Barrett A J, Davies M E, Grubb A
Biochem Biophys Res Commun. 1984 Apr 30;120(2):631-6. doi: 10.1016/0006-291x(84)91302-0.
Native gamma-trace, a small basic protein present in high concentration in cerebrospinal fluid, semen and neuroendocrine cells, but of unknown biological function, is shown to be a potent inhibitor of the cysteine proteinases papain, ficin, and human cathepsins B, H and L. It proves to be the tightest -binding protein inhibitor of cathepsin B so far discovered. The name cystatin C is proposed for gamma-trace to reflect the many similarities in activity and structure to chicken egg-white cystatin and mammalian cystatins A and B. The inhibition constants of cystatin C, taken together with its widespread distribution in human tissues and extracellular fluids, suggest that a physiological function could well be the regulation of cysteine proteinase activity.
天然γ-痕量蛋白是一种小的碱性蛋白,在脑脊液、精液和神经内分泌细胞中高浓度存在,但其生物学功能尚不清楚。现已表明它是半胱氨酸蛋白酶木瓜蛋白酶、无花果蛋白酶以及人组织蛋白酶B、H和L的有效抑制剂。它被证明是迄今发现的组织蛋白酶B结合最紧密的蛋白抑制剂。建议将γ-痕量蛋白命名为胱抑素C,以反映其在活性和结构上与鸡卵清胱抑素以及哺乳动物胱抑素A和B的诸多相似性。胱抑素C的抑制常数,连同其在人体组织和细胞外液中的广泛分布,表明其生理功能很可能是调节半胱氨酸蛋白酶的活性。