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Titolo:
Association of protein kinase A with AKAP150 facilitates pepsinogen secretion from gastric chief cells
Autore:
Xie, GF; Raufman, JP;
Indirizzi:
Univ Arkansas Med Sci, Dept Internal Med, Div Gastroenterol, Little Rock, AR 72205 USA Univ Arkansas Med Sci Little Rock AR USA 72205 Little Rock, AR 72205 USA Cent Arkansas Vet Healthcare Syst, Little Rock, AR 72205 USA Cent ArkansasVet Healthcare Syst Little Rock AR USA 72205 , AR 72205 USA
Titolo Testata:
AMERICAN JOURNAL OF PHYSIOLOGY-GASTROINTESTINAL AND LIVER PHYSIOLOGY
fascicolo: 4, volume: 281, anno: 2001,
pagine: G1051 - G1058
SICI:
0193-1857(200110)281:4<G1051:AOPKAW>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
GUINEA-PIG STOMACH; ANCHORING PROTEINS; REGULATORY SUBUNIT; ACTIN CYTOSKELETON; C INTERACTION; AKAP79; CALCIUM; TRANSLOCATION; POTENTIATION; PHOSPHATASES;
Keywords:
signal transduction; cAMP; A-kinase anchorin protein 150;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Raufman, JP Univ Arkansas Med Sci, Dept Internal Med, Div Gastroenterol, Mail Slot 567,4301 W Markham St, Little Rock, AR 72205 USA Univ Arkansas MedSci Mail Slot 567,4301 W Markham St Little Rock AR USA 72205
Citazione:
G.F. Xie e J.P. Raufman, "Association of protein kinase A with AKAP150 facilitates pepsinogen secretion from gastric chief cells", AM J P-GAST, 281(4), 2001, pp. G1051-G1058

Abstract

Cross talk between signal transduction pathways augments pepsinogen secretion from gastric chief cells. A-kinase anchoring proteins (AKAPs) associatewith regulatory subunits of protein kinase A (PKA), protein kinase C (PKC), and protein phosphatase 2B (PP2B) and localize this protein complex to specific cell compartments. We determined whether an AKAP-signaling protein complex exists in chief cells and whether this modulates secretion. In Western blots, we identified AKAP150, a rodent homologue of human AKAP79 that coimmunoprecipitates with PKA, PKC, and actin. The association of PKA and PP2B was demonstrated by affinity chromatography. Confocal microscopy revealedcolocalized staining at the cell periphery for AKAP150 and PKC. Ht31, a peptide that competitively displaces PKA from the AKAP complex, but not Ht31P, a control peptide, inhibited 8-Br-cAMP-induced pepsinogen secretion. Ht31did not inhibit secretion that was stimulated by agents whose actions are mediated by PKC and/or calcium. However, Ht31, but not Ht31P, inhibited carbachol- and A23187-stimulated augmentation of secretion from cells preincubated with cholera toxin. These data suggest the existence in chief cells ofa protein complex that includes AKAP150, PKA, PKC, and PP2B. Disruption ofthe AKAP-PKA linkage impairs cAMP-mediated pepsinogen secretion and cross talk between signaling pathways.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 18:06:27