• DNA damage repair
• RNA methylation
• electromagnetic field (EMF)
• heme oxygenase (HO)
• retina

• Humans
• Cell Survival/radiation effects
• Adenosine/analogs & derivatives
• Adenosine/metabolism
• Electromagnetic Fields
• Heme Oxygenase-1/metabolism
• Heme Oxygenase-1/genetics
• Retinal Pigment Epithelium/metabolism
• Retinal Pigment Epithelium/cytology
• Retinal Pigment Epithelium/radiation effects
• Methylation
• DNA Repair
• Retinal Ganglion Cells/metabolism
• Retinal Ganglion Cells/radiation effects
• Cell Line
• 5-Methylcytosine/analogs & derivatives
• 5-Methylcytosine/metabolism
• DNA Damage
• Cell Proliferation
• Methyltransferases/metabolism
• Methyltransferases/genetics
• Retina/metabolism
• RNA/metabolism
• RNA/genetics
• RNA Methylation

• NIG/30/2023 Young Research Grant from University of Rzeszow

• Cancer
• Cell biology
• Molecular biology
• Molecular physiology

• R01 CA174869 NCI NIH HHS
• R01 CA236386 NCI NIH HHS
• R01 CA268179 NCI NIH HHS

• ASGPR1
• alcohol-related liver disease
• efferocytosis
• heme oxygenase-1
• iron metabolism
• red blood cells
• scavenging receptors

• FgCyp51
• Fusarium graminearum
• conidiation
• growth
• heme
• stress response
• virulence
• β-oxidation

• Fusarium/drug effects
• Fusarium/metabolism
• Fusarium/growth & development
• Fusarium/genetics
• Heme/biosynthesis
• Heme/metabolism
• Fungal Proteins/genetics
• Fungal Proteins/metabolism
• Stress, Physiological
• Oxidative Stress/drug effects
• Triazoles/pharmacology
• Gene Expression Regulation, Fungal/drug effects
• Fungicides, Industrial/pharmacology
• Ferrochelatase/metabolism
• Ferrochelatase/genetics

• CX(21)2037 Jiangsu Agricultural Science and Technology Innovation Fund
• CX(22)3072 Jiangsu Agricultural Science and Technology Innovation Fund
• BE2021361 Jiangsu provincial key research and development project
• Nos. 31672065 National Science Foundation of China

• heme
• heme oxygenase
• iron
• metalloprotein
• oxidation-reduction (redox)

• Animals
• Humans
• Circadian Rhythm/physiology
• Heme/metabolism
• Hemeproteins/metabolism
• Oxidation-Reduction
• Signal Transduction
• Intracellular Space/metabolism
• Cell Physiological Phenomena/physiology

• R01 HL137112 NHLBI NIH HHS

• Iron
• PCBP2
• mitochondria
• sideroflexin-3

• Humans
• Mitochondria/metabolism
• RNA-Binding Proteins/metabolism
• RNA-Binding Proteins/genetics
• Iron/metabolism
• Animals
• Receptors, Cell Surface/metabolism
• Mice
• Mitochondrial Precursor Protein Import Complex Proteins/metabolism
• HeLa Cells
• Mitochondrial Membrane Transport Proteins/metabolism
• Mitochondrial Membrane Transport Proteins/genetics
• RNA Splicing Factors/metabolism
• RNA Splicing Factors/genetics

• cell apoptosis and proliferation
• glutamine addiction
• light-emitting diode (LED 640 nm)
• photobiomodulation (PBM)

• Glutamine
• Low-Level Light Therapy
• Phosphatidylinositol 3-Kinases/metabolism
• Glucose Transporter Type 1
• RNA, Messenger/genetics
• Cell Proliferation

• HNJG-2022-0225 Research Project of Teaching Reform in General Colleges and Universities in Hunan Province

• Schizochytrium sp. extracted lipids
• alopecia
• antioxidant
• dermal papilla cells
• ferroptosis
• unsaturated fatty acids

