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Article: Mechanisms of Sertoli cell insulin-like growth factor (IGF)-binding protein-3 regulation by IGF-I and adenosine 3',5'-monophosphate

TitleMechanisms of Sertoli cell insulin-like growth factor (IGF)-binding protein-3 regulation by IGF-I and adenosine 3',5'-monophosphate
Authors
Issue Date1992
PublisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.org
Citation
Endocrinology, 1992, v. 131 n. 6, p. 2733-2741 How to Cite?
AbstractFSH, which stimulates cAMP in the Sertoli cell, markedly lowers the concentration of insulin-like growth factor-binding protein-3 (IGFBP-3) in Sertoli cell-conditioned medium; in contrast, insulin-like growth factor-I (IGF-I) increases BP-3 expression. In this study, the mechanisms controlling the contrasting effects of cAMP and IGF-I were investigated. The abundance of BP-3 mRNA was dramatically lowered by (Bu) 2cAMP, but was unaffected by IGF- I. Analyzed by ligand blot of conditioned medium, coincubation of (Bu) 2cAMP and IGF-I largely eliminated the increase observed with IGF-I alone. Based on the following evidence, the effect of IGF-I appeared to be solely related to the capacity of IGF-I to interact directly with BP-3. 1) Insulin at micromolar concentrations failed to increase BP-3 abundance despite documentation by affinity cross-linking that insulin displaced [ 125I]IGF- I from the IGF-I receptor. 2) A synthetic IGF-I analog, (Leu 24,1-62]IGF-I, which has reduced binding affinity for rat IGF-I receptor but displays high affinity for rat Sertoli cell-conditioned medium BPs, increased BP-3 abundance. 3) A synthetic IGF-I analog, B-chain mutant, which has reduced affinity for rat Sertoli cell BPs but displays normal affinity for the rat IGF-I receptor, failed to increase BP-3 abundance. 4) Human recombinant glycosylated [ 125I]BP-3 when added to cultured Sertoli cells was preserved in the medium when IGF-I or analogs with BP-3 affinity were present. 5) IGF- I, in dose-responsive manner, both retarded the disappearance from the medium of exogenously added human recombinant nonglycosylated BP-3 and decreased the amount of membrane-associated BP-3. These results indicate that whereas cAMP lowers BP-3 abundance in medium, most likely by markedly decreasing synthesis, IGF-I increases BP-3 accumulation by retarding its clearance by the Sertoli cell.
Persistent Identifierhttp://hdl.handle.net/10722/170251
ISSN
2015 Impact Factor: 4.159
2015 SCImago Journal Rankings: 2.363
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorSmith, EPen_US
dc.contributor.authorPik To Cheungen_US
dc.contributor.authorFerguson, Aen_US
dc.contributor.authorChernausek, SDen_US
dc.date.accessioned2012-10-30T06:06:58Z-
dc.date.available2012-10-30T06:06:58Z-
dc.date.issued1992en_US
dc.identifier.citationEndocrinology, 1992, v. 131 n. 6, p. 2733-2741en_US
dc.identifier.issn0013-7227en_US
dc.identifier.urihttp://hdl.handle.net/10722/170251-
dc.description.abstractFSH, which stimulates cAMP in the Sertoli cell, markedly lowers the concentration of insulin-like growth factor-binding protein-3 (IGFBP-3) in Sertoli cell-conditioned medium; in contrast, insulin-like growth factor-I (IGF-I) increases BP-3 expression. In this study, the mechanisms controlling the contrasting effects of cAMP and IGF-I were investigated. The abundance of BP-3 mRNA was dramatically lowered by (Bu) 2cAMP, but was unaffected by IGF- I. Analyzed by ligand blot of conditioned medium, coincubation of (Bu) 2cAMP and IGF-I largely eliminated the increase observed with IGF-I alone. Based on the following evidence, the effect of IGF-I appeared to be solely related to the capacity of IGF-I to interact directly with BP-3. 1) Insulin at micromolar concentrations failed to increase BP-3 abundance despite documentation by affinity cross-linking that insulin displaced [ 125I]IGF- I from the IGF-I receptor. 2) A synthetic IGF-I analog, (Leu 24,1-62]IGF-I, which has reduced binding affinity for rat IGF-I receptor but displays high affinity for rat Sertoli cell-conditioned medium BPs, increased BP-3 abundance. 3) A synthetic IGF-I analog, B-chain mutant, which has reduced affinity for rat Sertoli cell BPs but displays normal affinity for the rat IGF-I receptor, failed to increase BP-3 abundance. 4) Human recombinant glycosylated [ 125I]BP-3 when added to cultured Sertoli cells was preserved in the medium when IGF-I or analogs with BP-3 affinity were present. 5) IGF- I, in dose-responsive manner, both retarded the disappearance from the medium of exogenously added human recombinant nonglycosylated BP-3 and decreased the amount of membrane-associated BP-3. These results indicate that whereas cAMP lowers BP-3 abundance in medium, most likely by markedly decreasing synthesis, IGF-I increases BP-3 accumulation by retarding its clearance by the Sertoli cell.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.meshAnimalsen_US
dc.subject.meshBucladesine - Pharmacologyen_US
dc.subject.meshCarrier Proteins - Geneticsen_US
dc.subject.meshCyclic Amp - Pharmacologyen_US
dc.subject.meshGene Expression Regulation - Drug Effectsen_US
dc.subject.meshGlycosylationen_US
dc.subject.meshHumansen_US
dc.subject.meshInsulin - Pharmacologyen_US
dc.subject.meshInsulin-Like Growth Factor Binding Proteinsen_US
dc.subject.meshInsulin-Like Growth Factor I - Metabolism - Pharmacologyen_US
dc.subject.meshMaleen_US
dc.subject.meshRna, Messenger - Metabolismen_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Sprague-Dawleyen_US
dc.subject.meshRecombinant Proteins - Metabolismen_US
dc.subject.meshSertoli Cells - Drug Effects - Metabolismen_US
dc.titleMechanisms of Sertoli cell insulin-like growth factor (IGF)-binding protein-3 regulation by IGF-I and adenosine 3',5'-monophosphateen_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.131.6.2733en_US
dc.identifier.pmid1280204-
dc.identifier.scopuseid_2-s2.0-0026482759en_US
dc.identifier.volume131en_US
dc.identifier.issue6en_US
dc.identifier.spage2733en_US
dc.identifier.epage2741en_US
dc.identifier.isiWOS:A1992KB06800036-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridSmith, EP=7408615693en_US
dc.identifier.scopusauthoridPik To Cheung=7202595465en_US
dc.identifier.scopusauthoridFerguson, A=7402054472en_US
dc.identifier.scopusauthoridChernausek, SD=7005403226en_US

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