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Aksoy M, Karaman M, Güller P, Güller U, Küfrevioğlu Öİ. In Vitro Inhibition Effect and Molecular Docking Study of Curcumin, Resveratrol, and Quercetin on Human Erythrocyte Glutathione Transferase. ACTA ACUST UNITED AC 2020. [DOI: 10.2174/1573408016666191231123544] [Citation(s) in RCA: 4] [Impact Index Per Article: 0.8] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 02/07/2023]
Abstract
Background:Chemotherapy has shown varying success rates in the treatment of metastatic cancer in the last 50 years. One of the problems in the use of many chemotherapeutic agents is to increase the expression of glutathione transferase enzyme (GST; EC 2.5.1.18). Therefore, the development of GST inhibitors is important to improve the effectiveness of antitumor drugs and to overcome multi-drug resistance.Introduction:Glutathione S-transferases (GSTs) are a major member of enzymes serving in the detoxification of exogenous and endogenous substances. But, it has been reported that GSTs are overexpressed in many tumour cells, and it has been found to be related to developing resistance to anticancer drugs by these cells. The development of GST inhibitors is important to increase the efficacy of antitumor drugs and overcome multi-drug resistance. The aim of our study was to investigate the effect of natural compounds including curcumin, resveratrol, and quercetin on GST enzyme activity. We also aimed to specify inhibition mechanism of the compounds on human erythrocytes GST (hGST) with in silico study.Method:GST was purified from human erythrocytes using affinity chromatography (glutathione agarose). The enzyme purity was checked with SDS-PAGE. After the inhibitory effect of the curcumin, quercetin, resveratrol was investigated. Lastly, inhibition mechanisms of these natural compound were identified with induced-fit docking method.Result:GST was purified with 19.31% yield from human erythrocytes. In inhibition studies, Ki values of curcumin, quercetin, resveratrol were determined as 0.0021 ± 0.0008, 0.0257 ± 0.0011, 663.3301 ± 0.0936 µM respectively. According to our results, all natural products showed the inhibition effect and the order of inhibition is as follows: curcumin ˃ quercetin ˃ resveratrol.Conclusion:According to the results of the in vitro and in silico studies, it can be said that curcumin, quercetin, resveratrol are the inhibitors of human erythrocyte GST. In conclusion, these observations may be of great importance for the potential use of these natural compounds as chemopreventive agents.
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Affiliation(s)
- Mine Aksoy
- Department of Chemistry, Faculty of Science, Atatürk University, 25240-Erzurum, Turkey
| | - Muhammet Karaman
- Department of Molecular Biology and Genetics, Faculty of Arts and Science, Kilis 7 Aralik University, 79000 Kilis, Turkey
| | - Pınar Güller
- Department of Chemistry, Faculty of Science, Atatürk University, 25240-Erzurum, Turkey
| | - Uğur Güller
- Department of Food Engineering, Faculty of Engineering, Igdir University, 76100-Igdir, Turkey
| | - Ö. İrfan Küfrevioğlu
- Department of Chemistry, Faculty of Science, Atatürk University, 25240-Erzurum, Turkey
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Deliu Z, Tamas T, Chowdhury J, Aqil M, Bassiony M, Radosevich JA. Expression of cross-tolerance to a wide range of conditions in a human lung cancer cell line after adaptation to nitric oxide. Tumour Biol 2017; 39:1010428317723778. [PMID: 28936924 DOI: 10.1177/1010428317723778] [Citation(s) in RCA: 2] [Impact Index Per Article: 0.3] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/15/2022] Open
Abstract
Previously, we have shown that A549, a human lung adenocarcinoma, can be adapted to nitric oxide (NO●). NO● is a nitrogen-based free radical that is synthesized by a family of enzymes known as nitric oxide synthases. NO● has been shown to be overexpressed in patient populations of different cancers. In addition, it has been observed that patients who express high levels of nitric oxide synthases tend to have poorer clinical outcomes than those with low levels of expression. The original cell line A549 (parent) and the adapted A549-HNO (high nitric oxide) cell line serve as a useful model system to investigate the role of NO● in tumor progression and prognosis. We have previously shown that the A549-HNO-adapted cells grow aggressively when compared to A549-parent cells. Furthermore, we have shown that the A549-HNO-adapted cells exhibit a higher percentage of cell viability when exposed to ultraviolet and X-ray radiation than the A549-parent cells. Cancer patients who develop resistance to one treatment often become resistant to other previously unencountered forms of treatment. This phenomenon is known as cross-tolerance. To determine whether NO● is a potential cross-tolerance causing agent, we have expanded our research by conducting parallel studies to a variety of other agents and conditions beyond radiation and ultraviolet exposure. We exposed both cell lines to varying levels of chemotherapeutic drugs (taxol and doxorubicin), temperature, pH, calcium chloride, cadmium chloride, copper chloride, sodium chloride, ferrous chloride, and sodium-R-lipoic acid. Our results show that the A549-HNO cells exhibit greater viability than the A549-parent cells when exposed to each of the various conditions. Therefore, NO● is one potential driving force that can make tumor cells exhibit cross-tolerance.