• 2018YFA0902500 National Key Research and Development Project
• 2020YFD0901002 National Key Research and Development Program of China
• 2021A1515012557 Natural Science Foundation of Guangdong Province
• KCXST20221021111206015 Shenzhen Science and Technology Program
• 2021-928 Shenzhen Special Fund for Agricultural Development (Fishery) Agricultural high tech projects
• KCXFZ20201221173404012 2021 Shenzhen Special Fund for Agricultural Development (Fishery) Project "Research and Demonstration Application of Algae-based Alternative Protein Aquatic Feed" and Shenzhen Sustainable Development Science and Technology Project

• Biotic and abiotic stresses
• Ferroptisis
• Oxidative burst
• Plant defense
• Reactive nitrogen species
• Reactive oxygen species

• Iron
• Lignin
• Nitrogen
• Oxidative Stress
• Oxygen
• Plant Immunity/genetics
• Plants/genetics
• Polyamines
• Reactive Nitrogen Species
• Reactive Oxygen Species
• Stress, Physiological

The liver is the major target organ of continued alcohol consumption at risk and resulting alcoholic liver disease (ALD) is the most common liver disease worldwide. The underlying molecular mechanisms are still poorly understood despite decades of scientific effort limiting our abilities to identify those individuals who are at risk to develop the disease, to develop appropriate screening strategies and, in addition, to develop targeted therapeutic approaches. ALD is predestined for the newly evolving translational medicine, as conventional clinical and health care structures seem to be constrained to fully appreciate this disease. This concept paper aims at summarizing the 15 years translational experience at the Center of Alcohol Research in Heidelberg, namely based on the long-term prospective and detailed characterization of heavy drinkers with mortality data. In addition, novel experimental findings will be presented. A special focus will be the long-known hepatic iron accumulation, the somewhat overlooked role of the hematopoietic system and novel insights into iron sensing and the role of hepcidin. Our preliminary work indicates that enhanced red blood cell (RBC) turnover is critical for survival in ALD patients. RBC turnover is not primarily due to vitamin deficiency but rather to ethanol toxicity directly targeted to erythrocytes but also to the bone marrow stem cell compartment. These novel insights also help to explain long-known aspects of ALD such as mean corpuscular volume of erythrocytes (MCV) and elevated aspartate transaminase (GOT/AST) levels. This work also aims at identifying future projects, naming unresolved observations, and presenting novel hypothetical concepts still requiring future validation.

• Nrf2
• Parkinson’s disease
• heme oxygenase-1
• neuroprotection
• oxidative stress

Radiotherapy is routinely used for the treatment of head and neck squamous cell carcinoma (HNSCC). However, the therapeutic efficacy is usually reduced by acquired radioresistance and locoregional recurrence. In this study, The Cancer Genome Atlas (TCGA) analysis showed that radiotherapy upregulated the miR-182/96/183 cluster and that miR-182 was the most significantly upregulated. Overexpression of miR-182-5p enhanced the radiosensitivity of HNSCC cells by increasing intracellular reactive oxygen species (ROS) levels, suggesting that expression of the miR-182 family is beneficial for radiotherapy. By intersecting the gene targeting results from three microRNA target prediction databases, we noticed that sestrin2 (SESN2), a molecule resistant to oxidative stress, was involved in 91 genes predicted in all three databases to be directly recognized by miR-182-5p. Knockdown of SESN2 enhanced radiation-induced ROS and cytotoxicity in HNSCC cells. In addition, the radiation-induced expression of SESN2 was repressed by overexpression of miR-182-5p. Reciprocal expression of the miR-182-5p and SESN2 genes was also analyzed in the TCGA database, and a high expression of miR-182-5p combined with a low expression of SESN2 was associated with a better survival rate in patients receiving radiotherapy. Taken together, the current data suggest that miR-182-5p may regulate radiation-induced antioxidant effects and mediate the efficacy of radiotherapy.

