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pubmed-article:15318816pubmed:abstractTextCathepsins are implicated in a multitude of physiological and pathophysiological processes. The aim of the present study was to investigate the function of cathepsin L (catL) in the proteolytic network of human lung epithelial cells and its role in the regulation of apoptosis. We found that catL-deficient A549 cells as well as lung tissue extracts of catL(-/-) mice express increased amounts of single-chain cathepsin D (catD). Degradation experiments indicate that catL specifically degrades the single-chain isoform of catD. Furthermore, we found that catL-deficient cells showed increased sensitivity to apoptosis. Finally, we demonstrate that the inhibition of catD activity by pepstatin A decreased the number of apoptotic cells in catL-deficient A549 cells after anti-Fas treatment. In conclusion, catL is involved in catD processing and the accumulation of catD isoforms in catL-deficient cells is associated with increased rates of spontaneous and anti-Fas-induced apoptosis.lld:pubmed
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pubmed-article:15318816pubmed:dateRevised2009-11-19lld:pubmed
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pubmed-article:15318816pubmed:articleTitleCathepsin L is involved in cathepsin D processing and regulation of apoptosis in A549 human lung epithelial cells.lld:pubmed
pubmed-article:15318816pubmed:affiliationInstitute of Immunology, Otto-von-Guericke-University Magdeburg, Leipziger-Str. 44, D-39120 Magdeburg Germany.lld:pubmed
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