Antileukoprotease inhibits stratum corneum chymotryptic enzyme - Evidence for a regulative function in desquamation
Antileukoprotease inhibits stratum corneum chymotryptic enzyme - Evidence for a regulative function in desquamation
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DOI：
10.1074/jbc.271.36.21886
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发表时间：
1996-09-06
影响因子：
4.8
通讯作者：
Wiedow, O
中科院分区：
文献类型：
--
作者：
Franzke, CW;Baici, A;Wiedow, O
角质层凝乳胰蛋白酶（SCCE）先前已经从人角质层中纯化出来，它类似于一种凝乳胰蛋白酶，参与角质层角质层细胞的生理脱离。从人角质层中可提取两种抑菌活性的SCCE。这是由于已知存在于人类表皮的丝氨酸蛋白酶抑制剂、抗白细胞蛋白酶（分泌性白细胞蛋白酶抑制剂）和elafin（皮肤源性抗白细胞蛋白酶）。抗白细胞蛋白酶对SCCE的抑制表现为双曲型混合抑制，平衡解离常数为63 nM。在体外实验中，抗白细胞蛋白酶也几乎完全抑制人足底愈伤组织角质层细胞的脱落（>96%）。此外，elafin被证明是SCCE活性的弱抑制剂，elafin显著减少角质层细胞的脱落。因此，已知由人角质形成细胞产生的抗白细胞蛋白酶可能是表皮SCCE的主要生理抑制剂。它似乎在生理和病理生理条件下参与了脱屑的调节。
The stratum corneum chymotryptic enzyme (SCCE) has been previously purified from human stratum corneum and resembles a chymotryptic serine endopeptidase involved in physiological detachment of corneocytes from human stratum corneum. From human stratum corneum two inhibitory activities of SCCE could be extracted. These were due to serine protease inhibitors already known to be present in human epidermis, antileukoprotease (secretory leukocyte protease inhibitor) and elafin (skin-derived antileukoprotease). The Inhibition of SCCE by antileukoprotease shows a hyperbolic, mixed type inhibition with an equilibrium dissociation constant of 63 nM. Antileukoprotease also inhibits detachment of corneocytes from human plantar callus in vitro almost completely (>96%). In addition, elafin was shown to be a weak inhibitor for SCCE activity, and elafin significantly reduces the shedding of corneocytes. Thus, antileukoprotease, which is known to be produced by human keratinocytes, is likely to be the major physiological inhibitor of SCCE in the epidermis. It seems to be involved in the regulation of desquamation under physiological and pathophysiological conditions.