• SESN2
• antioxidant
• head and neck squamous cell carcinoma
• miR-182-5p
• miR-182/96/183 cluster
• radioresistance

• Brown adipocyte
• Diabetes
• Fatty liver
• Leptin resistance
• Pericardial fat
• Stem cells
• hypertension

• anti-inflammatory response
• dolphin
• heme oxygenase
• immunology
• inflammation

• cell signalling
• growth factor signalling
• biomedical engineering

• Animals
• Blood Circulation/physiology
• Cells, Cultured
• Coculture Techniques
• Coronary Vessels
• Endothelial Cells/metabolism
• Gene Expression
• Heme Oxygenase-1/genetics
• Heme Oxygenase-1/metabolism
• Heme Oxygenase-1/physiology
• Humans
• Iron/metabolism
• Mesenteric Arteries
• Mice
• Muscle, Smooth, Vascular/metabolism
• Myocytes, Smooth Muscle/metabolism
• Placenta Growth Factor/metabolism
• RNA, Messenger/metabolism
• Reactive Oxygen Species/metabolism
• Shear Strength/physiology

• R01 HL084494 NHLBI NIH HHS
• R56 HL084494 NHLBI NIH HHS
• National Heart, Lung, and Blood Institute

The transcriptional repressor Rev-erbα is known to down-regulate fatty acid metabolism and gluconeogenesis gene expression. In animal models, disruption of Rev-erbα results in global changes in exercise performance, oxidative capacity, and blood glucose levels. However, the complete extent to which Rev-erbα-mediated transcriptional repression of metabolism impacts cell function remains unknown. We hypothesized that loss of Rev-erbα in a mouse embryonic fibroblast (MEF) model would result in global changes in metabolism. MEFs lacking Rev-erbα exhibited a hypermetabolic phenotype, demonstrating increased levels of glycolysis and oxidative phosphorylation. Rev-erbα deletion increased expression of hexokinase II, transketolase, and ribose-5-phosphate isomerase genes involved in glycolysis and the pentose phosphate pathway (PPP), and these effects were not mediated by the transcriptional activator BMAL1. Upregulation of oxidative phosphorylation was not accompanied by an increase in mitochondrial biogenesis or numbers. Rev-erbα repressed proliferation via glycolysis, but not the PPP. When treated with H₂O₂, cell viability was reduced in Rev-erbα knockout MEFs, accompanied by increased ratio of oxidized/reduced NADPH, suggesting that perturbation of the PPP reduces capacity to mount an antioxidant defense. These findings uncover novel mechanisms by which glycolysis and the PPP are modulated through Rev-erbα, and provide new insights into how Rev-erbα impacts proliferation.

• acute lung injury
• carbon monoxide
• heme
• heme oxygenase
• inflammation
• lung disease
• sepsis

• Animals
• Heme/metabolism
• Heme Oxygenase-1/metabolism
• Humans
• Inflammation/enzymology
• Inflammation/etiology
• Inflammation/metabolism
• Pneumonia/enzymology
• Pneumonia/etiology
• Pneumonia/metabolism
• Sepsis/etiology
• Sepsis/metabolism
• Systemic Inflammatory Response Syndrome/etiology
• Systemic Inflammatory Response Syndrome/metabolism

Heme-oxygenase is the enzyme responsible for degradation of endogenous iron protoporphyirin heme; it catalyzes the reaction’s rate-limiting step, resulting in the release of carbon monoxide (CO), ferrous ions, and biliverdin (BV), which is successively reduced in bilirubin (BR) by biliverdin reductase. Several studies have drawn attention to the controversial role of HO-1, the enzyme inducible isoform, pointing out its implications in cancer and other diseases development, but also underlining the importance of its antioxidant activity. The contribution of HO-1 in redox homeostasis leads to a relevant decrease in cells oxidative damage, which can be reconducted to its cytoprotective effects explicated alongside other endogenous mechanisms involving genes like TIGAR (TP53-induced glycolysis and apoptosis regulator), but also to the therapeutic functions of heme main transformation products, especially carbon monoxide (CO), which has been shown to be effective on GSH levels implementation sustaining body’s antioxidant response to oxidative stress. The aim of this review was to collect most of the knowledge on HO-1 from literature, analyzing different perspectives to try and put forward a hypothesis on revealing yet unknown HO-1-involved pathways that could be useful to promote development of new therapeutical strategies, and lay the foundation for further investigation to fully understand this important antioxidant system.