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Affiliation(s)
- Zane Deliu
- Department of Oral Medicine and Diagnostic Sciences, College of Dentistry, University of Illinois at Chicago, Chicago, IL, USA
| | - Timothy Tamas
- Department of Oral Medicine and Diagnostic Sciences, College of Dentistry, University of Illinois at Chicago, Chicago, IL, USA
| | - Juel Chowdhury
- Department of Oral Medicine and Diagnostic Sciences, College of Dentistry, University of Illinois at Chicago, Chicago, IL, USA
| | - Madeeha Aqil
- Department of Oral Medicine and Diagnostic Sciences, College of Dentistry, University of Illinois at Chicago, Chicago, IL, USA
| | - Maaly Bassiony
- Department of Oral Medicine and Diagnostic Sciences, College of Dentistry, University of Illinois at Chicago, Chicago, IL, USA
| | - James A Radosevich
- Department of Oral Medicine and Diagnostic Sciences, College of Dentistry, University of Illinois at Chicago, Chicago, IL, USA
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Aksoy M, Küfrevioglu I. Inhibition of human erythrocyte glutathione S-transferase by some flavonoid derivatives. TOXIN REV 2017. [DOI: 10.1080/15569543.2017.1345945] [Citation(s) in RCA: 6] [Impact Index Per Article: 0.8] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 12/12/2022]
Affiliation(s)
- Mine Aksoy
- Science Faculty, Chemistry Department, Ataturk Universitesi, Erzurum, Turkey
| | - Irfan Küfrevioglu
- Science Faculty, Chemistry Department, Ataturk Universitesi, Erzurum, Turkey
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McCormick Matthews LH, Noble F, Tod J, Jaynes E, Harris S, Primrose JN, Ottensmeier C, Thomas GJ, Underwood TJ. Systematic review and meta-analysis of immunohistochemical prognostic biomarkers in resected oesophageal adenocarcinoma. Br J Cancer 2015; 113:107-18. [PMID: 26110972 PMCID: PMC4647536 DOI: 10.1038/bjc.2015.179] [Citation(s) in RCA: 30] [Impact Index Per Article: 3.0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Grants] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 11/19/2014] [Revised: 02/22/2015] [Accepted: 04/29/2015] [Indexed: 02/07/2023] Open
Abstract
BACKGROUND Oesophageal adenocarcinoma (OAC) is one of the fastest rising malignancies with continued poor prognosis. Many studies have proposed novel biomarkers but, to date, no immunohistochemical markers of survival after oesophageal resection have entered clinical practice. Here, we systematically review and meta-analyse the published literature, to identify potential biomarkers. METHODS Relevant articles were identified via Ovid medline 1946-2013. For inclusion, studies had to conform to REporting recommendations for tumor MARKer (REMARK) prognostic study criteria. The primary end-point was a pooled hazard ratio (HR) and variance, summarising the effect of marker expression on prognosis. RESULTS A total of 3059 articles were identified. After exclusion of irrelevant titles and abstracts, 214 articles were reviewed in full. Nine molecules had been examined in more than one study (CD3, CD8, COX-2, EGFR, HER2, Ki67, LgR5, p53 and VEGF) and were meta-analysed. Markers with largest survival effects were COX-2 (HR=2.47, confidence interval (CI)=1.15-3.79), CD3 (HR=0.51, 95% CI=0.32-0.70), CD8 (HR=0.55, CI=0.31-0.80) and EGFR (HR=1.65, 95% CI=1.14-2.16). DISCUSSION Current methods have not delivered clinically useful molecular prognostic biomarkers in OAC. We have highlighted the paucity of good-quality robust studies in this field. A genome-to-protein approach would be better suited for the development and subsequent validation of biomarkers. Large collaborative projects with standardised methodology will be required to generate clinically useful biomarkers.
