title: Expression of glutaredoxin in human coronary arteries: its potential role in antioxidant protection against atherosclerosis.
abstract: Oxidative stress is considered an important factor in atherogenesis. Mammalian cells have a complex network of antioxidants such as catalase, superoxide dismutase, and glutathione peroxidase. However, the mechanisms that regulate the cellular redox state in the vessel wall remain unclear. Recent study has shown that thioredoxin, a thiol-disulfide oxidoreductase, is expressed in atherosclerotic plaques of human carotid arteries. In this study, we investigated the localization and expressional change of glutaredoxin and thioredoxin, two important members of the thiol-disulfide oxidoreductases, in autopsy samples of human coronary arteries. In nonatherosclerotic coronary arteries, glutaredoxin was expressed in endothelial cells, in fibroblasts of the adventitia, and most intensely in medial smooth muscle cells. Interestingly, in atherosclerotic lesions such as hypercellular lesions, the infiltrating macrophages highly expressed glutaredoxin. The expressional pattern of thioredoxin was quite similar to that of glutaredoxin. Western blot analysis demonstrated that hydrogen peroxide stimulated the expression of glutaredoxin in a time- and dose-dependent manner in cultured human coronary artery smooth muscle cells. Fluorescence microtopography with dihydroethidium demonstrated that the generation of reactive oxygen species was associated with the expression of glutaredoxin. These results suggest the possible involvement of thiol-disulfide oxidoreductases in antioxidant protection in human coronary arteries.
authors.affiliation: Division of Cardiovascular and Respiratory Medicine, Departments of Internal Medicine, Kobe University Graduate School of Medicine, Kobe, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Okuda
authors.forename: N
authors.initials: N
authors.lastname: Inoue
authors.forename: H
authors.initials: H
authors.lastname: Azumi
authors.forename: T
authors.initials: T
authors.lastname: Seno
authors.forename: Y
authors.initials: Y
authors.lastname: Sumi
authors.lastname: Hirata Ki
authors.forename: S
authors.initials: S
authors.lastname: Kawashima
authors.forename: Y
authors.initials: Y
authors.lastname: Hayashi
authors.forename: H
authors.initials: H
authors.lastname: Itoh
authors.forename: J
authors.initials: J
authors.lastname: Yodoi
authors.forename: M
authors.initials: M
authors.lastname: Yokoyama
mesh_terms: D000368:Aged; D002478:Cells, Cultured; D003324:Coronary Artery Disease / Q000378:metabolism*; D003331:Coronary Vessels / Q000166:cytology / Q000378:metabolism*; D004730:Endothelium, Vascular / Q000378:metabolism; D005347:Fibroblasts / Q000378:metabolism; D054477:Glutaredoxins; D006801:Humans; D006861:Hydrogen Peroxide / Q000494:pharmacology; D007150:Immunohistochemistry; D008264:Macrophages / Q000378:metabolism; D008856:Microscopy, Fluorescence; D008875:Middle Aged; D009131:Muscle, Smooth, Vascular / Q000187:drug effects / Q000378:metabolism; D018384:Oxidative Stress; D010088:Oxidoreductases / Q000502:physiology; D011506:Proteins / Q000276:immunology / Q000502:physiology*; D017382:Reactive Oxygen Species / Q000378:metabolism; D013879:Thioredoxins / Q000276:immunology / Q000378:metabolism
chemical_list: D054477:Glutaredoxins; D011506:Proteins; D017382:Reactive Oxygen Species; D013879:Thioredoxins; D006861:Hydrogen Peroxide; D010088:Oxidoreductases