• GSH
• Nrf2
• TIGAR
• heme oxygenase

Ischemia-reperfusion injury (IRI) is a leading cause of acute kidney injury (AKI), which contributes to the development of chronic kidney disease (CKD). Renal IRI combines major events, including a strong inflammatory immune response leading to extensive cell injuries, necrosis and late interstitial fibrosis. Macrophages act as key players in IRI-induced AKI by polarizing into proinflammatory M1 and anti-inflammatory M2 phenotypes. Compelling evidence exists that the stress-responsive enzyme, heme oxygenase-1 (HO-1), mediates protection against renal IRI and modulates macrophage polarization by enhancing a M2 subset. Hereafter, we review the dual effect of macrophages in the pathogenesis of IRI-induced AKI and discuss the critical role of HO-1 expressing macrophages.

• AKI
• HO-1
• macrophage polarization
• renal IRI

• apoptosis
• autophagy
• carbon monoxide
• cell death
• ferroptosis
• heme oxygenase
• inflammasome
• inflammation
• necroptosis
• pyroptosis

• Ferritin
• Folic acid
• Pediatric chalazion
• Thyroid
• Vitamin B12
• Vitamin D

Paracoccidioides spp. are thermally dimorphic fungi that cause paracoccidioidomycosis and can affect both immunocompetent and immunocompromised individuals. The infection can lead to moderate or severe illness and death. Paracoccidioides spp. undergo micronutrients deprivation within the host, including iron. To overcome such cellular stress, this genus of fungi responds in multiple ways, such as the utilization of hemoglobin. A glycosylphosphatidylinositol (GPI)-anchored fungal receptor, Rbt5, has the primary role of acquiring the essential nutrient iron from hemoglobin. Conversely, it is not clear if additional proteins participate in the process of using hemoglobin by the fungus. Therefore, in order to investigate changes in the proteomic level of P. lutzii cell wall, we deprived the fungus of iron and then treated those cells with hemoglobin. Deprived iron cells were used as control. Next, we performed cell wall fractionation and the obtained proteins were submitted to nanoUPLC-MS^E. Protein expression levels of the cell wall F1 fraction of cells exposed to hemoglobin were compared with the protein expression of the cell wall F1 fraction of iron-deprived cells. Our results showed that P. lutzii exposure to hemoglobin increased the level of adhesins expression by the fungus, according to the proteomic data. We confirmed that the exposure of the fungus to hemoglobin increased its ability to adhere to macrophages by flow cytometry. In addition, we found that HSP30 of P. lutzii is a novel hemoglobin-binding protein and a possible heme oxygenase. In order to investigate the importance of HSP30 in the Paracoccidioides genus, we developed a Paracoccidioides brasiliensis knockdown strain of HSP30 via Agrobacterium tumefaciens-mediated transformation and demonstrated that silencing this gene decreases the ability of P. brasiliensis to use hemoglobin as a nutrient source. Additional studies are needed to establish HSP30 as a virulence factor, which can support the development of new therapeutic and/or diagnostic approaches.

• cell wall proteins
• molecular dynamics
• nutritional immunity

• Chalazion
• ferritin
• folic acid
• thyroid
• vitamin B12
• vitamin D

Normal pregnancy is associated with dramatic increases in uterine blood flow to facilitate the bidirectional maternal–fetal exchanges of respiratory gases and to provide sole nutrient support for fetal growth and survival. The mechanism(s) underlying pregnancy-associated uterine vasodilation remain incompletely understood, but this is associated with elevated estrogens, which stimulate specific estrogen receptor (ER)-dependent vasodilator production in the uterine artery (UA). The classical ERs (ERα and ERβ) and the plasma-bound G protein-coupled ER (GPR30/GPER) are expressed in UA endothelial cells and smooth muscle cells, mediating the vasodilatory effects of estrogens through genomic and/or nongenomic pathways that are likely epigenetically modified. The activation of these three ERs by estrogens enhances the endothelial production of nitric oxide (NO), which has been shown to play a key role in uterine vasodilation during pregnancy. However, the local blockade of NO biosynthesis only partially attenuates estrogen-induced and pregnancy-associated uterine vasodilation, suggesting that mechanisms other than NO exist to mediate uterine vasodilation. In this review, we summarize the literature on the role of NO in ER-mediated mechanisms controlling estrogen-induced and pregnancy-associated uterine vasodilation and our recent work on a “new” UA vasodilator hydrogen sulfide (H₂S) that has dramatically changed our view of how estrogens regulate uterine vasodilation in pregnancy.

