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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2002-1-21
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pubmed:abstractText |
Proteolysis 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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin L,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsins,
http://linkedlifedata.com/resource/pubmed/chemical/Ctsl protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Conditioned,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor Binding...,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor Binding...,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
510
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
211-5
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11801256-Animals,
pubmed-meshheading:11801256-Cathepsin L,
pubmed-meshheading:11801256-Cathepsins,
pubmed-meshheading:11801256-Cells, Cultured,
pubmed-meshheading:11801256-Culture Media, Conditioned,
pubmed-meshheading:11801256-Cysteine Endopeptidases,
pubmed-meshheading:11801256-Endocytosis,
pubmed-meshheading:11801256-Endosomes,
pubmed-meshheading:11801256-Extracellular Space,
pubmed-meshheading:11801256-Fibroblasts,
pubmed-meshheading:11801256-Insulin-Like Growth Factor Binding Protein 3,
pubmed-meshheading:11801256-Insulin-Like Growth Factor Binding Protein 4,
pubmed-meshheading:11801256-Intracellular Fluid,
pubmed-meshheading:11801256-Lysosomes,
pubmed-meshheading:11801256-Mice,
pubmed-meshheading:11801256-Mice, Knockout,
pubmed-meshheading:11801256-RNA, Messenger,
pubmed-meshheading:11801256-Subcellular Fractions,
pubmed-meshheading:11801256-Substrate Specificity
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pubmed:year |
2002
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pubmed:articleTitle |
Decreased intracellular degradation of insulin-like growth factor binding protein-3 in cathepsin L-deficient fibroblasts.
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pubmed:affiliation |
Cildren's Hospital-Biochemistry, University of Hamburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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