO. First Case of Nodular Localized Primary Cutaneous Amyloidosis Treated With Bortezomib and Dexamethasone. J Investig Med High Impact Case Rep 2021; 9:23247096211058488. [PMID: 34894809 PMCID: PMC8672373 DOI: 10.1177/23247096211058488] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 12/05/2022] Open
Abstract
Nodular localized cutaneous amyloidosis is a rare form of cutaneous amyloidosis and is characterized by an extracellular deposition of insoluble amyloid fibrils which are either primarily cutaneous or a manifestation of an underlying systemic amyloidosis. Biopsy of the lesion is mandatory for the diagnosis, and histopathology shows diffuse amyloid deposits with plasmacytic infiltration. Apple-green birefringence characteristic of amyloidosis is observed when stained with Congo red and viewed under polarized light. Amyloid subtyping is done with laser microdissection followed by mass spectrometry. Majority of these lesions do not require any treatment but surgical excision, shave excision, laser therapy, and radiotherapy can be considered for symptomatic nodular localized primary cutaneous amyloidosis (NLPCA). We present a case of recurrent NLPCA in a 64-year-old woman who was treated with bortezomib and dexamethasone after failing several local therapies with excellent response.
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Affiliation(s)
| | - Emma Nellhaus
- Joan C. Edwards School of Medicine, Marshall University, Huntington, WV, USA
| | - Doreen Griswold
- Joan C. Edwards School of Medicine, Marshall University, Huntington, WV, USA
| | - Muhammad Omer Jamil
- Joan C. Edwards School of Medicine, Marshall University, Huntington, WV, USA
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Bourguiba R, Bachmeyer C, Moguelet P, Kaaki S, Ory C, Touchard G, Cattan E, Georgin-Lavialle S, Colombat M, Valleix S. LC-MS/MS and immuno-electron subtyping combined with genetics show that OSMR mutations cause amyloid deposition of keratins 5/14 in familial primary localized cutaneous amyloidosis. J Eur Acad Dermatol Venereol 2021; 36:e66-e68. [PMID: 34459039 DOI: 10.1111/jdv.17630] [Citation(s) in RCA: 1] [Impact Index Per Article: 0.3] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 05/14/2021] [Accepted: 07/29/2021] [Indexed: 11/27/2022]
Affiliation(s)
- R Bourguiba
- Service de Médecine Interne, Hôpital Tenon, AP-HP, Paris, France
| | - C Bachmeyer
- Service de Médecine Interne, Hôpital Tenon, AP-HP, Paris, France
| | - P Moguelet
- Service d'Anatomo-Pathologie, Hôpital Tenon, AP-HP, Paris, France
| | - S Kaaki
- Service d'Anatomie et Cytologie Pathologique, Unité de Pathologie Ultrastructurale, CHU Poitiers and Centre de Référence Amylose AL et autres maladies à dépôts d'immunoglobulines monoclonales, CHU Poitiers, Poitiers, France
| | - C Ory
- Service d'Anatomie et Cytologie Pathologique, Unité de Pathologie Ultrastructurale, CHU Poitiers and Centre de Référence Amylose AL et autres maladies à dépôts d'immunoglobulines monoclonales, CHU Poitiers, Poitiers, France
| | - G Touchard
- Service d'Anatomie et Cytologie Pathologique, Unité de Pathologie Ultrastructurale, CHU Poitiers and Centre de Référence Amylose AL et autres maladies à dépôts d'immunoglobulines monoclonales, CHU Poitiers, Poitiers, France
| | - E Cattan
- Cabinet de Dermatologie, Pantin, France
| | | | - M Colombat
- Service d'Anatomie et Cytologie Pathologique, Institut Universitaire du Cancer, CHU Toulouse, Université Paul Sabatier, Toulouse, France
| | - S Valleix
- Laboratoire de Biologie et Génétique Moléculaires, Hôpital Cochin, AP-HP.CUP, Université de Paris, Paris, France
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8
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Sadeq Islam KM, Hui Y, Singh K, Hansen K, James Sung C, Ruhul Quddus M. Localized amyloidosis in usual-type vulvar intraepithelial neoplasia : High-risk HPV association and potential clinical significance. A series of 45 cases. Gynecol Oncol Rep 2021; 37:100790. [PMID: 34150973 PMCID: PMC8190466 DOI: 10.1016/j.gore.2021.100790] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Received: 03/02/2021] [Revised: 05/07/2021] [Accepted: 05/16/2021] [Indexed: 11/30/2022] Open
Abstract
Localized amyloidosis is only identified in Usual-type HPV-associated VINs. Subtypes of hrHPV in both localized amyloidosis and non-amyloid cases are similar. VINs with localized amyloidosis appear to have a better prognosis. Amyloid deposits persisted even after regression of VINs. Localized amyloid deposits in VINs may be a manifestation of body’s defense mechanism. Localized cutaneous amyloidosis was reported recently in association with vulvar squamous intraepithelial neoplasia (VIN). High-risk human papillomavirus (hrHPV) type 16 is the most commonly reported subtype found in usual-type VIN. However, it is unknown whether any hrHPV subtype(s) is/are prevalent in simultaneous squamous intraepithelial lesions and localized amyloidosis in the same individual - the subject matter of this report. To observe the potential clinical significance, study cases were followed and compared to usual-type VINs without amyloid deposition. Of 45 patients of usual-type VINs associated with amyloidosis, 33 had detectable hrHPV, and 12 were negative. HPV 16 alone or in combination with HPV 31 accounted for 72%, HPV 51 alone accounted for 2% of the cases, and 26% were negative for hrHPV. Lack of demonstrable hrHPV in a significant proportion of cases (26%) raises the possibility of a novel or presently undetected hrHPV subtype. Five of the total 22 (23%) patients with amyloid had either Squamous cell carcinoma or high-grade VIN on follow-up. In contrast, 14 of 18 (78%) patients exhibiting lesions without amyloid had disease on follow-up. These findings may indicate that amyloid deposition may represent a feature of regression or a potential favorable prognostic indicator.
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Affiliation(s)
- K M Sadeq Islam
- Department of Pathology and Laboratory, Women & Infants Hospital/Alpert Medical School of Brown University, Providence, RI 02905, United States
| | - Yiang Hui
- Department of Pathology and Laboratory, Hospital Pathology Associates, PA, Allina Health Laboratories, 2800 10th Avenue South, Minneapolis, MN 55407, United States
| | - Kamaljeet Singh
- Department of Pathology and Laboratory, Women & Infants Hospital/Alpert Medical School of Brown University, Providence, RI 02905, United States
| | - Katrina Hansen
- Department of Pathology and Laboratory, Women & Infants Hospital/Alpert Medical School of Brown University, Providence, RI 02905, United States
| | - C James Sung
- Department of Pathology and Laboratory, Women & Infants Hospital/Alpert Medical School of Brown University, Providence, RI 02905, United States
| | - M Ruhul Quddus
- Department of Pathology and Laboratory, Women & Infants Hospital/Alpert Medical School of Brown University, Providence, RI 02905, United States
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9
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Khan IS, Loh KS, Petersson F. Amyloid and hyaline globules in undifferentiated nasopharyngeal carcinoma. Ann Diagn Pathol 2019; 40:1-6. [PMID: 30822626 DOI: 10.1016/j.anndiagpath.2019.02.016] [Citation(s) in RCA: 4] [Impact Index Per Article: 0.7] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 02/12/2019] [Accepted: 02/17/2019] [Indexed: 10/27/2022]
Abstract
We characterize the clinicopathological features of two patients (one 38 year old woman and one 42 year old man, both of Chinese ethnicity) with Epstein Barr Virus positive non-keratinizing nasopharyngeal carcinoma from an endemic region with prominent presence of amyloid and one case with both amyloid and abundant intracytoplasmic hyaline globules. The amyloid material was positive for Congo red and showed apple green birefringence when examined under polarized light. The amyloid was immunoreactive for cytokeratins and was located both intra- and extracellularly. Frequently the amyloid had a light microscopical spherical appearance and displayed peripheral radiating fibrils from a central homogenous core. One of the patients had a unique presentation of nasopharyngeal carcinoma with perceived hemoptysis and coughing up two pieces of tumor tissue. In reality, the nasopharyngeal tumor was polypoid and the two fragments were pinched of from the main tumor mass.