• estrogen receptors
• estrogens
• hydrogen sulfide
• nitric oxide
• preeclampsia
• pregnancy
• uterine artery
• vasodilatation

• Rosacea
• ferritin
• pulsed dye laser

Exposure to particulate matter (PM) has been linked to pulmonary and cardiovascular dysfunctions, as well as skin diseases, etc. PM impairs the skin barrier functions and is also involved in the initiation or exacerbation of skin inflammation, which is linked to the activation of reactive oxygen species (ROS) pathways. Fullerene is a single C₆₀ molecule which has been reported to act as a good radical scavenger. However, its poor water solubility limits its biological applications. The glyco-modification of fullerenes increases their water solubility and anti-bacterial and anti-virus functions. However, it is still unclear whether it affects their anti-inflammatory function against PM-induced skin diseases. Hence, glycofullerenes were synthesized to investigate their effects on PM-exposed HaCaT human keratinocytes. Our results showed that glycofullerenes could reduce the rate of PM-induced apoptosis and ROS production, as well as decrease the expression of downstream mitogen-activated protein kinase and Akt pathways. Moreover, PM-induced increases in inflammatory-related signals, such as cyclooxygenase-2, heme oxygenase-1, and prostaglandin E2, were also suppressed by glycofullerenes. Notably, our results suggested that PM-induced impairment of skin barrier proteins, such as filaggrin, involucrin, repetin, and loricrin, could be reduced by pre-treatment with glycofullerenes. The results of this study indicate that glycofullerenes could be potential candidates for treatments against PM-induced skin diseases and that they exert their protective effects via ROS scavenging, anti-inflammation, and maintenance of the expression of barrier proteins.

• anti-inflammation
• antioxidant
• glycofullerenes
• human keratinocytes
• particulate matter
• reactive oxygen species

• HIF-1α
• PHD
• aging
• neovascularization
• skin

Autophagy is an essential cellular process that maintains balanced cell life. Restriction in autophagy may induce degenerative changes in humans. Natural or pathological aging of susceptible tissues has been linked with reduced autophagic activity. Skin photoaging is an example of such pathological condition caused by ambient solar UV radiation exposure. The UV-induced production of reaction oxygen species (ROS) has been linked to the promotion and progression of the photoaging process in exposed tissues. Accordingly, it has been suggested that autophagy is capable of delaying the skin photoaging process caused by solar ultraviolet (UV), although the underlying mechanism is still under debate. This review highlights several plausible mechanisms by which UV-induced ROS activates the cellular signaling pathways and modulates the autophagy. More specifically, the UV-mediated regulation of autophagy and age-related transcription factors is discussed to pinpoint the contribution of autophagy to antiphotoaging effects in the skin. The outcome of this review will provide insights into design intervention strategies for delaying the phenomenon of sunlight-induced photodamage, photoaging, and other aging-related chronic diseases based on factors that activate the autophagy process in the skin.

• 17-Oxo-DHA
• Docosahexaenoic acid
• Heme oxygenase-1
• Mouse skin
• Nrf2
• Omega-3 polyunsaturated fatty acids

• Animals
• Docosahexaenoic Acids/metabolism
• Docosahexaenoic Acids/pharmacology
• Epidermis/drug effects
• Epidermis/metabolism
• Female
• Gene Expression Regulation, Enzymologic/drug effects
• HEK293 Cells
• Heme Oxygenase-1/metabolism
• Humans
• Kelch-Like ECH-Associated Protein 1/chemistry
• Kelch-Like ECH-Associated Protein 1/metabolism
• Mice
• Molecular Docking Simulation
• NF-E2-Related Factor 2/metabolism
• Protein Conformation

