The serpin superfamily of proteinase inhibitors: structure, function, and regulation.
The serpin superfamily of proteinase inhibitors: structure, function, and regulation.
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发表时间:
1994-06
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通讯作者:
J. Potempa;Edward KorzusO;James TravisJn
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作者:
J. Potempa;Edward KorzusO;James TravisJn
The regulation of proteolytic enzymes in tissues by endogenous inhibitors is a critical requirement in the maintenance of homeostasis. These proteins are found primarily in blood plasma and account for more than 10% of its total content, with the vast ma-jority targeted toward the serine proteinases known to be involved in phagocytosis, coagulation, complement activation, and fibrinolysis. There are several classes of proteinase inhibitors in plasma; however, one superfamily ofinhibitors referred to as serpins ( proteinase inhibitors) predominates (l), with its members also be- ing found in plants and viruses (2,3). For most, the primary function is regulation of proteolytic events associated with a myriad of biochemical pathways (Fig. l), but many have alternate functions such as hormone transport (cortisol-binding globulin and thyroxine binding globulin) or blood pressure regulation (angiotensinogen).