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Affiliation(s)
- Irfan Sagir Khan
- Department of Pathology, National University Health System, Singapore
| | - Kwok Seng Loh
- Department of Otolaryngology - Head and Neck Surgery, National University Health System, Singapore
| | - Fredrik Petersson
- Department of Pathology, National University Health System, Singapore.
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10
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Ishibuchi H, Motegi SI, Kishi C, Amano H, Yamashita T, Ishikawa O. Localized cutaneous immunoglobulin light chain kappa-positive amyloidosis associated with juvenile dermatomyositis. J Dermatol 2017; 44:e198-e199. [PMID: 28406528 DOI: 10.1111/1346-8138.13856] [Citation(s) in RCA: 1] [Impact Index Per Article: 0.1] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/30/2022]
Affiliation(s)
- Hirohisa Ishibuchi
- Department of Dermatology, Gunma University Graduate School of Medicine, Maebashi, Japan
| | - Sei-Ichiro Motegi
- Department of Dermatology, Gunma University Graduate School of Medicine, Maebashi, Japan
| | - Chikako Kishi
- Department of Dermatology, Gunma University Graduate School of Medicine, Maebashi, Japan
| | - Hiroo Amano
- Department of Dermatology, Gunma University Graduate School of Medicine, Maebashi, Japan
| | - Taro Yamashita
- Department of Neurology, Kumamoto University Graduate School of Medical Sciences, Kumamoto, Japan
| | - Osamu Ishikawa
- Department of Dermatology, Gunma University Graduate School of Medicine, Maebashi, Japan
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11
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Shimoda Y, Sato Y, Hayashida Y, Yamazaki Y, Mizukawa Y, Nakajima K, Shiohara T, Aoyama Y. Lichen amyloidosus as a sweat gland/duct-related disorder: resolution associated with restoration of sweating disturbance. Br J Dermatol 2017; 176:1308-1315. [DOI: 10.1111/bjd.15060] [Citation(s) in RCA: 14] [Impact Index Per Article: 1.8] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Accepted: 09/12/2016] [Indexed: 11/30/2022]
Affiliation(s)
- Y. Shimoda
- Department of Dermatology; Kyorin University School of Medicine; Mitaka Japan
| | - Y. Sato
- Department of Dermatology; Kyorin University School of Medicine; Mitaka Japan
| | - Y. Hayashida
- Dermatology; Kawasaki Medical School; General Medical Center; Okayama Japan
| | - Y. Yamazaki
- Department of Dermatology; Kyorin University School of Medicine; Mitaka Japan
| | - Y. Mizukawa
- Department of Dermatology; Kyorin University School of Medicine; Mitaka Japan
| | - K. Nakajima
- Department of Dermatology; Kochi University School of Medicine; Nankoku Japan
| | - T. Shiohara
- Department of Dermatology; Kyorin University School of Medicine; Mitaka Japan
| | - Y. Aoyama
- Dermatology; Kawasaki Medical School; General Medical Center; Okayama Japan
- Department of Dermatology; Kawasaki Medical School; Kurashiki Japan
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12
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Nam CH, Park MK, Choi MS, Hong SP, Park BC, Kim MH. Secondary Cutaneous Amyloidosis in a Patient with Mycosis Fungoides. Ann Dermatol 2017; 29:79-82. [PMID: 28223751 PMCID: PMC5318532 DOI: 10.5021/ad.2017.29.1.79] [Citation(s) in RCA: 1] [Impact Index Per Article: 0.1] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 03/21/2016] [Revised: 06/16/2016] [Accepted: 06/25/2016] [Indexed: 11/30/2022] Open
Abstract
Secondary cutaneous amyloidosis refers to clinically unapparent amyloid deposits within the skin in association with a pre-existing skin condition or skin tumors, such as basal cell carcinoma, porokeratosis, solar elastosis, Bowen's disease, and mycosis fungoides. A 70-year-old woman presented with a 6-month history of asymptomatic multiple yellowish plaques on both legs. She had been diagnosed with mycosis fungoides 7 years ago and was treated with psoralen and ultraviolet A radiation (PUVA) therapy, narrow-band ultraviolet B (UVB) therapy, and acitretin for 5 years. Finally, she reached complete remission of mycosis fungoides. However, new yellowish lesions started to appear 1 year after discontinuing the phototherapy. A physical examination revealed multiple yellowish plaques on both extremities. The plaques were well circumscribed and slightly elevated. All laboratory tests were normal. A biopsy specimen showed multiple nodular deposits of eosinophilic amorphous material in papillary dermis and upper reticular dermis. The deposits represented apple green birefringence on Congo red stain viewed under polarized light. Acellular small nodules in the upper dermis consisted of randomly oriented, non-branching, 6.67~12.7 nm thick amyloid fibrils on electron microscopy. We report an interesting and rare case of secondary cutaneous amyloidosis after narrow-band UVB therapy and PUVA therapy in a patient with mycosis fungoides.