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Affiliation(s)
- L H McCormick Matthews
- Cancer Sciences Unit, Faculty of Medicine, University of Southampton, Somers Cancer Research Building, MP824, Southampton SO16 6YD, UK
| | - F Noble
- Cancer Sciences Unit, Faculty of Medicine, University of Southampton, Somers Cancer Research Building, MP824, Southampton SO16 6YD, UK
- Department of Surgery, University Hospital Southampton NHS Foundation Trust, Southampton SO16 6YD, UK
| | - J Tod
- Cancer Sciences Unit, Faculty of Medicine, University of Southampton, Somers Cancer Research Building, MP824, Southampton SO16 6YD, UK
| | - E Jaynes
- Department of Cellular Pathology, University Hospital Southampton NHS Foundation Trust, Southampton SO16 6YD, UK
| | - S Harris
- Public Health Sciences and Medical Statistics, Faculty of Medicine, University of Southampton, Southampton SO16 6YD, UK
| | - J N Primrose
- Cancer Sciences Unit, Faculty of Medicine, University of Southampton, Somers Cancer Research Building, MP824, Southampton SO16 6YD, UK
- Department of Surgery, University Hospital Southampton NHS Foundation Trust, Southampton SO16 6YD, UK
| | - C Ottensmeier
- Cancer Sciences Unit, Faculty of Medicine, University of Southampton, Somers Cancer Research Building, MP824, Southampton SO16 6YD, UK
- National Institute for Health Research, Experimental Cancer Medicine Centre, Southampton SO16 6YD, UK
| | - G J Thomas
- Cancer Sciences Unit, Faculty of Medicine, University of Southampton, Somers Cancer Research Building, MP824, Southampton SO16 6YD, UK
- Department of Cellular Pathology, University Hospital Southampton NHS Foundation Trust, Southampton SO16 6YD, UK
| | - T J Underwood
- Cancer Sciences Unit, Faculty of Medicine, University of Southampton, Somers Cancer Research Building, MP824, Southampton SO16 6YD, UK
- Department of Surgery, University Hospital Southampton NHS Foundation Trust, Southampton SO16 6YD, UK
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Kordi-Tamandani DM, Mojahed A, Sahranavard R, Najafi M. Association of Glutathione S-Transferase Gene Methylation with Risk of Schizophrenia in an Iranian Population. Pharmacology 2014; 94:179-82. [DOI: 10.1159/000368083] [Citation(s) in RCA: 9] [Impact Index Per Article: 0.8] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 06/10/2014] [Accepted: 09/03/2014] [Indexed: 11/19/2022]
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A Relationship Between Replication Protein A and Occurrence and Prognosis of Esophageal Carcinoma. Cell Biochem Biophys 2013; 67:175-80. [DOI: 10.1007/s12013-013-9530-y] [Citation(s) in RCA: 27] [Impact Index Per Article: 2.3] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/26/2022]
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Song P, Bao H, Yu Y, Xue Y, Yun D, Zhang Y, He Y, Liu Y, Liu Q, Lu H, Fan H, Luo J, Yang P, Chen X. Comprehensive profiling of metastasis-related proteins in paired hepatocellular carcinoma cells with different metastasis potentials. Proteomics Clin Appl 2012; 3:841-52. [PMID: 21136991 DOI: 10.1002/prca.200780131] [Citation(s) in RCA: 11] [Impact Index Per Article: 0.8] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 12/20/2022]
Abstract
