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Contribution of cathepsin L to secretome composition and cleavage pattern of mouse embryonic fibroblasts

Abstract 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 ...

Authors:   Stefan Tholen; Martin L. Biniossek; Anna-Lena Geßler; Sebastian Müller; Juliane Weißer; Jayachandran N. Kizhakkedathu; Thomas Reinheckel; Oliver Schilling
Journal:   Biological Chemistry
Year:   2011
DOI:   10.1515/BC.2011.162
Publication date:   06-Oct-2011
Facts, background information, dossiers
  • protease inhibitors
  • immunodetection
  • cancer
  • arthritis
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