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Affiliation(s)
- Chan Hee Nam
- Department of Dermatology, Dankook University Medical College, Cheonan, Korea
| | - Min Kee Park
- Department of Dermatology, Dankook University Medical College, Cheonan, Korea
| | - Mi Soo Choi
- Department of Dermatology, Dankook University Medical College, Cheonan, Korea
| | - Seung Phil Hong
- Department of Dermatology, Dankook University Medical College, Cheonan, Korea
| | - Byung Cheol Park
- Department of Dermatology, Dankook University Medical College, Cheonan, Korea
| | - Myung Hwa Kim
- Department of Dermatology, Dankook University Medical College, Cheonan, Korea
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13
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Orchard GE, Wojcik K, Shams F, Georgaki E, Quaye CJ, Fernando P, Torres J, Ismail F, Shams M. Pan-cytokeratin markers for rapid frozen section immunocytochemistry from head and facial Mohs cases of basal cell carcinoma: a comparison and evaluation to determine the marker of choice. Br J Biomed Sci 2015; 72:61-6. [PMID: 26126321 DOI: 10.1080/09674845.2015.11666798] [Citation(s) in RCA: 5] [Impact Index Per Article: 0.5] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 10/21/2022]
Abstract
The application of immunocytochemistry in the field of Mohs micrographic surgery (MMS) is well established. This study evaluates the use of pan-cytokeratins (AE1/AE3, MNF116 and AE1/AE3+PCK26) in the assessment of basal cell carcinoma (BCC) on frozen tissue debulk specimens. Fifty-five cases of BCC, all from head and facial sites, were assessed in the study. In addition to staining all cases for the three cytokeratin antibodies under investigation, sections were also stained with haematoxylin and eosin (H&E) to demonstrate tumour architecture and morphology. All sections for immunocytochemistry were stained on a Roche Ventana BenchMark Ultra automated platform employing a rapid frozen section protocol. Results were assessed based on the intensity of staining of keratinocytes (scale: 0-100%), as well as sensitivity of staining determined by the total percentage of keratinocytes stained within the tissue section. AE1/AE3 demonstrated the most consistent staining both in terms of intensity of staining and sensitivity, with a mean of 99.1% and 99.9%, respectively. AE1/AE3+PCK26 average results indicated scores of 70.6% for intensity and 87.2% for sensitivity, with MNF116 scoring 92.9% for intensity but only 57.3% for sensitivity. The data indicate that AE1/AE3 is the best pan-cytokeratin antibody to use in the assessment of BCC in MMS. The use of cytokeratin immunocytochemistry is justified in morphologically complex cases of BCC, or in cases where dense inflammatory infiltrate surrounding any suspicious cells make identification of small numbers of tumour cells difficult to determine with just an H&E stain. The significant rationale is that cytokeratin staining is a valuable adjunct in the study of tumour cell assessment in cases of MMS for BCC. In addition, the use of anti-AE1/AE3 cytokeratin antibodies provides the most consistent staining results for such cases.
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14
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Panchaprateep R, Tusgate S, Munavalli GS, Noppakun N. Fractional 1,550nm Ytterbium/Erbium fiber laser in the treatment of lichen amyloidosis: Clinical and histological study. Lasers Surg Med 2015; 47:222-30. [DOI: 10.1002/lsm.22338] [Citation(s) in RCA: 9] [Impact Index Per Article: 0.9] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Accepted: 12/21/2014] [Indexed: 11/12/2022]
Affiliation(s)
- Ratchathorn Panchaprateep
- Department of Medicine; Division of Dermatology; King Chulalongkorn Memorial Hospital; Bangkok Thailand
| | - Sai Tusgate
- Department of Medicine; Division of Dermatology; King Chulalongkorn Memorial Hospital; Bangkok Thailand
| | - Girish S. Munavalli
- Division of Dermatology; Laser and Vein Specialists of Carolinas; Charlotte North Carolina
| | - Nopadon Noppakun
- Department of Medicine; Division of Dermatology; King Chulalongkorn Memorial Hospital; Bangkok Thailand
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15
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Westermark P. Localized Amyloidoses and Amyloidoses Associated with Aging Outside the Central Nervous System. CURRENT CLINICAL PATHOLOGY 2015. [DOI: 10.1007/978-3-319-19294-9_7] [Citation(s) in RCA: 5] [Impact Index Per Article: 0.5] [Reference Citation Analysis] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 12/18/2022]
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16
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Ono K, Fujimoto E, Fujimoto N, Akiyama M, Satoh T, Maeda H, Fujii N, Tajima S. In vitro amyloidogenic peptides of galectin-7: possible mechanism of amyloidogenesis of primary localized cutaneous amyloidosis. J Biol Chem 2014; 289:29195-207. [PMID: 25172508 DOI: 10.1074/jbc.m114.592998] [Citation(s) in RCA: 7] [Impact Index Per Article: 0.6] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 12/17/2022] Open
Abstract
Pathogenesis of primary localized cutaneous amyloidosis (PLCA) is unclear, but pathogenic relationship to keratinocyte apoptosis has been implicated. We have previously identified galectin-7, actin, and cytokeratins as the major constituents of PLCA. Determination of the amyloidogenetic potential of these proteins by thioflavin T (ThT) method demonstrated that galectin-7 molecule incubated at pH 2.0 was capable of binding to the dye, but failed to form amyloid fibrils. When a series of galectin-7 fragments containing β-strand peptides were prepared to compare their amyloidogenesis, Ser(31)-Gln(67) and Arg(120)-Phe(136) were aggregated to form amyloid fibrils at pH 2.0. The rates of aggregation of Ser(31)-Gln(67) and Arg(120)-Phe(136) were dose-dependent with maximal ThT levels after 3 and 48 h, respectively. Their synthetic analogs, Phe(33)-Lys(65) and Leu(121)-Arg(134), which are both putative tryptic peptides, showed comparable amyloidogenesis. The addition of sonicated fibrous form of Ser(31)-Gln(67) or Phe(33)-Lys(65) to monomeric Ser(31)-Gln(67) or Phe(33)-Lys(65) solution, respectively, resulted in an increased rate of aggregation and extension of amyloid fibrils. Amyloidogenic potentials of Ser(31)-Gln(67) and Phe(33)-Lys(65) were inhibited by actin and cytokeratin fragments, whereas those of Arg(120)-Phe(136) and Leu(121)-Arg(134) were enhanced in the presence of Gly(84)-Arg(113), a putative tryptic peptide of galectin-7. Degraded fragments of the galectin-7 molecule produced by limited trypsin digestion, formed amyloid fibrils after incubation at pH 2.0. These results suggest that the tryptic peptides of galectin-7 released at neutral pH, may lead to amyloid fibril formation of PLCA in the intracellular acidified conditions during keratinocyte apoptosis via regulation by the galectin-7 peptide as well as actin and cytokeratins.
