Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/9277
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dc.contributor.authorBaldwin, Graham Sen
dc.contributor.authorHollande, Fen
dc.contributor.authorYang, Zen
dc.contributor.authorKarelina, Yen
dc.contributor.authorPaterson, Aen
dc.contributor.authorStrang, Ren
dc.contributor.authorFourmy, Den
dc.contributor.authorNeumann, Gen
dc.contributor.authorShulkes, Arthuren
dc.date.accessioned2015-05-15T22:18:26Z
dc.date.available2015-05-15T22:18:26Z
dc.date.issued2000-12-11en
dc.identifier.citationThe Journal of Biological Chemistry 2000; 276(11): 7791-6en
dc.identifier.govdoc11113148en
dc.identifier.otherPUBMEDen
dc.identifier.urihttps://ahro.austin.org.au/austinjspui/handle/1/9277en
dc.description.abstractEvidence is accumulating that gastrin precursors may act as growth factors for the colonic mucosa in vivo. The aims of this study were to prepare recombinant human progastrin(6-80) and to investigate its structure and biological activities in vitro. Human progastrin(6-80) was expressed in Escherichia coli as a glutathione S-transferase fusion protein. After thrombin cleavage progastrin(6-80) was purified by reverse phase high pressure liquid chromatography and characterized by radioimmunoassay, amino acid sequencing, and mass spectrometry. Assays for metal ions by atomic emission spectroscopy revealed the presence of a single tightly bound calcium ion. Progastrin(6-80) at concentrations in the pm to nm range stimulated proliferation of the conditionally transformed mouse colon cell line YAMC. The observations that progastrin(6-80) did not bind to either the cholecystokinin (CCK)-A or the gastrin/CCK-B receptor expressed in COS cells and that antagonists selective for either receptor did not reverse the proliferative effects of progastrin(6-80) suggested that progastrin(6-80) stimulated proliferation independently of either the CCK-A or the gastrin/CCK-B receptor. We conclude that recombinant human progastrin(6-80) is biologically active and contains a single calcium ion. With the exception of the well known zinc-dependent polymerization of insulin and proinsulin, this is the first report of selective, high affinity binding of metal ions to a prohormone.en
dc.language.isoenen
dc.subject.otherAmino Acid Sequenceen
dc.subject.otherAnimalsen
dc.subject.otherCOS Cellsen
dc.subject.otherCalcium.metabolismen
dc.subject.otherCell Division.drug effectsen
dc.subject.otherGastrins.chemistry.isolation & purification.physiologyen
dc.subject.otherHumansen
dc.subject.otherMolecular Sequence Dataen
dc.subject.otherPeptide Fragments.chemistryen
dc.subject.otherProtein Precursors.chemistry.isolation & purification.physiologyen
dc.subject.otherRecombinant Proteins.chemistry.isolation & purification.pharmacologyen
dc.subject.otherSincalide.metabolismen
dc.titleBiologically active recombinant human progastrin(6-80) contains a tightly bound calcium ion.en
dc.typeJournal Articleen
dc.identifier.journaltitleThe Journal of biological chemistryen
dc.identifier.affiliationUniversity Department of Surgery, Austin Hospital, Heidelberg, Victoria 3084, Australiaen
dc.identifier.doi10.1074/jbc.M009985200en
dc.description.pages7791-6en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/11113148en
dc.type.austinJournal Articleen
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.fulltextNo Fulltext-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairetypeJournal Article-
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