Heme oxygenase.docVIP

 PAGE \* MERGEFORMAT 20 Heme oxygenase Keywords: heme oxygenase [Keywords:] heme oxygenase-1; heart disease; Literature Review Evolution of a human adaptive change is to be able to withstand external oxidative damage while maintaining its own stability. Superoxide dismutase, peroxidase, catalase, and some non-enzyme substances of vitamin E, vitamin C in withstanding oxidative injury in the outside world have played an important role, as well as little-known heme oxygenase ( HO) in stress conditions, to maintain the stability of cells is also crucial. HO gene deletion of the individuals can not grow normally, and increased sensitivity to oxidative damage and eventually death [1]. HO is the rate-limiting enzyme heme oxygenase, in the body there are three kinds of isozymes, HO1, HO2, and HO3, respectively, encoded by different genes, their amino acid sequence homology between HO1 and HO2 is 40%, HO2 and HO3 was 90%. Their molecular structure, expression regulation and tissue distribution has very different. HO1 and HO2 is induced to constitute a type. HO The first three kinds of subtypes HO3 discovered only very recently, and HO2 structurally similar, but weaker function of hemoglobin breakdown. HO1 in the organization of the pathological conditions of oxidative damage plays a role in protecting cells, while HO2 have played a role in physiological regulation [2]. Current research focuses on HO1 gene expression, regulation and control as well as the relationship between the disease and so on. 1 HO1 general biological characteristics and functions of HO1, also known as heat shock protein 32 (HSP32), is currently the most studied kind of isozymes. Relative molecular mass of 32000, chromosome location 22q12, in cells located in microsomes, induced expression in the liver, spleen, heart, lung, vascular smooth muscle, brain, and induce stress factors, hypoxia, endotoxin, too hydrogen peroxide, heavy metals, ultraviolet radiation, cytokines,