Ferroptosis is an iron-dependent type of cell death distinct from apoptosis or necrosis characterized by accumulation of reactive oxygen species. The combination of siramesine, a lysosomotropic agent, and lapatinib, a dual tyrosine kinase inhibitor (TKI), synergistically induced cell death in breast cancer cells mediated by ferroptosis. In this study, we showed that this combination of siramesine and lapatinib induces synergistic cell death in glioma cell line U87 and lung adenocarcinoma cell line A549. This cell death was characterized by the increase in iron content, reactive oxygen species (ROS) production, and lipid peroxidation accumulation after 24 hours of treatment. Moreover, iron chelator DFO and ferrostatin-1, a ferroptosis inhibitor, significantly reduced cell death. The mechanism underlying the activation of the ferroptotic pathway involves lysosomal permeabilization and increase in reactive iron levels in these cells. In addition, the downregulation of heme oxygenase-1 (HO-1) protein occurred. Overexpression of HO-1 resulted in reduction of ROS and lipid peroxidation production and cell death. Furthermore, knocking down of HO-1 combined with siramesine treatment resulted in increased cell death. Finally, we found that the inhibition of the proteasome system rescued HO-1 expression levels. Our results suggest that the induction of ferroptosis by combining a lysosomotropic agent and a tyrosine kinase inhibitor is mediated by iron release from lysosomes and HO-1 degradation by the proteasome system.

Particulate matter (PM), a widespread air pollutant, consists of a complex mixture of solid and liquid particles suspended in air. Many diseases have been linked to PM exposure, which induces an imbalance in reactive oxygen species (ROS) generated in cells, and might result in skin diseases (such as aging and atopic dermatitis). New techniques involving nanomedicine and nano-delivery systems are being rapidly developed in the medicinal field. Fullerene, a kind of nanomaterial, acts as a super radical scavenger. Lower water solubility levels limit the bio-applications of fullerene. Hence, to improve the water solubility of fullerene, while retaining its radical scavenger functions, a fullerene derivative, fullerenol C₆₀(OH)₃₆, was synthesized, to examine its biofunctions in PM-exposed human keratinocyte (HaCaT) cells. The PM-induced increase in ROS levels and expression of phosphorylated mitogen-activated protein kinase and Akt could be inhibited via fullerenol pre-treatment. Furthermore, the expression of inflammation-related proteins, cyclooxygenase-2, heme oxygenase-1, and prostaglandin E2 was also suppressed. Fullerenol could preserve the impaired state of skin barrier proteins (filaggrin, involucrin, repetin, and loricrin), which was attributable to PM exposure. These results suggest that fullerenol could act against PM-induced cytotoxicity via ROS scavenging and anti-inflammatory mechanisms, and the maintenance of expression of barrier proteins, and is a potential candidate compound for the treatment of skin diseases.

• anti-inflammation
• antioxidant
• fullerenol
• human keratinocyte cell
• particulate matter
• reactive oxygen species

• Air Pollution/prevention & control
• Apoptosis/drug effects
• Cell Line
• Cities
• Filaggrin Proteins
• Fullerenes/analysis
• Fullerenes/chemistry
• Humans
• Inflammation/pathology
• Keratinocytes/drug effects
• Keratinocytes/metabolism
• Keratinocytes/ultrastructure
• Mitochondria/drug effects
• Mitochondria/metabolism
• Mitochondria/ultrastructure
• Mitogen-Activated Protein Kinases/metabolism
• Models, Biological
• Particulate Matter/toxicity
• Phosphorylation/drug effects
• Proto-Oncogene Proteins c-akt/metabolism
• Reactive Oxygen Species/metabolism
• Solubility
• Water/chemistry

• cisplatin
• heme oxygenase-1
• hyperthermic intraperitoneal chemotherapy

• Bilirubin
• oxidative stress
• preterm infant
• term infant

Utilizing the energy released from the nuclear fusion of deuterium with tritium (D-T) may be an important method of supplying energy in the future. The ionizing radiation emitted from nuclear fusion is a potential health risk to humans, including scientists who are currently performing nuclear fusion experiments and the employees of fusion nuclear plants, in the future. However, there have been few reports on the biological effects of fusion radiation. In the present study, using the High Intensity D-T Fusion Neutron Generator, the DNA damage and its regulation in normal human fibroblasts exposed to fusion radiation were investigated. Heme oxygenase 1 (HO-1), which is reported to induce anti-inflammatory activity, was upregulated in the irradiated cells. Pretreatment with the HO-1 inhibitor, protoporphyrin IX zinc (II), exacerbated double strand break formation following exposure to fusion radiation. The expression of cyclooxygenase-2 (COX-2) contributed to the upregulation of HO-1, as demonstrated by the result that its inhibitor, NS-398, inhibited the induction of HO-1 in irradiated cells. It was further clarified that the ataxia telangiectasia mutated DNA damage response was activated and it stimulated the phosphorylation of p38 mitogen-activated protein kinase, which was responsible for the upregulation of COX-2 and HO-1. These results provide novel information on fusion radiation-induced biological effects and potential targets for decreasing the associated health risks.

