Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/10868
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dc.contributor.authorKovac, Suzanaen
dc.contributor.authorFerrand, Audreyen
dc.contributor.authorEstève, Jean-Pierreen
dc.contributor.authorMason, Anne Ben
dc.contributor.authorBaldwin, Graham Sen
dc.date.accessioned2015-05-16T00:26:46Z
dc.date.available2015-05-16T00:26:46Z
dc.date.issued2009-07-31en
dc.identifier.citationThe Febs Journal 2009; 276(17): 4866-74en
dc.identifier.govdoc19664057en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/10868en
dc.description.abstractTransferrin is the main iron transport protein found in the circulation, and the level of transferrin saturation in the blood is an important indicator of iron status. The peptides amidated gastrin(17) (Gamide) and glycine-extended gastrin(17) (Ggly) are well known for their roles in controlling acid secretion and as growth factors in the gastrointestinal tract. Several lines of evidence, including the facts that transferrin binds gastrin, that gastrins bind ferric ions, and that the level of expression of gastrins positively correlates with transferrin saturation, suggest the possible involvement of the transferrin-gastrin interaction in iron homeostasis. In the present work, the interaction between gastrins and transferrin has been characterized by surface plasmon resonance and covalent crosslinking. First, an interaction between iron-free apo-transferrin and Gamide or Ggly was observed. The fact that no interaction was observed in the presence of the chelator EDTA suggested that the gastrin-ferric ion complex was the interacting species. Moreover, removal of ferric ions with EDTA reduced the stability of the complex between apo-transferrin and gastrins, and no interaction was observed between Gamide or Ggly and diferric transferrin. Second, some or all of glutamates at positions 8-10 of the Ggly molecule, together with the C-terminal domain, were necessary for the interaction with apo-transferrin. Third, monoferric transferrin mutants incapable of binding iron in either the N-terminal or C-terminal lobe still bound Ggly. These findings are consistent with the hypothesis that gastrin peptides bind to nonligand residues within the open cleft in each lobe of transferrin and are involved in iron loading of transferrin in vivo.en
dc.language.isoenen
dc.subject.otherCationsen
dc.subject.otherCross-Linking Reagents.chemistryen
dc.subject.otherEdetic Acid.chemistryen
dc.subject.otherGastrins.chemistry.geneticsen
dc.subject.otherGlycine.chemistry.geneticsen
dc.subject.otherIron.chemistryen
dc.subject.otherIron Chelating Agents.chemistryen
dc.subject.otherMutationen
dc.subject.otherProtein Bindingen
dc.subject.otherTransferrin.chemistryen
dc.titleDefinition of the residues required for the interaction between glycine-extended gastrin and transferrin in vitro.en
dc.typeJournal Articleen
dc.identifier.journaltitleThe FEBS journalen
dc.identifier.affiliationDepartment of Surgery, University of Melbourne, Austin Health, Victoria, Australiaen
dc.identifier.doi10.1111/j.1742-4658.2009.07186.xen
dc.description.pages4866-74en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/19664057en
dc.type.austinJournal Articleen
item.cerifentitytypePublications-
item.languageiso639-1en-
item.grantfulltextnone-
item.openairetypeJournal Article-
item.fulltextNo Fulltext-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
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