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首页> 外文期刊>The Journal of investigative dermatology. >Analysis of Proteins with Caseinolytic Activity in a Human Stratum Corneum Extract Revealed a Yet Unidentified Cysteine Protease and Identified the So-Called 'Stratum Corneum Thiol Protease' as Cathepsin L2.
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Analysis of Proteins with Caseinolytic Activity in a Human Stratum Corneum Extract Revealed a Yet Unidentified Cysteine Protease and Identified the So-Called 'Stratum Corneum Thiol Protease' as Cathepsin L2.

机译：在人类角质层提取物中具有酪蛋白水解活性的蛋白质分析揭示了尚未鉴定的半胱氨酸蛋白酶，并将所谓的“角质层巯基丙氨酸蛋白酶”鉴定为组织蛋白酶L2。

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Desquamation is described as a protease-dependent phenomenon where serine proteases with a basic pH optimum play a key role. Recently proteases with an acidic pH optimum were identified in the stratumcorneum and associated with desquamation, e.g., cathepsin D and the stratum corneum thiol protease. The purpose of this study was to investigate if human stratum corneum contains proteases different from the above, exhibiting similar properties. After gel filtration, we identified four distinct proteolytic activities in a human stratum corneum extract, a cathepsin-E-like activity (80 kDa), a cathepsin-D activity (40 kDa), a yet unknown cathepsin-L-like form (28 kDa) exhibiting the highest caseinolytic activity, and a chymotrypsin-like protein (24 kDa) containing the acidic activity of the well described stratum corneum chymotryptic enzyme. We named the new 28 kDa protease stratum corneum cathepsin-L-like enzyme. Characterization of stratum corneum cathepsin-L-like enzyme provided clear evidence that this new protease, despite its membership to the cathepsin-L-like family, is distinct from cathepsin L and from the recently described stratum corneum thiol protease. Its ability to hydrolyze corneodesmosin, a marker of corneocyte cohesion, was in favor of a role of stratum corneum cathepsin-L-like enzyme in the desquamation process. A more detailed analysis did not allow us to identify stratum corneum cathepsin-L-like enzyme at the molecular level but revealed that stratum corneum thiol protease is identical with the recently described cathepsin L2 protease. Reverse transcription polymerase chain reaction studies and the use of a specific antibody revealed that, in contrast to earlier reports, expression of stratum corneum thiol protease in human epidermis is not related to keratinocyte differentiation. Our results indicate that the stratum corneum thiol protease is probably expressed as a pro-enzyme in the lower layers of the epidermis and in part activated by a yet unidentified mechanism in the upper layers during keratinocyte differentiation.
机译：脱皮现象被描述为一种蛋白酶依赖性现象，其中具有最适pH值的最佳丝氨酸蛋白酶起着关键作用。最近，在角质层中鉴定出具有最佳酸性pH的蛋白酶，并且该蛋白酶与脱皮有关，例如组织蛋白酶D和角质层硫醇蛋白酶。这项研究的目的是调查人角质层是否含有与上述不同的蛋白酶，并具有相似的特性。凝胶过滤后，我们在人角质层提取物中鉴定出四种不同的蛋白水解活性：组织蛋白酶E样活性（80 kDa），组织蛋白酶D活性（40 kDa）和未知的组织蛋白酶L样形式（28）。 kDa）表现出最高的酪蛋白水解活性，而一种胰凝乳蛋白酶样蛋白（24 kDa）则包含已充分描述的角质层胰凝乳蛋白酶的酸性活性。我们将新的28 kDa蛋白酶命名为角质层组织蛋白酶L样酶。角质层组织蛋白酶-L样酶的表征提供了明确的证据，表明这种新蛋白酶尽管是组织蛋白酶-L样家族的成员，但与组织蛋白酶L和最近描述的角质层硫醇蛋白酶不同。它具有水解角质形成素的能力，角质形成素是角质细胞凝聚力的标志，有利于角质层组织蛋白酶L样酶在脱皮过程中的作用。更详细的分析不允许我们在分子水平上鉴定角质层组织蛋白酶-L样酶，但显示角质层硫醇蛋白酶与最近描述的组织蛋白酶L2蛋白酶相同。逆转录聚合酶链反应研究和特定抗体的使用表明，与早期报道相反，人表皮中角质层硫醇蛋白酶的表达与角质形成细胞的分化无关。我们的结果表明，角质层硫醇蛋白酶可能在表皮的较低层中表达为一种原酶，并在角质形成细胞分化过程中由较高层中的一种尚未被识别的机制部分激活。

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