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dc.contributor.authorClairmont, Kevin B.
dc.contributor.authorCzech, Michael P.
dc.date2022-08-11T08:08:56.000
dc.date.accessioned2022-08-23T16:13:11Z
dc.date.available2022-08-23T16:13:11Z
dc.date.issued1989-10-05
dc.date.submitted2008-08-26
dc.identifier.citation<p>J Biol Chem. 1989 Oct 5;264(28):16390-2.</p>
dc.identifier.issn0021-9258 (Print)
dc.identifier.pmid2550441
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33561
dc.description.abstractThe recent demonstration that a single mammalian receptor protein binds both mannose 6-phosphate (Man-6-P) and insulin-like growth factor II (IGF-II) with high affinity has suggested a multifunctional physiological role for this receptor, possibly including signal transduction. In order to better understand the functions of this receptor, we have investigated the properties of Man-6-P receptors from non-mammalian species. Receptors were affinity-purified from Triton X-100 extracts of total membranes from Xenopus and chicken liver as well as rat placenta using pentamannosyl 6-phosphate-Sepharose. The Man-6-P receptor was adsorbed to the pentamannosyl 6-phosphate-Sepharose and specifically eluted by Man-6-P in all three species, as evaluated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by silver staining. When the purified receptors from these three species were cross-linked to 125I-IGF-II with disuccinimidyl suberate, only receptors isolated from rat membranes were affinity-labeled. To further evaluate the properties of these Man-6-P receptors, binding of 125I-rat-IGF-II and 125I-chicken Tyr-Gly-Thr-Ala-IGF-II to purified receptors from Xenopus, chicken, and rat was evaluated by polyethylene glycol precipitation. Only the rat Man-6-P receptor exhibited detectable binding of 125I-IGF-II. These data suggest that the emergence of a high affinity IGF-II binding site on the Man-6-P receptor occurred in evolution after the divergence of mammals from other vertebrates. Thus, the biological actions of IGF-II in chickens and frogs appear to be initiated by the type I IGF receptor.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2550441&dopt=Abstract ">Link to article in PubMed</a></p>
dc.relation.urlhttp://www.jbc.org/content/264/28/16390.short
dc.subjectAnimals; Chickens; Chromatography, Affinity; Female; Hexosephosphates; Humans; Insulin-Like Growth Factor II; Kinetics; Mannosephosphates; Microsomes; Microsomes, Liver; Molecular Weight; Placenta; Pregnancy; Protein Binding; Rats; Receptor, IGF Type 2; Receptors, Cell Surface; Somatomedins; Xenopus laevis
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleChicken and Xenopus mannose 6-phosphate receptors fail to bind insulin-like growth factor II
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume264
dc.source.issue28
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/232
dc.identifier.contextkey604125
html.description.abstract<p>The recent demonstration that a single mammalian receptor protein binds both mannose 6-phosphate (Man-6-P) and insulin-like growth factor II (IGF-II) with high affinity has suggested a multifunctional physiological role for this receptor, possibly including signal transduction. In order to better understand the functions of this receptor, we have investigated the properties of Man-6-P receptors from non-mammalian species. Receptors were affinity-purified from Triton X-100 extracts of total membranes from Xenopus and chicken liver as well as rat placenta using pentamannosyl 6-phosphate-Sepharose. The Man-6-P receptor was adsorbed to the pentamannosyl 6-phosphate-Sepharose and specifically eluted by Man-6-P in all three species, as evaluated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by silver staining. When the purified receptors from these three species were cross-linked to 125I-IGF-II with disuccinimidyl suberate, only receptors isolated from rat membranes were affinity-labeled. To further evaluate the properties of these Man-6-P receptors, binding of 125I-rat-IGF-II and 125I-chicken Tyr-Gly-Thr-Ala-IGF-II to purified receptors from Xenopus, chicken, and rat was evaluated by polyethylene glycol precipitation. Only the rat Man-6-P receptor exhibited detectable binding of 125I-IGF-II. These data suggest that the emergence of a high affinity IGF-II binding site on the Man-6-P receptor occurred in evolution after the divergence of mammals from other vertebrates. Thus, the biological actions of IGF-II in chickens and frogs appear to be initiated by the type I IGF receptor.</p>
dc.identifier.submissionpathgsbs_sp/232
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentDepartment of Biochemistry
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages16390-2


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