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Affiliation(s)
- Koji Ono
- From the Department of Dermatology, National Defense Medical College, 3-2 Namiki, Tokorozawa, Saitama 359-8513, Japan and
| | - Eita Fujimoto
- From the Department of Dermatology, National Defense Medical College, 3-2 Namiki, Tokorozawa, Saitama 359-8513, Japan and
| | - Norihiro Fujimoto
- From the Department of Dermatology, National Defense Medical College, 3-2 Namiki, Tokorozawa, Saitama 359-8513, Japan and
| | - Minoru Akiyama
- From the Department of Dermatology, National Defense Medical College, 3-2 Namiki, Tokorozawa, Saitama 359-8513, Japan and
| | - Takahiro Satoh
- From the Department of Dermatology, National Defense Medical College, 3-2 Namiki, Tokorozawa, Saitama 359-8513, Japan and
| | - Hiroki Maeda
- Research Reactor Institute, Kyoto University, Kumatori, Sennan, Osaka 590-0494, Japan
| | - Noriko Fujii
- Research Reactor Institute, Kyoto University, Kumatori, Sennan, Osaka 590-0494, Japan
| | - Shingo Tajima
- From the Department of Dermatology, National Defense Medical College, 3-2 Namiki, Tokorozawa, Saitama 359-8513, Japan and
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17
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Haemel A, Fox L, McCalmont TH. Keratinocyte-derived amyloidosis as a manifestation of chronic graft-versus-host disease. J Cutan Pathol 2013; 40:291-4. [PMID: 23899263 DOI: 10.1111/cup.12105] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Accepted: 01/08/2013] [Indexed: 11/30/2022]
Affiliation(s)
- Anna Haemel
- Department of Dermatology, University of California, San Francisco, CA, USA
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18
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Miura Y, Harumiya S, Ono K, Fujimoto E, Akiyama M, Fujii N, Kawano H, Wachi H, Tajima S. Galectin-7 and actin are components of amyloid deposit of localized cutaneous amyloidosis. Exp Dermatol 2012; 22:36-40. [DOI: 10.1111/exd.12065] [Citation(s) in RCA: 14] [Impact Index Per Article: 1.1] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Accepted: 11/15/2012] [Indexed: 12/15/2022]
Affiliation(s)
- Yoshinori Miura
- Department of Dermatology; National Defense Medical College; Saitama; Japan
| | - Satoru Harumiya
- Department of Cell Signaling, Graduate School of Medical and Dental Sciences; Tokyo Medical and Dental University; Tokyo; Japan
| | - Koji Ono
- Department of Dermatology; National Defense Medical College; Saitama; Japan
| | - Eita Fujimoto
- Department of Dermatology; National Defense Medical College; Saitama; Japan
| | - Minoru Akiyama
- Department of Dermatology; National Defense Medical College; Saitama; Japan
| | - Noriko Fujii
- Research Reactor Institute; Kyoto University; Osaka; Japan
| | - Hiroo Kawano
- Department of Pathology; Yamaguchi University Graduate School of Medicine; Yamaguchi; Japan
| | - Hiroshi Wachi
- Department of Clinical Chemistry; Hoshi University School of Pharmacy and Pharmaceutical Science; Tokyo; Japan
| | - Shingo Tajima
- Department of Dermatology; National Defense Medical College; Saitama; Japan
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19
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Abstract
Concepts and semantics are crucial for good communication between clinicians and pathologists. Amyloidosis was described more than 150 years ago. Therefore, the terminology related to it is abundant, varied, and sometimes complex. In this report, we intend to discuss several terms related to the disease, with special emphasis on cutaneous amyloidosis. We present a review, from Virchow to present, of the concepts related to amyloidosis: its nature, the classification of cutaneous forms of the disease, and the techniques used in its diagnosis.
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20
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Extensive Fibrin Accumulation and Accompanying Epithelial Changes in the Pathogenesis of Ligneous Mucosal Disease (Ligneous Periodontitis). Am J Dermatopathol 2012; 34:35-40. [DOI: 10.1097/dad.0b013e3182169507] [Citation(s) in RCA: 11] [Impact Index Per Article: 0.8] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/25/2022]
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21
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Clos AL, Kayed R, Lasagna-Reeves CA. Association of skin with the pathogenesis and treatment of neurodegenerative amyloidosis. Front Neurol 2012; 3:5. [PMID: 22319507 PMCID: PMC3262151 DOI: 10.3389/fneur.2012.00005] [Citation(s) in RCA: 17] [Impact Index Per Article: 1.3] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 10/06/2011] [Accepted: 01/04/2012] [Indexed: 12/12/2022] Open
Abstract
Amyloidosis are a large group of conformational diseases characterized by abnormal protein folding and assembly which results in the accumulation of insoluble protein aggregates that may accumulate systemically or locally in certain organs or tissue. In local amyloidosis, amyloid deposits are restricted to a particular organ or tissue. Alzheimer’s, Parkinson’s disease, and amyotrophic lateral sclerosis are some examples of neurodegenerative amyloidosis. Local manifestation of protein aggregation in the skin has also been reported. Brain and skin are highly connected at a physiological and pathological level. Recently several studies demonstrated a strong connection between brain and skin in different amyloid diseases. In the present review, we discuss the relevance of the “brain–skin connection” in different neurodegenerative amyloidosis, not only at the pathological level, but also as a strategy for the treatment of these diseases.
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Affiliation(s)
- Audra L Clos
- Department of Dermatology, MD Anderson Cancer Center, University of Texas Houston, TX, USA
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22
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Wenson SF, Jessup CJ, Johnson MM, Cohen LM, Mahmoodi M. Primary cutaneous amyloidosis of the external ear: a clinicopathological and immunohistochemical study of 17 cases. J Cutan Pathol 2011; 39:263-9. [PMID: 22077601 DOI: 10.1111/j.1600-0560.2011.01812.x] [Citation(s) in RCA: 10] [Impact Index Per Article: 0.7] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/28/2022]
Abstract
Primary cutaneous amyloidosis includes several forms of localized amyloidosis characterized by superficial amyloid deposits occurring at or near the dermal-epidermal junction in the absence of systemic involvement. Primary cutaneous amyloidosis of the auricular concha and external ear represents a rarely described variant. There have been 27 cases reported in the English language literature, and herein we report 17 additional cases. This article demonstrates that the amyloid observed in this context is generally positive for Congo red, crystal violet and thioflavin T. It also expresses cytokeratin 34ßE12 via immunohistochemistry. Our immunohistochemical results and review of the literature suggest that the amyloid in amyloidosis of the external ear is the result of basal keratinocyte degeneration and does not signify deposition from a systemic or generalized process.
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Affiliation(s)
- Scott F Wenson
- Department of Pathology, Beth Israel Deaconess Medical Center/Harvard Medical School, Boston, MA, USA
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23
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Clos AL, Lasagna-Reeves CA, Kelly B, Wagner R, Wilkerson M, Jackson GR, Kayed R. Role of oligomers in the amyloidogenesis of primary cutaneous amyloidosis. J Am Acad Dermatol 2011; 65:1023-31. [DOI: 10.1016/j.jaad.2010.09.735] [Citation(s) in RCA: 9] [Impact Index Per Article: 0.6] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 07/29/2010] [Revised: 09/28/2010] [Accepted: 09/30/2010] [Indexed: 11/30/2022]
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24
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Tanaka A, Lai-Cheong JE, van den Akker PC, Nagy N, Millington G, Diercks GFH, van Voorst Vader PC, Clements SE, Almaani N, Techanukul T, Hide M, South AP, McGrath JA. The molecular skin pathology of familial primary localized cutaneous amyloidosis. Exp Dermatol 2011; 19:416-23. [PMID: 20507362 DOI: 10.1111/j.1600-0625.2010.01083.x] [Citation(s) in RCA: 24] [Impact Index Per Article: 1.7] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/30/2022]
Abstract
Familial primary localized cutaneous amyloidosis (FPLCA) is an autosomal dominant disorder associated with chronic itching and skin lichenification. In lesional skin, there are apoptotic basal keratinocytes and deposits of amyloid material on degenerate keratin filaments in the upper dermis. The genetic basis of FPLCA involves mutations in the OSMR and IL31RA genes but the disease pathophysiology is not fully understood. In this study, we identified new pathogenic heterozygous missense mutations in the OSMR gene (p.Val631Leu and p.Asp647Tyr) in two Dutch FPLCA families. We then compared gene expression profiles between FPLCA lesional skin (n = 4) and site-matched control skin (n = 6). There was twofold or greater upregulation of 34 genes and downregulation of 43 genes. Most changes in gene expression (verified by quantitative RT-PCR) reflected alterations in epidermal differentiation and proliferation consistent with lichenification, but we also noted a reduction in several interfollicular keratinocyte stem cell markers in FPLCA skin. Differences in gene expression were also noted for proteins involved in apoptosis and nerve conduction. Collectively, this study expands the molecular basis of FPLCA and provides new insight into the skin pathology of this condition.
