HEME OXYGENASE IS THE MAJOR 32-KDA STRESS PROTEIN-INDUCED IN HUMAN-SKIN FIBROBLASTS BY UVA RADIATION, HYDROGEN-PEROXIDE, AND SODIUM ARSENITE
HEME OXYGENASE IS THE MAJOR 32-KDA STRESS PROTEIN-INDUCED IN HUMAN-SKIN FIBROBLASTS BY UVA RADIATION, HYDROGEN-PEROXIDE, AND SODIUM ARSENITE
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DOI：
10.1073/pnas.86.1.99
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发表时间：
1989-01-01
影响因子：
11.1
通讯作者：
TYRRELL, RM
中科院分区：
文献类型：
--
作者：
KEYSE, SM;TYRRELL, RM
我们已经证明UVA(320-380 nm)辐射、过氧化氢和亚砷酸钠诱导了一种应激蛋白.apprxeq。32 kDa的人皮肤成纤维细胞。从亚砷酸盐诱导的mRNA群体中合成和克隆cDNA，现在已经使我们能够明确地确定32 kDa的蛋白质是血红素加氧酶。通过信使核糖核酸分析表明，在培养的人皮肤成纤维细胞中，经UVA辐射、过氧化氢、氯化镉、碘乙酰胺和甲萘二酮也能诱导血红素加氧酶基因的表达。已知的血红素分解代谢物的抗氧化特性，以及观察到在一个不参与血红蛋白分解的器官的细胞中高水平诱导该酶，有力地支持了以下假设：血红素加氧酶的诱导可能是对氧化应激的一般反应，并构成了对抗氧化损伤的重要细胞防御机制。
We have shown that UVA (320-380 nm) radiation, hydrogen peroxide, and sodium arsenite induce a stress protein of .apprxeq. 32 kDa in human skin fibroblasts. The synthesis and cloning of cDNA from arsenite-induced mRNA populations have now allowed us to unequivocally identify the 32-kDa protein as heme oxygenase. By mRNA analysis we have shown that the heme oxygenase gene is also induced in cultured human skin fibroblasts by UVA radiation, hydrogen peroxide, cadmium chloride, iodoacetamide, and menadione. The known antioxidant properties of heme catabolites taken together with the observation of a high level of induction of the enzyme in cells from an organ not involved in hemoglobin breakdown strongly supports the proposal that the induction of heme oxygenase may be a general response to oxidant stress and constitutes an important cellular defense mechanism against oxidative damage.