Precise and comprehensive identifications of the proteins associated with metastasis are critical for early diagnosis and therapeutic intervention of hepatocellular carcinoma (HCC). Therefore, we investigated the proteomic differences between a pair of HCC cell lines, originating from the same progenitor, with different metastasis potential using amino acid-coded mass tagging-based LC-MS/MS quantitative proteomic approach. Totally the relative abundance of 336 proteins in these cell lines were quantified, in which 121 proteins were upregulated by >30%, and 64 proteins were downregulated by >23% in the cells with high metastasis potential. Further validation studies by Western blotting in a series of HCC cell types with progressively increasing trend of metastasis showed that peroxiredoxin 4, HSP90β and HSP27 were positively correlated with increasing metastasis while prohibitin was negatively correlated with metastasis potential. These validation results were also consistent with that obtained from comparative analysis of clinic tissues samples. Function annotations of differentially expressed HCC proteome suggested that the emergence and development of high metastasis involved the dysregulation of cell migration, cell cycle and membrane traffics. Together our results revealed a much more comprehensive profile than that from 2-DE-based method and provided more global insights into the mechanisms of HCC metastasis and potential markers for clinical diagnosis.
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Affiliation(s)
- Peiming Song
- College of Life Science and Biotechnology, Shanghai Jiaotong University, Shanghai, P. R. China; Institutes of Biomedical Science, Fudan University, Shanghai, P. R. China
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Zhao Y, Wang F, Shan S, Zhao Y, Qiu X, Li X, Jiao F, Wang J, Du Y. Genetic polymorphism of p53, but not GSTP1, is association with susceptibility to esophageal cancer risk - a meta-analysis. Int J Med Sci 2010; 7:300-8. [PMID: 20827430 PMCID: PMC2934729 DOI: 10.7150/ijms.7.300] [Citation(s) in RCA: 16] [Impact Index Per Article: 1.1] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Received: 07/25/2010] [Accepted: 08/31/2010] [Indexed: 12/30/2022] Open
Abstract
A number of studies have evaluated two functional polymorphisms on p53 Arg72Pro and GSTP1 Ile105Val, in relation to esophageal cancer susceptibility. However, the results remain conflicting rather than conclusive. This meta-analysis on 2919 cases and 4074 controls for p53 Arg72Pro and 1885 cases and 2194 controls for GSTP1 Ile105Val from 13 published case-control studies showed that no significant general main effects for GSTP1 Ile105Val on esophageal cancer risk. However, we found that the p53 Arg72Pro was associated with an increased risk of esophageal cancer ((Pro/Arg +Pro/Pro) versus Arg/Arg: OR=1.20, 95%CI=1.06-1.36) without any between-study heterogeneity. In the stratified analysis by ethnicity, we found that the increased esophageal cancer risk associated with p53 Arg72Pro polymorphism was more evident in Asian group ((Pro/Arg +Pro/Pro) versus Arg/Arg: OR=1.35, 95%CI=1.14-1.60, P=0.09 for heterogeneity test), although we still failed to find any significant association between GSTP1 Ile105Val polymorphism and esophageal cancer risk in different ethnicity. These results suggest that p53 Arg72Pro polymorphism, but not GSTP1 Ile105Val, may contribute to esophageal cancer development, especially in Asian. Additional well-designed large studies were required for the validation of this association.