• Aryl hydrocarbon receptor (AhR)
• Dendritic cells (DCs)
• Particulate matter (PM)
• Polycyclic aromatic hydrocarbons (PAHs)
• Th17 cells

• Animals
• Basic Helix-Loop-Helix Transcription Factors/agonists
• Basic Helix-Loop-Helix Transcription Factors/deficiency
• Basic Helix-Loop-Helix Transcription Factors/genetics
• Basic Helix-Loop-Helix Transcription Factors/metabolism
• Coculture Techniques
• Cyclooxygenase 2/genetics
• Cyclooxygenase 2/metabolism
• Cytochrome P-450 CYP1A1/genetics
• Cytochrome P-450 CYP1A1/metabolism
• Cytochrome P-450 CYP1B1/genetics
• Cytochrome P-450 CYP1B1/metabolism
• Cytokines/genetics
• Cytokines/metabolism
• Dendritic Cells/drug effects
• Dendritic Cells/immunology
• Dendritic Cells/metabolism
• Hep G2 Cells
• Humans
• Immunity, Innate/drug effects
• Lymphocyte Activation/drug effects
• Macrophages/drug effects
• Macrophages/immunology
• Macrophages/metabolism
• Mice, Inbred C57BL
• Mice, Knockout
• Particulate Matter/toxicity
• Phenotype
• Receptors, Aryl Hydrocarbon/agonists
• Receptors, Aryl Hydrocarbon/deficiency
• Receptors, Aryl Hydrocarbon/genetics
• Receptors, Aryl Hydrocarbon/metabolism
• Repressor Proteins/genetics
• Repressor Proteins/metabolism
• Response Elements
• Signal Transduction/drug effects
• Th17 Cells/drug effects
• Th17 Cells/immunology
• Th17 Cells/metabolism

• P01 ES011269 NIEHS NIH HHS
• U54 HD079125 NICHD NIH HHS
• T32 GM099608 NIGMS NIH HHS
• R21 ES025560 NIEHS NIH HHS
• P30 ES023513 NIEHS NIH HHS
• R01 ES019898 NIEHS NIH HHS
• U54 OH007550 NIOSH CDC HHS

• Apoptosis
• Networking
• PPRH
• Pharmacogenomics
• Survivin
• Toxicity

• BACH1
• HO-1
• genetic variation
• pancreatic cancer
• survival

• Neuroprotection
• Parkinson’s disease
• microglia
• neurodegeneration
• oxidative stress

• HAND
• HIV-associated neurocognitive disorders
• HMOX1
• HO-1
• Heme oxygenase-1
• Immune activation
• Interferon
• Interferon-stimulated genes
• Neuroinflammation

• Adult
• Aged
• Antigens, CD/metabolism
• Brain/immunology
• Brain/metabolism
• Cohort Studies
• Dinucleotide Repeats/genetics
• Encephalitis, Viral/etiology
• Encephalitis, Viral/genetics
• Encephalitis, Viral/pathology
• Female
• Genetic Association Studies
• HIV Infections/complications
• HIV Infections/genetics
• Heme Oxygenase-1/genetics
• Humans
• Male
• Middle Aged
• Polymorphism, Genetic/genetics
• Promoter Regions, Genetic/genetics
• RNA, Messenger

