Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/10006
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dc.contributor.authorDumesny, Chelseaen
dc.contributor.authorPatel, Oneelen
dc.contributor.authorLachal, Shamilahen
dc.contributor.authorGiraud, Andrew Sen
dc.contributor.authorBaldwin, Graham Sen
dc.contributor.authorShulkes, Arthuren
dc.date.accessioned2015-05-15T23:19:00Z
dc.date.available2015-05-15T23:19:00Z
dc.date.issued2005-10-13en
dc.identifier.citationEndocrinology 2005; 147(1): 502-9en
dc.identifier.govdoc16223866en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/10006en
dc.description.abstractGastrin-releasing peptide (GRP) has a widespread distribution and multiple stimulating effects on endocrine and exocrine secretions and metabolism. The prohormone for GRP (ProGRP, 125 amino acids) is processed to the amidated, biologically active end products GRP(1-27) and GRP(18-27). Amidated forms of GRP are putative autocrine or paracrine growth factors in a number of cancers including colorectal cancer. However, the potential role and biological activity of proGRP has not been investigated. Using a newly developed antisera directed to the N terminus of human proGRP, proGRP immunoreactivity was detected in all of the endometrial, prostate, and colon cancer cell lines tested and in nine of 10 resected colorectal carcinomas. However, no amidated forms were detected, suggesting an attenuation of processing in tumors. Recombinant proGRP was expressed as a His-tag fusion protein and purified by metal affinity chromatography and HPLC. ProGRP stimulated proliferation of a colon cancer cell line and activated MAPK, but unlike GRP(18-27)amide had no effect on inositol phosphate production. ProGRP did not compete with iodinated bombesin in binding assays on Balb-3T3 cells transfected with the known GRP receptors, GRP-R or BRS-3. We conclude that proGRP is present in a number of cancer cell lines and in resected colorectal tumors and is biologically active. Our results suggest that antagonists to GRP precursors rather than the amidated end products should be developed as a treatment for colorectal and other cancers that express proGRP-derived peptides.en
dc.language.isoenen
dc.subject.otherAmino Acid Sequenceen
dc.subject.otherAnimalsen
dc.subject.otherCell Line, Tumoren
dc.subject.otherCloning, Molecularen
dc.subject.otherFemaleen
dc.subject.otherGene Expression Regulationen
dc.subject.otherHumansen
dc.subject.otherMaleen
dc.subject.otherMass Spectrometryen
dc.subject.otherMolecular Sequence Dataen
dc.subject.otherPeptide Fragments.chemistry.genetics.metabolismen
dc.subject.otherPeptides.chemistry.genetics.metabolismen
dc.subject.otherRecombinant Fusion Proteins.metabolismen
dc.subject.otherRecombinant Proteins.chemistry.genetics.metabolismen
dc.titleSynthesis, expression and biological activity of the prohormone for gastrin releasing peptide (ProGRP).en
dc.typeJournal Articleen
dc.identifier.journaltitleEndocrinologyen
dc.identifier.affiliationDepartment of Surgery, Austin Health, University of Melbourne, Heidelberg, Victoria 3084, Australiaen
dc.identifier.doi10.1210/en.2005-0574en
dc.description.pages502-9en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/16223866en
dc.type.austinJournal Articleen
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypeJournal Article-
item.grantfulltextnone-
item.cerifentitytypePublications-
item.fulltextNo Fulltext-
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