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Article: Insulin-like growth factor-I (IGF-I) enhanced proteolysis of IGF-binding protein-4 in conditioned medium from primary cultures of human decidua: Independence from IGF receptor binding

TitleInsulin-like growth factor-I (IGF-I) enhanced proteolysis of IGF-binding protein-4 in conditioned medium from primary cultures of human decidua: Independence from IGF receptor binding
Authors
Issue Date1993
PublisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.org
Citation
Endocrinology, 1993, v. 133 n. 4, p. 1525-1531 How to Cite?
AbstractPrevious studies demonstrated that human decidual cells release insulin- like growth factor-binding protein (IGFBP)-1, IGFBP-2, and a 21 kilodalton (kDa) IGFBP in culture. The accumulation of 24-kDa IGFBP, as assessed by ligand blot analysis, decreased when the cells were exposed to IGF-I, but the mechanism was not explored. In the present study, we observed that the IGF- I-mediated decrease in IGFBP-4 accumulation could be explained by increased IGFBP-4 proteolysis. Analysis by IGFBP-4 immunoblotting demonstrated a decline in 24-kDa IGFBP-4 accompanied by a marked increase in a 17- to 18.5- kDa IGFBP-4 fragment(s). In addition, when medium from IGF-I-treated cells was incubated with rat IGFBP-4, the decrease in IGFBP-4 was inhibited by chelators of divalent cations and inhibitors of serine proteases. IGF-I enhancement of IGFBP-4 proteolysis occurs independent of the type I IGF receptor. [Leu 24,1-62]IGF-I, an analog with reduced receptor affinity, mimicked the effect of native IGF-I in cell culture. Additionally, α-IR 3, a monoclonal antibody to the type IIGF receptor, did not block the effect of IGF-I. When IGF-I was incubated with medium from control cells, there was a marked decrease in 24-kDa IGFBP-4 levels and a concomitant increase in levels of a 17- to 18.5-kDa fragment(s), suggesting that IGFBP-4 complexed with IGF- I is more susceptible to proteolysis than IGFBP-4 alone. Together, these findings suggest a novel mechanism for regulation of IGF-I action in the decidua.
Persistent Identifierhttp://hdl.handle.net/10722/170269
ISSN
2015 Impact Factor: 4.159
2015 SCImago Journal Rankings: 2.363
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorMyers, SEen_US
dc.contributor.authorPik To Cheungen_US
dc.contributor.authorHandwerger, Sen_US
dc.contributor.authorChernausek, SDen_US
dc.date.accessioned2012-10-30T06:07:05Z-
dc.date.available2012-10-30T06:07:05Z-
dc.date.issued1993en_US
dc.identifier.citationEndocrinology, 1993, v. 133 n. 4, p. 1525-1531en_US
dc.identifier.issn0013-7227en_US
dc.identifier.urihttp://hdl.handle.net/10722/170269-
dc.description.abstractPrevious studies demonstrated that human decidual cells release insulin- like growth factor-binding protein (IGFBP)-1, IGFBP-2, and a 21 kilodalton (kDa) IGFBP in culture. The accumulation of 24-kDa IGFBP, as assessed by ligand blot analysis, decreased when the cells were exposed to IGF-I, but the mechanism was not explored. In the present study, we observed that the IGF- I-mediated decrease in IGFBP-4 accumulation could be explained by increased IGFBP-4 proteolysis. Analysis by IGFBP-4 immunoblotting demonstrated a decline in 24-kDa IGFBP-4 accompanied by a marked increase in a 17- to 18.5- kDa IGFBP-4 fragment(s). In addition, when medium from IGF-I-treated cells was incubated with rat IGFBP-4, the decrease in IGFBP-4 was inhibited by chelators of divalent cations and inhibitors of serine proteases. IGF-I enhancement of IGFBP-4 proteolysis occurs independent of the type I IGF receptor. [Leu 24,1-62]IGF-I, an analog with reduced receptor affinity, mimicked the effect of native IGF-I in cell culture. Additionally, α-IR 3, a monoclonal antibody to the type IIGF receptor, did not block the effect of IGF-I. When IGF-I was incubated with medium from control cells, there was a marked decrease in 24-kDa IGFBP-4 levels and a concomitant increase in levels of a 17- to 18.5-kDa fragment(s), suggesting that IGFBP-4 complexed with IGF- I is more susceptible to proteolysis than IGFBP-4 alone. Together, these findings suggest a novel mechanism for regulation of IGF-I action in the decidua.en_US
dc.languageengen_US
dc.publisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.orgen_US
dc.relation.ispartofEndocrinologyen_US
dc.subject.meshCarrier Proteins - Metabolismen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshCulture Media, Conditioneden_US
dc.subject.meshDecidua - Cytology - Metabolismen_US
dc.subject.meshDose-Response Relationship, Drugen_US
dc.subject.meshFemaleen_US
dc.subject.meshHumansen_US
dc.subject.meshImmunoblottingen_US
dc.subject.meshInsulin - Pharmacologyen_US
dc.subject.meshInsulin-Like Growth Factor Binding Protein 4en_US
dc.subject.meshInsulin-Like Growth Factor Binding Proteinsen_US
dc.subject.meshInsulin-Like Growth Factor I - Pharmacologyen_US
dc.subject.meshPeptide Hydrolases - Metabolismen_US
dc.subject.meshReceptors, Somatomedin - Metabolismen_US
dc.subject.meshSomatomedins - Metabolismen_US
dc.titleInsulin-like growth factor-I (IGF-I) enhanced proteolysis of IGF-binding protein-4 in conditioned medium from primary cultures of human decidua: Independence from IGF receptor bindingen_US
dc.typeArticleen_US
dc.identifier.emailPik To Cheung:ptcheung@hkucc.hku.hken_US
dc.identifier.authorityPik To Cheung=rp00351en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1210/en.133.4.1525en_US
dc.identifier.pmid7691578-
dc.identifier.scopuseid_2-s2.0-0027504344en_US
dc.identifier.volume133en_US
dc.identifier.issue4en_US
dc.identifier.spage1525en_US
dc.identifier.epage1531en_US
dc.identifier.isiWOS:A1993MA41100006-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridMyers, SE=36779481200en_US
dc.identifier.scopusauthoridPik To Cheung=7202595465en_US
dc.identifier.scopusauthoridHandwerger, S=7005235562en_US
dc.identifier.scopusauthoridChernausek, SD=7005403226en_US

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