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首页> 外文期刊>Biological chemistry >Contribution of cathepsin L to secretome composition and cleavage pattern of mouse embryonic fibroblasts.
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Contribution of cathepsin L to secretome composition and cleavage pattern of mouse embryonic fibroblasts.

机译：组织蛋白酶L对小鼠胚胎成纤维细胞分泌组组成和裂解模式的贡献。

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摘要

The endolysosomal cysteine endoprotease cathepsin L is secreted from cells in a variety of pathological conditions such as cancer and arthritis. We compared the secretome composition and extracellular proteolytic cleavage events in cell supernatants of cathepsin L-deficient and wild-type mouse embryonic fibroblasts (MEFs). Quantitative proteomic comparison of cell conditioned media indicated that cathepsin L deficiency affects, albeit in a limited manner, the abundances of extracellular matrix (ECM) components, signaling proteins, and further proteases as well as endogenous protease inhibitors. Immunodetection corroborated that cathepsin L deficiency results in decreased abundance of the ECM protein periostin and elevated abundance of matrix metalloprotease (MMP)-2. While mRNA levels of MMP-2 were not affected by cathepsin L ablation, periostin mRNA levels were reduced, potentially indicating a downstream effect. To characterize cathepsin L contribution to extracellular proteolysis, we performed terminal amine isotopic labeling of substrates (TAILS), an N-terminomic technique for the identification and quantification of native and proteolytically generated protein N-termini. TAILS identified >1500 protein N-termini. Cathepsin L deficiency predominantly reduced the magnitude of collagenous cleavage sites C-terminal to a proline residue. This contradicts cathepsin L active site specificity and indicates altered activity of further proteases as a result of cathepsin L ablation.
机译：内溶酶体半胱氨酸内切蛋白酶组织蛋白酶L在多种病理状况（例如癌症和关节炎）中从细胞分泌。我们比较了组织蛋白酶L缺陷和野生型小鼠胚胎成纤维细胞（MEFs）的细胞上清液中的分泌组组成和细胞外蛋白水解裂解事件。细胞条件培养基的蛋白质组学定量比较表明，组织蛋白酶L缺乏会以有限的方式影响细胞外基质（ECM）成分，信号蛋白，其他蛋白酶以及内源蛋白酶抑制剂的丰度。免疫检测证实组织蛋白酶L缺乏会导致ECM蛋白骨膜蛋白的丰度降低和基质金属蛋白酶（MMP）-2的丰度升高。虽然MMP-2的mRNA水平不受组织蛋白酶L消融的影响，但骨膜素mRNA的水平却降低了，可能表明有下游作用。为了表征组织蛋白酶L对细胞外蛋白水解的贡献，我们进行了底物的末端胺同位素标记（TAILS），这是一种N端技术，用于鉴定和定量天然和蛋白水解生成的蛋白N末端。尾巴鉴定出> 1500个蛋白质N末端。组织蛋白酶L缺乏主要减少了脯氨酸残基C端的胶原蛋白切割位点的大小。这与组织蛋白酶L的活性位点特异性相矛盾，并表明由于组织蛋白酶L的消融，其他蛋白酶的活性发生了改变。

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