Matches in SemOpenAlex for { <https://semopenalex.org/work/W2023343511> ?p ?o ?g. }
Showing items 1 to 71 of
71
with 100 items per page.
- W2023343511 abstract "ABSTRACT The biological effects of insulin-like growth factors (IGFs) are mediated by cell surface receptors but their bioavailability is regulated by IGF binding proteins (IGFBPs) which bind IGF with higher affinity than the receptor. Proteolytic cleavage of the binding proteins reduces their affinity for IGF making the IGF more available to the cell receptor. In the current study we have examined the regulation of IGFBP-4 protease produced by cultured human dermal fibroblasts. IGF-I and the analogs of IGF-I (LR 3 and Des[1-3]) induced a dose dependent increase in both proliferation and IGFBP-3 production. Low concentrations of IGF-I induced a marked loss of IGFBP-4 by Western ligand blotting (WLB). This effect was confirmed by the ability of media collected from cells exposed to increasing concentrations of IGF-I to fragment recombinant IGFBP-4, an effect blocked by EDTA. IGFBP-4 proteolysis was observed when cells were exposed to Des[1-3] (albeit at higher concentrations) but not with LR 3 . Both analogs bind to the IGF receptor but do not bind to IGFBP-4 and have reduced (Des[1-3]) or no (LR 3 ) affinity for IGFBP-3. This demonstrated that neither receptor activation nor ligand binding directly to IGFBP-4 was necessary for IGF induced proteolysis. Protease activity correlated with affinity for IGFBP-3 suggesting a role for IGFBP-3 in the regulation of IGFBP-4 proteolysis. This was confirmed by the ability of excess recombinant IGFBP-3 to inhibit the IGF-I and Des[1-3] induced proteolysis of IGFBP-4. Addition of IGF-I to media from cells unexposed to IGF induced IGFBP-4 proteolysis but this was not seen with LR 3 which does not bind to IGFBP-3. Fragmentation occured at higher concentrations of Des[1-3] consistent with its reduced affinity for IGFBP-3 This data suggests that IGFBP-4 proteolysis is regulated in a novel manner by IGFBP-3 which is dependent on the relative proportions of the different binding proteins and the levels of IGFs" @default.
- W2023343511 created "2016-06-24" @default.
- W2023343511 creator A5045581195 @default.
- W2023343511 creator A5084761875 @default.
- W2023343511 date "1996-06-01" @default.
- W2023343511 modified "2023-09-27" @default.
- W2023343511 title "THE ROLE OF IGFBP-3 IN THE REGULATION OF IGFBP-4 PROTEOLYSIS" @default.
- W2023343511 doi "https://doi.org/10.1677/joe.0.149r001" @default.
- W2023343511 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8691093" @default.
- W2023343511 hasPublicationYear "1996" @default.
- W2023343511 type Work @default.
- W2023343511 sameAs 2023343511 @default.
- W2023343511 citedByCount "34" @default.
- W2023343511 countsByYear W20233435112015 @default.
- W2023343511 crossrefType "journal-article" @default.
- W2023343511 hasAuthorship W2023343511A5045581195 @default.
- W2023343511 hasAuthorship W2023343511A5084761875 @default.
- W2023343511 hasConcept C104317684 @default.
- W2023343511 hasConcept C116569031 @default.
- W2023343511 hasConcept C134018914 @default.
- W2023343511 hasConcept C153911025 @default.
- W2023343511 hasConcept C170493617 @default.
- W2023343511 hasConcept C181199279 @default.
- W2023343511 hasConcept C182220744 @default.
- W2023343511 hasConcept C185592680 @default.
- W2023343511 hasConcept C2775960820 @default.
- W2023343511 hasConcept C2776714187 @default.
- W2023343511 hasConcept C2780378035 @default.
- W2023343511 hasConcept C2780689927 @default.
- W2023343511 hasConcept C2781307694 @default.
- W2023343511 hasConcept C40767141 @default.
- W2023343511 hasConcept C55493867 @default.
- W2023343511 hasConcept C62112901 @default.
- W2023343511 hasConcept C85265743 @default.
- W2023343511 hasConcept C86803240 @default.
- W2023343511 hasConceptScore W2023343511C104317684 @default.
- W2023343511 hasConceptScore W2023343511C116569031 @default.
- W2023343511 hasConceptScore W2023343511C134018914 @default.
- W2023343511 hasConceptScore W2023343511C153911025 @default.
- W2023343511 hasConceptScore W2023343511C170493617 @default.
- W2023343511 hasConceptScore W2023343511C181199279 @default.
- W2023343511 hasConceptScore W2023343511C182220744 @default.
- W2023343511 hasConceptScore W2023343511C185592680 @default.
- W2023343511 hasConceptScore W2023343511C2775960820 @default.
- W2023343511 hasConceptScore W2023343511C2776714187 @default.
- W2023343511 hasConceptScore W2023343511C2780378035 @default.
- W2023343511 hasConceptScore W2023343511C2780689927 @default.
- W2023343511 hasConceptScore W2023343511C2781307694 @default.
- W2023343511 hasConceptScore W2023343511C40767141 @default.
- W2023343511 hasConceptScore W2023343511C55493867 @default.
- W2023343511 hasConceptScore W2023343511C62112901 @default.
- W2023343511 hasConceptScore W2023343511C85265743 @default.
- W2023343511 hasConceptScore W2023343511C86803240 @default.
- W2023343511 hasLocation W20233435111 @default.
- W2023343511 hasLocation W20233435112 @default.
- W2023343511 hasOpenAccess W2023343511 @default.
- W2023343511 hasPrimaryLocation W20233435111 @default.
- W2023343511 hasRelatedWork W2017442945 @default.
- W2023343511 hasRelatedWork W2017530941 @default.
- W2023343511 hasRelatedWork W2019020719 @default.
- W2023343511 hasRelatedWork W2020677035 @default.
- W2023343511 hasRelatedWork W2023162617 @default.
- W2023343511 hasRelatedWork W2023343511 @default.
- W2023343511 hasRelatedWork W2042693437 @default.
- W2023343511 hasRelatedWork W2053888774 @default.
- W2023343511 hasRelatedWork W2071102974 @default.
- W2023343511 hasRelatedWork W2085996553 @default.
- W2023343511 isParatext "false" @default.
- W2023343511 isRetracted "false" @default.
- W2023343511 magId "2023343511" @default.
- W2023343511 workType "article" @default.