pubmed-article:11801256 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11801256 | lifeskim:mentions | umls-concept:C0016030 | lld:lifeskim |
pubmed-article:11801256 | lifeskim:mentions | umls-concept:C0178719 | lld:lifeskim |
pubmed-article:11801256 | lifeskim:mentions | umls-concept:C0007428 | lld:lifeskim |
pubmed-article:11801256 | lifeskim:mentions | umls-concept:C0205216 | lld:lifeskim |
pubmed-article:11801256 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
pubmed-article:11801256 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
pubmed-article:11801256 | lifeskim:mentions | umls-concept:C1149301 | lld:lifeskim |
pubmed-article:11801256 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:11801256 | pubmed:dateCreated | 2002-1-21 | lld:pubmed |
pubmed-article:11801256 | 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. | lld:pubmed |
pubmed-article:11801256 | pubmed:language | eng | lld:pubmed |
pubmed-article:11801256 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11801256 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11801256 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:11801256 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11801256 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:11801256 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11801256 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11801256 | pubmed:month | Jan | lld:pubmed |
pubmed-article:11801256 | pubmed:issn | 0014-5793 | lld:pubmed |
pubmed-article:11801256 | pubmed:author | pubmed-author:SaftigPaulP | lld:pubmed |
pubmed-article:11801256 | pubmed:author | pubmed-author:ZwadOlafO | lld:pubmed |
pubmed-article:11801256 | pubmed:author | pubmed-author:KüblerBerndB | lld:pubmed |
pubmed-article:11801256 | pubmed:author | pubmed-author:RothWeraW | lld:pubmed |
pubmed-article:11801256 | pubmed:author | pubmed-author:ScharfJens-Ge... | lld:pubmed |
pubmed-article:11801256 | pubmed:author | pubmed-author:PetersChristo... | lld:pubmed |
pubmed-article:11801256 | pubmed:author | pubmed-author:BraulkeThomas... | lld:pubmed |
pubmed-article:11801256 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11801256 | pubmed:day | 16 | lld:pubmed |
pubmed-article:11801256 | pubmed:volume | 510 | lld:pubmed |
pubmed-article:11801256 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11801256 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11801256 | pubmed:pagination | 211-5 | lld:pubmed |
pubmed-article:11801256 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:11801256 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:11801256 | pubmed:articleTitle | Decreased intracellular degradation of insulin-like growth factor binding protein-3 in cathepsin L-deficient fibroblasts. | lld:pubmed |
pubmed-article:11801256 | pubmed:affiliation | Cildren's Hospital-Biochemistry, University of Hamburg, Germany. | lld:pubmed |
pubmed-article:11801256 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11801256 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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