Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/11106
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dc.contributor.authorPatel, Oneelen
dc.contributor.authorMarshall, Kathryn Men
dc.contributor.authorBramante, Giannien
dc.contributor.authorBaldwin, Graham Sen
dc.contributor.authorShulkes, Arthuren
dc.date.accessioned2015-05-16T00:41:37Z
dc.date.available2015-05-16T00:41:37Z
dc.date.issued2010-08-19en
dc.identifier.citationRegulatory Peptides 2010; 165(2-3): 224-31en
dc.identifier.govdoc20727916en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/11106en
dc.description.abstractProgastrin is processed to a number of peptides including glycine-extended gastrin, amidated gastrin and the C-terminal flanking peptide (CTFP). Progastrin and gastrin-gly are pro-proliferative and anti-apoptotic in gastric and colorectal cancer cell lines. The CTFP is a major form of progastrin in the stomach and colon and stimulates proliferation. However the effect of CTFP on apoptosis has not been examined. Using the human gastric carcinoma cell line AGS we show that CTFP attenuates apoptosis through a PI3-kinase pathway by stimulating the phosphorylation of Akt leading to sustained increases in the concentrations of Bcl-xL and phosphorylated Bad protein and by reducing caspase 3 activity. The anti-apoptotic effect represents an important potential mechanism for the growth promoting action of CTFP.en
dc.language.isoenen
dc.subject.otherApoptosis.drug effectsen
dc.subject.otherBlotting, Westernen
dc.subject.otherCell Line, Tumoren
dc.subject.otherCell Survival.drug effectsen
dc.subject.otherFlow Cytometryen
dc.subject.otherGastrins.chemistryen
dc.subject.otherHumansen
dc.subject.otherPeptide Fragments.chemistry.pharmacologyen
dc.subject.otherPhosphatidylinositol 3-Kinases.metabolismen
dc.subject.otherProtein Precursors.chemistryen
dc.subject.otherSignal Transduction.drug effectsen
dc.titleThe C-terminal flanking peptide (CTFP) of progastrin inhibits apoptosis via a PI3-kinase-dependent pathway.en
dc.typeJournal Articleen
dc.identifier.journaltitleRegulatory peptidesen
dc.identifier.affiliationDepartment of Surgery, University of Melbourne Austin Health, Heidelberg, Victoria, Australia 3084, Australiaen
dc.identifier.doi10.1016/j.regpep.2010.08.005en
dc.description.pages224-31en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/20727916en
dc.type.austinJournal Articleen
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.grantfulltextnone-
item.openairetypeJournal Article-
item.fulltextNo Fulltext-
item.cerifentitytypePublications-
item.languageiso639-1en-
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