Tsushima H, Mine H, Kawakami Y, Hyodoh F, Ueki A
Department of Hygiene, Kawasaki Medical School, Kurashiki, Japan.
Microbiology (Reading). 1994 Jan;140 ( Pt 1):167-71. doi: 10.1099/13500872-140-1-167.
It is known that the cysteine proteinase inhibitor, cystatin, has a defence function against exogenous pathogens. Human epidermal cysteine proteinase inhibitor, cystatin A, which is a member of the cystatin family, is localized in the upper epidermal layer. In this study, the relationship between cystatin A and Candida aspartic proteinase (CAP), a putative Candida virulence factor, was studied. CAP activity was not affected by human epidermal cystatin A, while 90% of cystatin A activity was lost after incubation with CAP for 12 h at 37 degrees C. Human epidermal cystatin A was cleaved into small peptides by CAP, and the released peptides had no cystatin activity. These results suggest that CAP may induce an imbalance between cysteine proteinase and its inhibitor in cutaneous Candida infectious lesions through the degradation and inactivation of epidermal cystatin A.
已知半胱氨酸蛋白酶抑制剂胱抑素对外源性病原体具有防御功能。人表皮半胱氨酸蛋白酶抑制剂胱抑素A是胱抑素家族的成员之一，定位于表皮上层。在本研究中，对胱抑素A与白色念珠菌天冬氨酸蛋白酶（CAP，一种假定的白色念珠菌毒力因子）之间的关系进行了研究。人表皮胱抑素A不影响CAP活性，而在37℃与CAP孵育12小时后，90%的胱抑素A活性丧失。人表皮胱抑素A被CAP切割成小肽，释放的肽没有胱抑素活性。这些结果表明，CAP可能通过降解和使表皮胱抑素A失活，在皮肤念珠菌感染性病变中诱导半胱氨酸蛋白酶与其抑制剂之间的失衡。