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Affiliation(s)
- Akio Tanaka
- St John's Institute of Dermatology, King's College London, London, UK
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25
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Abstract
Amyloids are common protein aggregates in nature. Some amyloids fulfill important biological tasks while others are known to cause diseases. Despite the fact that the ultrastructure of amyloid is highly conserved, the mechanism of amyloidogenesis remains a challenging research topic. In humans, amyloidoses may develop in the skin or lead to skin signs due to secondary cutaneous involvement. An accurate diagnostic procedure is crucial for planning the therapy of this heterogeneous group of diseases. Therefore, the aim of this paper is to give an overview on the different kinds of amyloidoses as well as on diagnostic and therapeutic approaches. Furthermore, the discrimination between functional and disease-causing amyloid is briefly presented.
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Affiliation(s)
- S Schreml
- Klinik und Poliklinik für Dermatologie, Universitätsklinikum Regensburg, Franz-Josef-Strauss-Allee 11, 93053, Regensburg.
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26
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Aoki M, Niimi Y, Ishiko A, Kawana S. Pretibial dystrophic epidermolysis bullosa with localized cutaneous amyloidosis: coincidental or secondary amyloidosis? J Dermatol 2010; 37:259-63. [PMID: 20507391 DOI: 10.1111/j.1346-8138.2009.00794.x] [Citation(s) in RCA: 1] [Impact Index Per Article: 0.1] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/27/2022]
Abstract
Here, we describe the case of a patient with pretibial dystrophic epidermolysis bullosa (PDEB) with amyloid deposition. The patient was a 40-year-old Japanese woman who presented a blistering eruption in the pretibial area with flat violaceous-brown lichenoid papules. The histology of the blister revealed a subepidermal bulla with antibodies bound to basement membrane antigens on the blister roof by immunoflourescent mapping. Electron microscopy revealed a blister cleavage plane below the lamina densa. The histology of the lichenoid papules showed amyloid deposition in the papillary dermis. Because it was confined to just beneath the bulla base of the blister specimen, the amyloid deposition may have been derived from degenerated keratinocytes induced by damage to the epidermal-dermal junction due to blister formation in PDEB in this case. PDEB, in general, is often misdiagnosed as lichen amyloidosis; however, some PDEB cases could actually be associated with amyloid deposition.
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Affiliation(s)
- Mikako Aoki
- Department of Dermatology, Nippon Medical School Musashikosugi Hospital, Kawasaki City, Kanagawa, Japan.
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27
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Amyloid light chain deposition associated with dermatofibroma: serendipity or association? Am J Dermatopathol 2010; 32:298-300. [PMID: 20110798 DOI: 10.1097/dad.0b013e3181b7fd94] [Citation(s) in RCA: 2] [Impact Index Per Article: 0.1] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/25/2022]
Abstract
Primary cutaneous amyloidosis, also known as nodular amyloidosis, is defined as deposition of amyloid light chain in the skin in the absence of a systemic cause of amyloidosis. Such amyloid is produced by a localized aggregate of clonal plasma cells. In contrast, secondary cutaneous amyloidosis is related to lesions such as squamous cell carcinoma, Bowen disease, basal cell carcinoma, and discoid lupus erythematosus, and has been shown in most cases to be derived from keratin epithelial elements. Herein, we present a unique case of nodular amyloidosis occurring in association with a cellular dermatofibroma.
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28
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Babilas P, Fiebig B, Aslanidis C, Hansen J, Röcken C, Schroeder J, Schmitz G, Weber B, Landthaler M, Vogt T. Identification of an oncostatin M receptor mutation associated with familial primary cutaneous amyloidosis. Br J Dermatol 2009; 161:944-7. [DOI: 10.1111/j.1365-2133.2009.09237.x] [Citation(s) in RCA: 10] [Impact Index Per Article: 0.6] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/28/2022]
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29
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Arita K, Abe R, Baba K, McGrath JA, Akiyama M, Shimizu H. A novel OSMR mutation in familial primary localized cutaneous amyloidosis in a Japanese family. J Dermatol Sci 2009; 55:64-5. [DOI: 10.1016/j.jdermsci.2009.03.003] [Citation(s) in RCA: 7] [Impact Index Per Article: 0.4] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 01/09/2009] [Revised: 02/23/2009] [Accepted: 03/02/2009] [Indexed: 11/26/2022]
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30
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Tanaka A, Arita K, Lai-Cheong JE, Palisson F, Hide M, McGrath JA. New insight into mechanisms of pruritus from molecular studies on familial primary localized cutaneous amyloidosis. Br J Dermatol 2009; 161:1217-24. [PMID: 19663869 DOI: 10.1111/j.1365-2133.2009.09311.x] [Citation(s) in RCA: 53] [Impact Index Per Article: 3.3] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/26/2022]
Abstract
Macular and lichen amyloidosis are common variants of primary localized cutaneous amyloidosis (PLCA) in which clinical features of pruritus and skin scratching are associated with histological findings of deposits of amyloid staining on keratinous debris in the papillary dermis. Most cases are sporadic, but an autosomal dominant family history may be present in up to 10% of cases, consistent with a genetic predisposition in some individuals. Familial PLCA has been mapped to a locus on 5p13.1-q11.2 and in 2008 pathogenic heterozygous missense mutations were identified in the OSMR gene, which encodes oncostatin M receptor beta (OSMRbeta), an interleukin (IL)-6 family cytokine receptor. OSMRbeta is expressed in various cell types, including keratinocytes, cutaneous nerves and nociceptive neurones in dorsal root ganglia; its ligands are oncostatin M and IL-31. All pathogenic mutations are clustered in the fibronectin-III repeat domains of the extracellular part of OSMRbeta, sites that are critical for receptor dimerization (with either gp130 or IL-31RA), and lead to defective signalling through Janus kinase-signal transducers and activators of transcription, extracellular signal-regulated protein kinase 1/2 and phosphoinositide 3 kinase/Akt pathways. Elucidating the molecular pathology of familial PLCA provides new insight into mechanisms of pruritus in human skin, findings that may have relevance to developing novel treatments for skin itching. This review provides a clinicopathological and molecular update on familial PLCA.
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Affiliation(s)
- A Tanaka
- St John's Institute of Dermatology, King's College London (Guy's Campus), London, U.K
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31
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Taniguchi Y, Horino T, Terada Y. Cutaneous amyloidosis associated with amyopathic dermatomyositis. J Rheumatol 2009; 36:1088-9. [PMID: 19435977 DOI: 10.3899/jrheum.081148] [Citation(s) in RCA: 6] [Impact Index Per Article: 0.4] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/22/2022]
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32
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Abstract
Amyloid and amyloidosis describes a heterogeneous group of diseases which are characterized by the pathological extracellular deposition of autologous proteins. Basically, amyloidoses can be divided into systemic or organ-limited (e.g. cutaneous) forms and can be acquired or hereditary in nature. The subclassification discriminates between primary amyloidosis (in the absence of an obvious predisposing disease) and secondary amyloidosis (if caused by a certain underlying disease). The subclassification of amyloidoses is based on the main protein constituent and therefore on the chemical composition of the amyloid fibrils. However, the exact etiopathogenesis of amyloid formation remains unclear. In addition to the clinical presentation, histology, electron microscopy and biochemical-immunological differentiation are also decisive for a proper diagnosis. In cutaneous amyloidosis the deposition of amyloid either occurs along reticulin fibers and the basal membrane (perireticulary amyloidoses) or along collagen fibers (pericollagenous amyloidosis). The purpose of this article is to provide an up-to-date overview on the different kinds of cutaneous amyloidoses.
