Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/11174
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dc.contributor.authorBramante, Giannien
dc.contributor.authorPatel, Oneelen
dc.contributor.authorShulkes, Arthuren
dc.contributor.authorBaldwin, Graham Sen
dc.date.accessioned2015-05-16T00:45:43Z
dc.date.available2015-05-16T00:45:43Z
dc.date.issued2010-12-30en
dc.identifier.citationBiochemical and Biophysical Research Communications 2010; 404(4): 1083-7en
dc.identifier.govdoc21195058en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/11174en
dc.description.abstractThe gastrointestinal hormone gastrin is generated from an 80 amino acid precursor (progastrin) by cleavage after dibasic residues by prohormone convertase 1. Phosphorylation of Ser(75) has previously been suggested, on the basis of indirect evidence, to inhibit cleavage of progastrin after Arg(73)Arg(74). Gastrins bind two ferric ions with high affinity, and iron binding is essential for the biological activity of non-amidated gastrins in vitro and in vivo. This study directly investigated the effect of iron binding and of serine phosphorylation on the cleavage of synthetic progastrin-derived peptides. The affinity of synthetic progastrin(55-80) for ferric ions, and the rate of cleavage by prohormone convertase 1, were not affected by phosphorylation of Ser(75). In contrast, in the presence of ferric ions the rate of cleavage of both progastrin(55-80) and phosphoSer(75)progastrin(55-80) by prohormone convertase 1 was significantly reduced. Hence iron binding to progastrin may regulate processing and secretion in vivo, and regulation may be particularly important in diseases with altered iron homeostasis.en
dc.language.isoenen
dc.subject.otherAmino Acid Sequenceen
dc.subject.otherGastrins.chemistry.metabolismen
dc.subject.otherHumansen
dc.subject.otherIron.chemistry.metabolismen
dc.subject.otherMolecular Sequence Dataen
dc.subject.otherPhosphorylationen
dc.subject.otherPhosphoserine.metabolismen
dc.subject.otherProprotein Convertase 1.metabolismen
dc.subject.otherProtein Precursors.chemistry.metabolismen
dc.subject.otherSerine.metabolismen
dc.subject.otherTrypsin.metabolismen
dc.titleFerric ions inhibit proteolytic processing of progastrin.en
dc.typeJournal Articleen
dc.identifier.journaltitleBiochemical and biophysical research communicationsen
dc.identifier.affiliationThe University of Melbourne, Department of Surgery, Austin Health, Heidelberg, 3084 Victoria, Australiaen
dc.identifier.doi10.1016/j.bbrc.2010.12.117en
dc.description.pages1083-7en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/21195058en
dc.type.austinJournal Articleen
item.fulltextNo Fulltext-
item.openairetypeJournal Article-
item.languageiso639-1en-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
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