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Affiliation(s)
- Yaping Zhao
- Department of Laboratory, The 82th Hospital of the People's Liberation Army, Huaian,China
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Paradise WA, Vesper BJ, Goel A, Waltonen JD, Altman KW, Haines GK, Radosevich JA. Nitric oxide: perspectives and emerging studies of a well known cytotoxin. Int J Mol Sci 2010; 11:2715-45. [PMID: 20717533 PMCID: PMC2920563 DOI: 10.3390/ijms11072715] [Citation(s) in RCA: 32] [Impact Index Per Article: 2.1] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 05/26/2010] [Revised: 06/17/2010] [Accepted: 07/13/2010] [Indexed: 12/19/2022] Open
Abstract
The free radical nitric oxide (NO•) is known to play a dual role in human physiology and pathophysiology. At low levels, NO• can protect cells; however, at higher levels, NO• is a known cytotoxin, having been implicated in tumor angiogenesis and progression. While the majority of research devoted to understanding the role of NO• in cancer has to date been tissue-specific, we herein review underlying commonalities of NO• which may well exist among tumors arising from a variety of different sites. We also discuss the role of NO• in human physiology and pathophysiology, including the very important relationship between NO• and the glutathione-transferases, a class of protective enzymes involved in cellular protection. The emerging role of NO• in three main areas of epigenetics—DNA methylation, microRNAs, and histone modifications—is then discussed. Finally, we describe the recent development of a model cell line system in which human tumor cell lines were adapted to high NO• (HNO) levels. We anticipate that these HNO cell lines will serve as a useful tool in the ongoing efforts to better understand the role of NO• in cancer.
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Affiliation(s)
- William A. Paradise
- Center for Molecular Biology of Oral Diseases, College of Dentistry, University of Illinois at Chicago, Chicago, IL 60612, USA; E-Mails: (W.A.P.); (B.J.V.)
- Department of Jesse Brown, Veterans Administration Medical Center, Chicago, IL 60612, USA
| | - Benjamin J. Vesper
- Center for Molecular Biology of Oral Diseases, College of Dentistry, University of Illinois at Chicago, Chicago, IL 60612, USA; E-Mails: (W.A.P.); (B.J.V.)
- Department of Jesse Brown, Veterans Administration Medical Center, Chicago, IL 60612, USA
| | - Ajay Goel
- Division of Gastroenterology, Department of Internal Medicine, Charles A. Sammons Cancer Center and Baylor Research Institute, Baylor University Medical Center, Dallas, TX 75246, USA; E-Mail:
| | - Joshua D. Waltonen
- Department of Otolaryngology, Wake Forest University, Winston-Salem, NC 27157, USA; E-Mail:
| | | | - G. Kenneth Haines
- Department of Pathology, Yale University School of Medicine, New Haven, CT 06510, USA; E-Mail:
| | - James A. Radosevich
- Center for Molecular Biology of Oral Diseases, College of Dentistry, University of Illinois at Chicago, Chicago, IL 60612, USA; E-Mails: (W.A.P.); (B.J.V.)
- Department of Jesse Brown, Veterans Administration Medical Center, Chicago, IL 60612, USA
- Author to whom correspondence should be addressed; E-Mail:
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Decreased expression of GST pi is correlated with a poor prognosis in human esophageal squamous carcinoma. BMC Cancer 2010; 10:352. [PMID: 20602752 PMCID: PMC2909209 DOI: 10.1186/1471-2407-10-352] [Citation(s) in RCA: 15] [Impact Index Per Article: 1.0] [Reference Citation Analysis] [Abstract] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 11/27/2009] [Accepted: 07/05/2010] [Indexed: 11/25/2022] Open
Abstract
Background Glutathione S-transferase pi (GST pi) is a subgroup of GST family, which provides cellular protection against free radical and carcinogenic compounds due to its detoxifying function. Expression patterns of GST pi have been studied in several carcinomas and its down-regulation was implicated to be involved in malignant transformation in patients with Barrett's esophagus. However, neither the exact role of GST pi in the pathogenesis nor its prognostic impact in squamous esophageal carcinoma is fully characterized. Methods Immunohistochemistry was used to investigate GST pi expression on 153 archival squamous esophageal carcinoma specimens with a GST pi monoclonal antibody. Statistic analyses were performed to explore its association with clinicopathological factors and clinical outcome. Results The GST pi expression was greatly reduced in tissues of esophageal carcinomas compared to adjacent normal tissues and residual benign tissues. Absent of GST pi protein expression in cytoplasm, nuclear and cytoplasm/nucleus was found in 51%, 64.7% and 48% of all the carcinoma cases, respectively. GST pi deficiency in cytoplasm, nucleus and cytoplasm/nucleus was significantly correlated to poor differentiation (p < 0.001, p < 0.001 and p < 0.001, respectively). UICC stage and T stage were found significantly correlated to negative expression of GST pi in cytoplasm (p < 0.001 and p = 0.004, respectively) and cytoplasm/nucleus (p = 0.017 and p = 0.031, respectively). In univariate analysis, absent of GST pi protein expression in cytoplasm, nucleus and cytoplasm/nucleus was significantly associated with a shorter overall survival (p < 0.001, p < 0.001 and p < 0.001, respectively), whereas only GST pi cytoplasmic staining retained an independent prognostic significance (p < 0.001) in multivariate analysis. Conclusions Our results show that GST pi expression is down regulated in the squamous esophageal carcinoma, and that the lack of GST pi expression is associated with poor prognosis. Therefore, deficiency of GST pi protein expression may be an important mechanism involved in the carcinogenesis and progression of the squamous esophageal carcinoma, and the underlying mechanisms leading to decreased GST pi expression deserve further investigation.