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33
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Maddison B, Namazi M, Samuel L, Sanchez J, Pichardo R, Stocks J, Maruziva D, Yosipovitch G. Unexpected diminished innervation of epidermis and dermoepidermal junction in lichen amyloidosus. Br J Dermatol 2008; 159:403-6. [DOI: 10.1111/j.1365-2133.2008.08685.x] [Citation(s) in RCA: 30] [Impact Index Per Article: 1.8] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/29/2022]
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34
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CHANG Y, LIU H, WONG C, CHOW K, CHEN K. Detection of Epstein-Barr virus in primary cutaneous amyloidosis. Br J Dermatol 2008. [DOI: 10.1046/j.1365-2133.1997.01824.x] [Citation(s) in RCA: 9] [Impact Index Per Article: 0.5] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/20/2022]
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35
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Arita K, South AP, Hans-Filho G, Sakuma TH, Lai-Cheong J, Clements S, Odashiro M, Odashiro DN, Hans-Neto G, Hans NR, Holder MV, Bhogal BS, Hartshorne ST, Akiyama M, Shimizu H, McGrath JA. Oncostatin M receptor-beta mutations underlie familial primary localized cutaneous amyloidosis. Am J Hum Genet 2008; 82:73-80. [PMID: 18179886 DOI: 10.1016/j.ajhg.2007.09.002] [Citation(s) in RCA: 95] [Impact Index Per Article: 5.6] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 07/26/2007] [Revised: 08/28/2007] [Accepted: 09/11/2007] [Indexed: 10/22/2022] Open
Abstract
Familial primary localized cutaneous amyloidosis (FPLCA) is an autosomal-dominant disorder associated with chronic skin itching and deposition of epidermal keratin filament-associated amyloid material in the dermis. FPLCA has been mapped to 5p13.1-q11.2, and by candidate gene analysis, we identified missense mutations in the OSMR gene, encoding oncostatin M-specific receptor beta (OSMRbeta), in three families. OSMRbeta is a component of the oncostatin M (OSM) type II receptor and the interleukin (IL)-31 receptor, and cultured FPLCA keratinocytes showed reduced activation of Jak/STAT, MAPK, and PI3K/Akt pathways after OSM or IL-31 cytokine stimulation. The pathogenic amino acid substitutions are located within the extracellular fibronectin type III-like (FNIII) domains, regions critical for receptor dimerization and function. OSM and IL-31 signaling have been implicated in keratinocyte cell proliferation, differentiation, apoptosis, and inflammation, but our OSMR data in individuals with FPLCA represent the first human germline mutations in this cytokine receptor complex and provide new insight into mechanisms of skin itching.
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36
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HUMPHREYS F, SPENCER J, MCLAREN K, TIDMAN M. An histological and ultrastructural study of the ‘dirty neck’ appearance in atopic eczema. Clin Exp Dermatol 2006. [DOI: 10.1111/j.1365-2230.1996.tb00004.x] [Citation(s) in RCA: 20] [Impact Index Per Article: 1.1] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/29/2022]
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37
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Abstract
Scleroderma is characterized by major clinical symptoms, but a number of unrelated disease may mimic these features more or less completely. Even scleroderma itself sometimes presents in an unusual manner. This article deals with uncommon presentations of true scleroderma and its variants and pseudo -scleroderma diseases.
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Affiliation(s)
- Uwe-Frithjof Haustein
- Department of Dermatology, Venerology and Allergology, University of Leipzig, D-04103 Leipzig, Germany.
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38
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Miura Y, Fujimoto N, Komatsu T, Tajima S, Kawada A, Saito T, Fujii N. Immunohistochemical study of chronological and photo-induced aging skins using the antibody raised against D-aspartyl residue-containing peptide. J Cutan Pathol 2004; 31:51-6. [PMID: 14675285 DOI: 10.1046/j.0303-6987.2004.0144.x] [Citation(s) in RCA: 8] [Impact Index Per Article: 0.4] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/20/2022]
Abstract
BACKGROUND Biologically uncommon D-aspartyl residues have been reported in the elderly tissues such as tooth, eye lens, aorta, and brain. We have previously prepared the antibody against D-aspartyl residue-containing peptide and found that it reacted with elastotic material of actinic elastosis. METHODS Immunoreactivity of the normal skins obtained from sun-exposed and sun-protected skins of varied ages with this antibody was studied. RESULTS In the sun-exposed skins, the antibody showed negative reaction with the skin specimens of young donors, whereas it reacted with elastotic materials of actinic elastosis of the elderly. In the sun-protected skins, the antibody recognized elastic fiber-like structures and inner layer of vessels found from the mid to lower dermis of old donors but showed no positive reaction to skin specimens of young donors. CONCLUSIONS The results suggest that the antibody is a potent marker for chronological and ultraviolet (UV)-induced skin aging. Unusual eosinophilic bodies seen in the superficial dermis in the sun-exposed area of the elderly skins were also immunoreactive with the antibody, suggesting that the eosinophilic bodies resulted from UV-induced skin damage.
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Affiliation(s)
- Yoshinori Miura
- Department of Dermatology, National Defense Medical College, 3-2 Namiki, Tokorozawa, Saitama 359-8513, Japan
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39
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Chang YT, Liu HN, Wang WJ, Lee DD, Tsai SF. A study of cytokeratin profiles in localized cutaneous amyloids. Arch Dermatol Res 2004; 296:83-8. [PMID: 15141317 DOI: 10.1007/s00403-004-0474-3] [Citation(s) in RCA: 30] [Impact Index Per Article: 1.4] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 09/26/2003] [Revised: 03/12/2004] [Accepted: 04/02/2004] [Indexed: 10/26/2022]
Abstract
The major component of localized cutaneous amyloids may be derived from cytokeratin (CK). However, the CK profiles of primary cutaneous amyloidosis (PCA) and secondary cutaneous amyloidosis (SCA) remain obscure. Paraffin-embedded sections of skin tissue from 64 patients with PCA, 111 with SCA and 3 with systemic amyloidosis were analyzed immunohistochemically using 12 different polyclonal or monoclonal anti-CK antibodies (34betaE12, MNF116, LP34, AE1/AE3, anti-CK1, CK5, CK6, CK7, CK10, CK14, CK16 and CK17). In addition, frozen skin tissues from 12 patients with PCA were analyzed for comparison with the paraffin-embedded tissue. In all 64 PCA paraffin sections, the amyloid deposits were immunopositive for anti-CK5 antibody and 34betaE12. In all 12 frozen sections of PCA, the amyloid deposits were immunopositive for anti-CK5 antibody, 34betaE12, MNF116 and LP34, and seven (58.3%), three (25%) and one (8.3%) were immunopositive for anti-CK1, CK14, and CK10 antibodies, respectively. In all SCA sections, the amyloid deposits were immunopositive for CK5 and 34betaE12. In addition, MNF116 immunolabeled amyloids of all sections from patients with basal cell carcinoma and trichoepithelioma, and MNF116 and LP34 immunolabeled amyloids of sections from patients with porokeratosis. Our results indicate that CK5 is the major CK present in the amyloid deposits of PCA and SCA, and "amyloid-K" is mainly derived from basal keratinocytes.
