Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/9203
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dc.contributor.authorRorison, K Aen
dc.contributor.authorYang, Zen
dc.contributor.authorBaldwin, Graham Sen
dc.date.accessioned2015-05-15T22:12:29Z
dc.date.available2015-05-15T22:12:29Z
dc.date.issued2000-01-24en
dc.identifier.citationEuropean Journal of Pharmacology; 388(1): 9-15en
dc.identifier.govdoc10657541en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/9203en
dc.description.abstractA 78 kDa gastrin-binding protein is a likely target for the anti-proliferative effects of the cholecystokinin (CCK) receptor antagonists D,L-4-benzamido-N,N-dipropylglutaramic acid (proglumide) and N-4-chlorobenzoyl-L-tryptophan (benzotript) on colorectal carcinoma cell lines [Baldwin, G.S., 1994. Antiproliferative gastrin/cholecystokinin receptor antagonists target the 78-kDa gastrin-binding protein. Proc. Natl. Acad. Sci. USA 91, 7593-7597.]. Definition of the physiological role of the gastrin-binding protein has been hampered by the very low affinity of benzotript for the gastrin-binding protein. Benzotript analogues were therefore tested for their ability to inhibit the binding of iodinated gastrin to the gastrin-binding protein. The affinity of the most potent analogue (the D-isomer of benzotript, CR 665) was similar to the value reported previously for the L-isomer. In order to isolate more potent binding inhibitors, several selective CCK receptor antagonists were also tested as inhibitors of the binding of gastrin to the gastrin-binding protein. The affinity of the most potent binding inhibitor PD 149164 (benzenebutanoic acid, 4-fluoro-!b/-[[3-(1H-indol-3-yl)-2-methyl-1-oxo-2-[[(tricyclo-[3.3 .1. 1(3,7)]dec-2-yloxy)carbonyl]amino]propyl]amino]-, [R-(R*,S*)]-) was approximately 10-fold higher than the L-isomer of benzotript. PD 149164 may serve as the lead compound for the future development of more potent and selective gastrin-binding protein inhibitors.en
dc.language.isoenen
dc.subject.otherAdamantane.analogs & derivatives.pharmacologyen
dc.subject.otherAnimalsen
dc.subject.otherAnti-Ulcer Agents.metabolism.pharmacologyen
dc.subject.otherBenzamides.metabolism.pharmacologyen
dc.subject.otherCarrier Proteins.antagonists & inhibitors.isolation & purification.metabolismen
dc.subject.otherCells, Cultureden
dc.subject.otherFatty Acids.metabolismen
dc.subject.otherFibroblasts.metabolismen
dc.subject.otherGastrins.metabolismen
dc.subject.otherHumansen
dc.subject.otherIndoles.pharmacologyen
dc.subject.otherMitochondria.metabolismen
dc.subject.otherMitochondrial Trifunctional Proteinen
dc.subject.otherMultienzyme Complexesen
dc.subject.otherOxidation-Reductionen
dc.subject.otherProglumide.metabolism.pharmacologyen
dc.subject.otherProtein Bindingen
dc.subject.otherReceptors, Cholecystokinin.agonists.antagonists & inhibitorsen
dc.subject.otherSwineen
dc.titleAffinity of cholecystokinin receptor antagonists for the gastrin-binding protein.en
dc.typeJournal Articleen
dc.identifier.journaltitleEuropean Journal of Pharmacologyen
dc.identifier.affiliationDepartment of Surgery, University of Melbourne, Austin and Repatriation Medical Centre, Austin Campus, Studley Rd., Heidelberg, Australiaen
dc.description.pages9-15en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/10657541en
dc.type.austinJournal Articleen
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextNo Fulltext-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairetypeJournal Article-
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