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Gao P, Yang X, Xue YW, Zhang XF, Wang Y, Liu WJ, Wu XJ. Promoter methylation of glutathione S-transferase pi1 and multidrug resistance gene 1 in bronchioloalveolar carcinoma and its correlation with DNA methyltransferase 1 expression. Cancer 2009; 115:3222-32. [PMID: 19484794 DOI: 10.1002/cncr.24369] [Citation(s) in RCA: 22] [Impact Index Per Article: 1.4] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 12/21/2022]
Abstract
BACKGROUND The presence of glutathione S-transferase (GST) pi1 (GSTP1) or multidrug resistance gene 1 (MDR1) promoter methylation in lung cancer was studied for the first time to the authors' knowledge; and, to date, the clinical significance of methylation is not clear. The objective of the current study was to determine the promoter methylation status of GSTP1 and MDR1, which encode GST-pi and P-glycoprotein (Pgp), respectively, in patients with bronchioloalveolar carcinoma (BAC) and to investigate whether methyltransferase 1 (DNMT1)-mediated GSTP1 or MDR1 methylation are responsible for disease progression and prognosis in patients with BAC. METHODS Protein expression levels of DNTM1, GST-pi, and Pgp were determined by immunohistochemistry in samples from 36 patients with BAC. Promoter methylation status of the GSTP1 and MDR1 genes was determined by using methylation-specific polymerase chain reaction analysis. RESULTS The results demonstrated a significant correlation between the methylation of the GSTP1 or MDR1 promoters and negative expression of their respective proteins in BAC (P < .05). A significant correlation also was demonstrated between GSTP1 methylation and recurrence-free and overall survival of patients with BAC. DNMT1 protein expression levels were correlated with GSTP1 promoter methylation and patient prognosis (P < .05). However, no correlation was observed between DNMT1 expression and MDR1 methylation. CONCLUSIONS GSTP1 promoter methylation mediated by DNMT1 may promote BAC progression and could serve as a poor prognostic indicator for patients with this disease. DNMT1 protein expression also may be considered as a prognostic indicator. Methylation of the MDR1 promoter may be mediated through pathways other than DNMT1 in BAC and does not appear to be associated with disease progression or patient prognosis.
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Affiliation(s)
- Peng Gao
- Department of Pathology, School of Medicine, Shandong University, Jinan, People's Republic of China.