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Affiliation(s)
- Y T Chang
- Department of Dermatology, Taipei Veterans General Hospital and National Yang-Ming University, Shih-Pai, Taipei, Taiwan, ROC.
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40
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Apaydin R, Gürbüz Y, Bayramgürler D, Müezzinoglu B, Bilen N. Cytokeratin expression in lichen amyloidosus and macular amyloidosis. J Eur Acad Dermatol Venereol 2004; 18:305-9. [PMID: 15096140 DOI: 10.1111/j.1468-3083.2004.00905.x] [Citation(s) in RCA: 25] [Impact Index Per Article: 1.2] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/29/2022]
Abstract
AIM To understand the role of epidermal cells in the pathogenesis of lichen amyloidosus (LA) and macular amyloidosis (MA). METHODS We carried out immunohistochemical investigations on cytokeratins (CKs) in amyloid deposits in formalin-fixed and paraffin-embedded tissue specimens from eight persons with LA and 12 with MA. The primary antibodies of CK1-8 (AE3), CK10 (DEK-10), CK14 (LL002), CK17 (E3), CK18 (DC10), CK19 (KS19.1), CK5/6/18 (LP34) and CK8/18 (5D3) were used in the study. RESULTS In amyloid deposits, immunoreactivity with only two monoclonal antibodies (CK1-8 and CK5/6/18) was observed in 14 cases (eight LA and six MA), confirming the hypothesis that epidermal cells participate in amyloid formation of LA and MA. COMMENTS All of the CKs detected in amyloid deposits were basic type (type II). It seems plausible either that acidic CKs might be degraded faster than basic types in amyloidogenesis or that paraffin-embedded tissue specimens are less sensitive than frozen tissue sections. The results of our study suggest that when paraffin-embedded specimens are investigated by immunohistochemical methods, CK5 antibody is useful in the diagnosis of LA and MA.
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Affiliation(s)
- R Apaydin
- Department of Dermatology, Medical Faculty, Kocaeli University, 41 900 Kocaeli, Turkey
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41
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Abstract
Atopic dermatitis, nummular dermatitis, dyshidrosis, and melasma seem to be more common in Asians, whereas psoriasis and skin cancer are less common. In addition, there are less common skin conditions that are usually seen in Asians, including Mongolian spot, nevus of Ota, nevus of Ito, Kawasaki disease, primary cutaneous amyloidosis, Kikuchi-Fujimoto disease, and LCAI. Awareness of these less common cutaneous disorders can be helpful, especially for clinicians who work in areas with a large Asian population.
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Affiliation(s)
- Chai Sue Lee
- Department of Dermatology, Henry Ford Health System, 2799 West Grand Boulevard, Detroit, MI 48202, USA
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42
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Affiliation(s)
- Umit Tursen
- Department of Dermatology and of Pathology, Faculty of Medicine, Mersin University, Mersin, Turkey.
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43
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Ritter M, Nawab RA, Tannenbaum M, Hakky SI, Morgan MB. Localized amyloidosis of the glans penis: a case report and literature review. J Cutan Pathol 2003; 30:37-40. [PMID: 12534803 DOI: 10.1034/j.1600-0560.2003.300107.x] [Citation(s) in RCA: 22] [Impact Index Per Article: 1.0] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/23/2022]
Abstract
BACKGROUND Primary localized cutaneous amyloidosis is an uncommon lesion with a varied pathogenesis. METHODS We report the case of a 67-year-old-male discovered to have a localized amyloid lesion of the glans penis. RESULTS Biopsy of the lesion revealed dermal deposits of amorphous eosinophilic material which stained positive with Congo red and amyloid P protein. Additional stains, including kappa and lambda light chains, amyloid A, and transthyretin, were negative. The lesion has remained asymptomatic, with no evidence of systemic disease identified, and no further treatment has been necessary. CONCLUSIONS This is the sixth reported case of localized amyloidosis of the glans penis. Based on the clinical behavior and pathologic characteristics, this type of lesion is best classified as primary localized cutaneous amyloidosis, in the same family as the macular/lichenoid type lesions.
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Affiliation(s)
- Marylynn Ritter
- Department of Pathology, University of South Florida, Tampa, FL, USA.
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Furumoto H, Hashimoto Y, Muto M, Shimizu T, Nakamura K. Apolipoprotein E4 is associated with primary localized cutaneous amyloidosis. J Invest Dermatol 2002; 119:532-3. [PMID: 12190881 DOI: 10.1046/j.1523-1747.2002.18581.x] [Citation(s) in RCA: 7] [Impact Index Per Article: 0.3] [Reference Citation Analysis] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/20/2022]
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45
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Fujimoto N, Yajima M, Ohnishi Y, Tajima S, Ishibashi A, Hata Y, Enomoto U, Konohana I, Wachi H, Seyama Y. Advanced glycation end product-modified beta2-microglobulin is a component of amyloid fibrils of primary localized cutaneous nodular amyloidosis. J Invest Dermatol 2002; 118:479-84. [PMID: 11874487 DOI: 10.1046/j.0022-202x.2001.01695.x] [Citation(s) in RCA: 16] [Impact Index Per Article: 0.7] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/20/2022]
Abstract
Primary localized cutaneous nodular amyloidosis is a rare form of cutaneous amyloidosis. Amyloid fibrils in primary localized cutaneous nodular amyloidosis have been reported to be originated from immunoglobulin light chains. Immunohistochemical studies on the lesional skins of four patients with primary localized cutaneous nodular amyloidosis demonstrated that amyloid deposits of all cases showed a positive reaction with the antibodies for beta2-microglobulin and advanced glycation end products as well as immunoglobulin light chain (kappa or lambda). No beta2-microglobulin and advanced glycation end product immunoreactivity was found in the amyloid deposits of other primary localized cutaneous amyloidosis (lichen amyloidosis and macular amyloidosis). Double immunofluorescence study of the lesional skin of primary localized cutaneous nodular amyloidosis showed that anti-kappa light chain, anti-beta2-microglobulin and anti-advanced glycation end product antibodies mostly reacted with the same area of amyloid deposit. Amyloid proteins were sequentially extracted with distilled water from one case of primary localized cutaneous nodular amyloidosis and recovered in the five water-soluble fractions (fractions I-V). Immunoblot assay of amyloid fibril proteins demonstrated that immunoreactive polypeptides with anti-kappa light chain antibody (29 kDa) and with anti-beta2-microglobulin antibody (12 kDa) were detected in fractions I-V, whereas immunoreactive polypeptide with anti-advanced glycation end product antibody (12 kDa) was detected exclusively in fractions III-V but not in fractions I and II. Two-dimensional polyacrylamide gel electrophoresis revealed that 12 kDa polypeptide in fractions I and II was electrophoretically identical with authentic beta2-microglobulin and that beta2-microglobulin in fractions III-V was advanced glycation end product-modified beta2-microglobulin with more acidic pI value. These results indicate that beta2-microglobulin is another major component of amyloid fibrils in primary localized cutaneous nodular amyloidosis and that beta2-microglobulin in primary localized cutaneous nodular amyloidosis is partly subjected to the modification of advanced glycation end product.
