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pubmed-article:11801256pubmed:abstractTextProteolysis of insulin-like growth factor binding proteins (IGFBPs) is the major mechanism of releasing IGFs from their IGFBP complexes. Analysis of fibroblasts deficient for the lysosomal cysteine protease cathepsin L (CTSL) revealed an accumulation of IGFBP-3 in the medium which was due neither to alterations in IGFBP-3 mRNA expression nor to extracellular IGFBP-3 protease activity. Incubation of CTSL-deficient fibroblasts with radiolabeled IGFBP-3 followed by subcellular fractionation indicates that both intact and fragmented IGFBP-3 accumulate transiently in endosomal and lysosomal fractions of CTSL-deficient cells. This suggests the involvement of CTSL in the intracellular degradation of IGFBP-3 representing a new mechanism to regulate the extracellular concentration of IGFBP-3.lld:pubmed
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pubmed-article:11801256pubmed:articleTitleDecreased intracellular degradation of insulin-like growth factor binding protein-3 in cathepsin L-deficient fibroblasts.lld:pubmed
pubmed-article:11801256pubmed:affiliationCildren's Hospital-Biochemistry, University of Hamburg, Germany.lld:pubmed
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