• U24 MH100931 NIMH NIH HHS
• T32 NS007180 NINDS NIH HHS
• F30MH102120 NIMH NIH HHS
• U24 MH100928 NIMH NIH HHS
• R01 MH104134 NIMH NIH HHS
• R01MH101017 NIMH NIH HHS
• R01 MH095671 NIMH NIH HHS
• R01 MH101017 NIMH NIH HHS
• U24 MH100930 NIMH NIH HHS
• R01 MH111389 NIMH NIH HHS
• T32NS007180 NINDS NIH HHS
• R01MH095671 NIMH NIH HHS
• F30 MH102120 NIMH NIH HHS
• U24 MH100929 NIMH NIH HHS
• R01MH104134 NIMH NIH HHS
• U24 MH100925 NIMH NIH HHS
• National Institute of Mental Health
• National Institute of Neurological Disorders and Stroke

• Heme oxygenase
• atmosphere exposure chambers
• carbon monoxide
• carboxyhaemoglobin
• haemoglobin

A large number of terpenoids exhibit potential geroprotector and anti-cancer properties. Here, we studied whole transcriptomic effects of Abisil, the extract of fir (Abies sibirica) terpenes, on normal and cancer cell lines. We used early passaged and senescent none-immortalized fibroblasts as cellular aging models. It was revealed that in normal fibroblasts, terpenes induced genes of stress response, apoptosis regulation and tissue regeneration. The restoration of the expression level of some prolongevity genes after fir extract treatment was shown in old cells. In Caco-2 and AsPC-1 cancer cell lines, Abisil induced expression of both onco-suppressors (members of GADD45, DUSP, and DDIT gene families), and proto-oncogenes (c-Myc, c-Jun, EGR and others). Thus, the study demonstrates the potential anti-aging and anti-cancer effects of Abisil on senescent and cancer cell lines.

• Abies sibirica
• anti-aging effects
• anti-cancer effects
• plant extract
• terpenoids

• Ferroptosis
• Glutathione and glutathione peroxidases
• Iron homeostasis
• Lipid peroxidation
• Mitochondrial function
• Oxidative and nitrosative stress

Adipose derived stem cells (ADSCs) are acquired from abdominal liposuction yielding a thousand fold more stem cells per millilitre than those from bone marrow. A large research void exists as to whether ADSCs are capable of transdermal differentiation toward neuronal phenotypes. Previous studies have investigated the use of chemical cocktails with varying inconclusive results.

Human ADSCs were treated with a chemical stimulant, beta-mercaptoethanol, to direct them toward a neuronal-like lineage within 24 hours. Quantitative proteomics using iTRAQ was then performed to ascertain protein abundance differences between ADSCs, beta-mercaptoethanol treated ADSCs and a glioblastoma cell line.

The soluble proteome of ADSCs differentiated for 12 hours and 24 hours was significantly different from basal ADSCs and control cells, expressing a number of remodeling, neuroprotective and neuroproliferative proteins. However toward the later time point presented stress and shock related proteins were observed to be up regulated with a large down regulation of structural proteins. Cytokine profiles support a large cellular remodeling shift as well indicating cellular distress.

The earlier time point indicates an initiation of differentiation. At the latter time point there is a vast loss of cell population during treatment. At 24 hours drastically decreased cytokine profiles and overexpression of stress proteins reveal that exposure to beta-mercaptoethanol beyond 24 hours may not be suitable for clinical application as our results indicate that the cells are in trauma whilst producing neuronal-like morphologies. The shorter treatment time is promising, indicating a reducing agent has fast acting potential to initiate neuronal differentiation of ADSCs.

• Adipose
• Adult Stem Cells
• Cytokines
• Neuronal
• Proteomics

• Megalobrama amblycephala
• Nrf2
• Oral glucose administration
• Oxidative stress
• PI3K/Akt pathway

• Animals
• Antioxidants/metabolism
• Cyprinidae/metabolism
• Fish Proteins/genetics
• Fish Proteins/metabolism
• Glucose/metabolism
• Heme Oxygenase-1/genetics
• Heme Oxygenase-1/metabolism
• Liver/physiopathology
• NF-E2-Related Factor 2
• Oxidative Stress
• Phosphatidylinositol 3-Kinases/metabolism
• Proto-Oncogene Proteins c-akt
• Random Allocation
• Signal Transduction

• antiviral drug
• capsid
• carbon monoxide
• heme oxygenase-1
• herpes simplex virus
• pharmacological induction