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Appiah-Opong R, Commandeur JNM, Istyastono E, Bogaards JJ, Vermeulen NPE. Inhibition of human glutathioneS-transferases by curcumin and analogues. Xenobiotica 2009; 39:302-11. [DOI: 10.1080/00498250802702316] [Citation(s) in RCA: 19] [Impact Index Per Article: 1.2] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 10/20/2022]
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Rasmi Y, Allameh A, Nasseri-Moghaddam S, Gill P, Moghaddam MF, Hedayati M. Comparison of glutathione S-transferase-Pi expression at mRNA levels in oesophageal mucosa using RT-PCR-ELISA in individuals with reflux diseases, adenocarcinoma and squamous cell carcinoma. Clin Biochem 2006; 39:997-1001. [PMID: 16979613 DOI: 10.1016/j.clinbiochem.2006.06.010] [Citation(s) in RCA: 5] [Impact Index Per Article: 0.3] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 03/29/2006] [Revised: 06/19/2006] [Accepted: 06/21/2006] [Indexed: 11/19/2022]
Abstract
OBJECTIVES To develop a RT-PCR technique coupled with Enzyme Linked Immunosobant Assay (ELISA) i.e. RT-PCR-ELISA for measurement of class-Pi glutathione S-transferase (GST-P)-specific mRNA in esophageal diseases. METHODS In this study, 66 esophageal tissue biopsies diagnosed as non-erosive reflux disease (NERD), gastroesophageal reflux disease (GERD), adenocarcinoma (ADC), and squamous cell carcinoma (SCC) were used. Standardization of the RT-PCR-ELISA was carried out using specific GST-Pi and beta-actin primers, biotin labeled probe, DIG-labeling RT-PCR and anti-DIG-HRP conjugate. RESULTS The results of RT-PCR-ELISA based on OD ratio of GST-Pi mRNA/beta-actin showed that there was no significant difference in GST-Pi expression in normal, NERD and GERD samples. Overexpression of GST-Pi in malignant tissues (ADC and SCC) was distinguishable. The OD ratio of GST-Pi mRNA expression to beta-actin mRNA was 1.17+/-0.13 and 1.3+/-0.13 in ADC and SCC samples, respectively, which is significantly higher (P<0.05) than matching control (0.78+/-0.06 and 0.85+/-0.07). CONCLUSIONS RT-PCR-ELISA showed that GST-Pi expression was not altered in GERD and NERD esophagus, whereas, in ADC and SCC samples, it was significantly higher (P<0.05) as compared to inflamed and normal tissues.
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Affiliation(s)
- Y Rasmi
- Department of Clinical Biochemistry, Faculty of Medical Sciences, Tarbiat Modarres University, P. O. Box 14115-331, Tehran, Iran
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Niu ZS, Wang M. Expression of c-erbB-2 and glutathione S-transferase-pi in hepatocellular carcinoma and its adjacent tissue. World J Gastroenterol 2005; 11:4404-4408. [PMID: 16038042 PMCID: PMC4434670 DOI: 10.3748/wjg.v11.i28.4404] [Citation(s) in RCA: 13] [Impact Index Per Article: 0.7] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Download PDF] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Received: 09/22/2004] [Revised: 11/13/2004] [Accepted: 11/19/2004] [Indexed: 02/06/2023] Open
Abstract
AIM To investigate the possible role of c-erbB-2 and glutathione S-transferase (GST-Pi) in primary hepatocellular carcinogenesis and the relationship between liver hype-rplastic nodule (LHN), liver cirrhosis (LC), and hepatocellular carcinoma (HCC). METHODS The expression of c-erbB-2 and GST-Pi was detected immunohistochemically in 41 tissue specimens of HCC and 77 specimens of its adjacent tissue. RESULTS The positive expression of c-erbB-2 in LHN (28.6%) was significantly higher than that in LC (0%) (P = 0.032<0.05), but no significant difference was seen between HCC and LHN or LC (P>0.05, chi2= 0.002, 3.447). The positive expression of GST-Pi in HCC (89.6%) or LHN (71.1%) was significantly higher than that in LC (22.9%, P<0.001, chi2= 49.91, 16.96). There was a significant difference between HCC and LHN (P<0.05, chi2= 6.353). CONCLUSION The c-erbB-2 expression is an early event in the pathogenesis of HCC. GST-Pi may be a marker enzyme for immunohistochemical detection of human HCC and its preneoplastic lesions. LHN seems to be a preneoplastic lesion related to hepatocarcinogenesis.
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Affiliation(s)
- Zhao-Shan Niu
- Department of Pathology, Medical College of Qingdao University, 38 Dengzhou Road, Qingdao 266021, Shandong Province, China.
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