| pubmed-article:9724028 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9724028 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:9724028 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:9724028 | lifeskim:mentions | umls-concept:C0140079 | lld:lifeskim |
| pubmed-article:9724028 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:9724028 | lifeskim:mentions | umls-concept:C0011155 | lld:lifeskim |
| pubmed-article:9724028 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:9724028 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:9724028 | pubmed:dateCreated | 1998-9-23 | lld:pubmed |
| pubmed-article:9724028 | pubmed:abstractText | To investigate endoproteolytic processing of the type I insulin-like growth factor receptor (IGF-IR), we have examined its structure and activity in the furin-deficient LoVo-C5 cell line. Immunoprecipitation experiments using the monoclonal anti-IGF-IR antibody (alpha-IR3) showed that LoVo-C5 cells expressed a major high molecular mass receptor (200 kDa) corresponding to the unprocessed alpha/beta pro-receptor. A small amount of successfully cleaved alpha/beta heterodimers was also produced, indicating a residual endoproteolytic cleavage activity in these cells. In vitro, a soluble form of recombinant furin was able to cleave the pro-IGF-IR (200 kDa) into alpha-subunit (130 kDa) and beta-subunit (97 kDa). Measurement of IGF binding parameters in LoVo-C5 cells indicated a low number of typical type I IGF-binding sites (binding capacity, 5 x 10(3) sites/cell; Kd, 1.9 nM for IGF-I and 7.0 nM for IGF-II). These findings in LoVo-C5 contrast with those in HT29-D4 cells, which have active furin, and where IGF-IR (2.8 x 10(4) sites/cell) was fully processed. Moreover, the 200-kDa pro-IGF-IR of LoVo-C5 was unable to induce intracellular signaling, such as beta-subunit tyrosine autophosphorylation and insulin-related substrate-1 tyrosine phosphorylation. Flow immunocytometry analysis using alpha-IR3 antibody indicated that LoVo-C5 cells expressed 40% more receptors than HT29-D4 cells, suggesting that in LoVo-C5 cells only the small amount of mature type I IGF-IR binds IGFs with high affinity. To provide evidence for this idea, we showed that mild trypsin treatment of living LoVo-C5 cells partially restored alpha/beta cleavage of IGF-IR, and greatly enhanced (6-fold) the IGF-I binding capacity of LoVo-C5 cells, but did not restore IGF-IR signaling activity. Moreover, LoVo-C5 cells were totally unresponsive to IGF-I in terms of cell migration, in contrast to fully processed IGF-IR-HT29-D4 cells. Our data indicate that furin is involved in the endoproteolytic processing of the IGF-IR and suggest that this posttranslational event might be crucial for its ligand binding and signaling activities. However, our data do not exclude that other proprotein convertases could participate to IGF-IR maturation. | lld:pubmed |
| pubmed-article:9724028 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9724028 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9724028 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:9724028 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9724028 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:9724028 | pubmed:issn | 0013-7227 | lld:pubmed |
| pubmed-article:9724028 | pubmed:author | pubmed-author:LehmannMM | lld:pubmed |
| pubmed-article:9724028 | pubmed:author | pubmed-author:AndräAA | lld:pubmed |
| pubmed-article:9724028 | pubmed:author | pubmed-author:PommierGG | lld:pubmed |
| pubmed-article:9724028 | pubmed:author | pubmed-author:Remacle-Bonne... | lld:pubmed |
| pubmed-article:9724028 | pubmed:author | pubmed-author:MarvaldiJJ | lld:pubmed |
| pubmed-article:9724028 | pubmed:author | pubmed-author:LissitskyJ... | lld:pubmed |
| pubmed-article:9724028 | pubmed:author | pubmed-author:GarrousteFF | lld:pubmed |
| pubmed-article:9724028 | pubmed:author | pubmed-author:BellasFF | lld:pubmed |
| pubmed-article:9724028 | pubmed:author | pubmed-author:ParabPP | lld:pubmed |
| pubmed-article:9724028 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9724028 | pubmed:volume | 139 | lld:pubmed |
| pubmed-article:9724028 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9724028 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9724028 | pubmed:pagination | 3763-71 | lld:pubmed |
| pubmed-article:9724028 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:9724028 | pubmed:meshHeading | pubmed-meshheading:9724028-... | lld:pubmed |
| pubmed-article:9724028 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9724028 | pubmed:articleTitle | Deficient processing and activity of type I insulin-like growth factor receptor in the furin-deficient LoVo-C5 cells. | lld:pubmed |
| pubmed-article:9724028 | pubmed:affiliation | Unité Interactions entre Systèmes Protéiques et Différenciation dans la Cellule Tumorale, UPRES-A CNRS 6032, Université d'Aix-Marseille I, Faculté de Pharmacie, France. | lld:pubmed |
| pubmed-article:9724028 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9724028 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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