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Affiliation(s)
- Norihiro Fujimoto
- Department of Dermatology, National Defense Medical College, Saitama, Japan
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46
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Abstract
BACKGROUND Primary cutaneous amyloidoses are rare in Western countries, but are relatively common in Taiwan. Anosacral cutaneous amyloidosis is a rare type of primary cutaneous amyloidoses, first reported in Japanese patients. PATIENTS/METHODS In the present study, we investigated the age of onset, sites of involvement, associated systemic diseases, and histopathological findings in 10 cases of anosacral cutaneous amyloidosis seen during the past 27 years. RESULTS In previous reports the aetiology of anosacral cutaneous amyloidosis was thought to be a senile change, but half of our patients developed the disease before the age of 60 years. Based on our histopathological findings, apoptosis may be the initial event causing amyloid deposition, although the precise mechanism causing apoptosis needs further investigation. Three patients were found to have diabetes mellitus, but any relationship to anosacral cutaneous amyloidosis is unclear. CONCLUSIONS No cases of this cutaneous disorder have been reported in the Western literature; there seems to be a racial difference accounting for the disease, although the precise factor is not clarified yet. The disease could easily be misdiagnosed as lichen simplex chronicus, postinflammatory hyperpigmentation or tinea cruris; therefore, a thorough history, a careful physical examination and a skin biopsy is needed to establish a firm diagnosis.
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Affiliation(s)
- W J Wang
- Department of Dermatology, Taipei Veterans General Hospital, Shih-Pai, Taipei 112 and National Yang-Ming University, Taipei, Taiwan, R.O.C
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Inoue K, Takahashi M, Hamamoto Y, Muto M, Ishihara T. An immunohistochemical study of cytokeratins in skin-limited amyloidosis. Amyloid 2000; 7:259-65. [PMID: 11132094 DOI: 10.3109/13506120009146439] [Citation(s) in RCA: 16] [Impact Index Per Article: 0.6] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Indexed: 11/13/2022]
Abstract
The frequency of amyloid deposits in cases of seborrheic keratosis was investigated In addition, the origin of amyloid protein(s) in lichen amyloidosis, macular amyloidosis and seborrheic keratosis was studied by immunohistochemical staining using a panel of anti-cytokeratin (CK) monoclonal antibodies. Amyloid deposits were found in 41 of 327 specimens (12.5%) from 301 cases of seborrheic keratosis. Amyloid deposits in seborrheic keratosis reacted with 6 of 12 CK antibodies and in lichen and macular amyloidosis (20 specimens) reacted with 5 of 12 CK antibodies. In seborrheic keratosis, antibody DE-K10 (labeling CK10) reacted with amyloid in 17 of 36 cases, antibody 34betaE12 (labeling CK1, 5, 10, 14) reacted in 33 of 39 cases, and antibody MNF116 (labeling CK5, 6, 8, 17) reacted in 32 of 35 cases. Among 20 specimens from lichen and macular amyloidosis, the three antibodies reacted with amyloid in the following rates: 1 with antibody DE-K10, all 20 with antibody 34betaE12, and 6 with antibody MNF116. These results suggest that amyloid deposits in seborrheic keratosis and lichen and macular amyloidosis may derive from epidermal cytokeratins.
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Affiliation(s)
- K Inoue
- Department of Dermatology, Yamaguchi University School of Medicine, Ube, Japan.
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Abstract
Four members of a white South African family, spanning four generations were diagnosed as suffering from familial primary lichen amyloidosis. All showed similar clinical features which included scaling papules on the lower legs and arms, and a pebbled, lichenified appearance of the skin on the back. The diagnosis was confirmed by light and electron microscopy. This is the eleventh report of familial primary cutaneous amyloidosis and the first in South Africa.
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Affiliation(s)
- S T Hartshorne
- Division of Dermatology, Department of Medicine, University of the Witwatersrand, Johannesburg, South Africa.
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Schepis C, Siragusa M, Gagliardi ME, Torre V, Cicciarello R, Albiero F, Cavallari V. Primary macular amyloidosis: an ultrastructural approach to diagnosis. Ultrastruct Pathol 1999; 23:279-84. [PMID: 10582265 DOI: 10.1080/019131299281428] [Citation(s) in RCA: 6] [Impact Index Per Article: 0.2] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 10/17/2022]
Abstract
Seven cases of primary macular amyloidosis were studied on skin biopsies. The Congo red stain was positive only in three cases, whereas the ultrastructural observation allowed for the detection of amyloid deposits in all biopsies. Fibrillary degeneration of basal keratynocytes was occasionally observed, and regressive changes of keratynocytes and dermal nerve bundles presumably related to the intensity of the scratch trauma were detected in one case. In six biopsies mast cell profiles exhibiting various degrees of degranulation were detected in the dermis. Melanosome aggregates were also observed consistently in dermal macrophages and occasionally in Schwann cells. A variable degree of structural alteration was observed in dermal unmyelinated nerve fibers. Even if the intimate mechanism of amyloid deposition was not explained by the ultrastructural study, this approach is a useful instrument in the differential diagnosis of cutaneous macular hyperpigmented lesions.
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Affiliation(s)
- C Schepis
- Unit of Dermatology, Oasi Institute (IRCCS), Troina, Italy
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50
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Abstract
Macular amyloidosis is the commonest form of primary localized cutaneous amyloidosis; its etiology remains unclear. Various incriminating factors include genetics, sunlight, and friction. Seventy-five patients with a clinical diagnosis of macular amyloidosis (confirmed by at least two observers) were enrolled in the study. A detailed history was elicited in relation to the etiological factors and followed by cutaneous examination. Skin biopsy was performed in 44 patients. Amyloid deposits were demonstrated in 21 (48%) of the biopsies. The female to male ratio was over 3:1. Patients with skin type V had a more delayed onset than those with skin types III and IV. Two patients gave histories of regularly subjecting their skin to friction. There was no correlation between the sites affected and the sites subjected to friction, hair style of the patient, or the use of cosmetics. Family history was present in 7 (9.3%) patients. A majority, 44 (58.7%) of the patients, had involvement of both sun-exposed and sun-protected sites. To conclude, there was no direct correlation between macular amyloidosis and atopy, sunlight, or friction to the skin in our patients. Multiple factors may play a collective role in the genesis of macular amyloidosis to variable degrees. These include racial, familial, and environmental factors, atopy, sunlight, friction, and female gender.
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Affiliation(s)
- V Eswaramoorthy
- Department of Dermatology, Venereology & Leprology, Postgraduate Institute of Medical Education and Research, Chandigarh, India
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