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Titolo:
ENDOGENOUS TYPE-II CGMP-DEPENDENT PROTEIN-KINASE EXISTS AS A DIMER INMEMBRANES AND CAN BE FUNCTIONALLY DISTINGUISHED FROM THE TYPE-I ISOFORMS
Autore:
VAANDRAGER AB; EDIXHOVEN M; BOT AGM; KROOS MA; JARCHAU T; LOHMANN S; GENIESER HG; DEJONGE HR;
Indirizzi:
ERASMUS UNIV ROTTERDAM,FAC MED,DEPT BIOCHEM,CARDIOVASC RES INST COEUR,POB 1738 NL-3000 DR ROTTERDAM NETHERLANDS ERASMUS UNIV ROTTERDAM,FAC MED & HLTH SCI,DEPT CLIN GENET NL-3000 DR ROTTERDAM NETHERLANDS MED UNIV CLIN WURZBURG,LAB CLIN BIOCHEM D-97080 WURZBURG GERMANY BIOLOG LIFE SCI INST D-28199 BREMEN GERMANY
Titolo Testata:
The Journal of biological chemistry
fascicolo: 18, volume: 272, anno: 1997,
pagine: 11816 - 11823
SICI:
0021-9258(1997)272:18<11816:ETCPEA>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSMEMBRANE CONDUCTANCE REGULATOR; INTESTINAL ELECTROLYTE TRANSPORT; STABLE ENTEROTOXIN RECEPTOR; GUANYLYL CYCLASE-C; CYCLIC-GMP; CYSTIC-FIBROSIS; DIARRHEAL DISEASE; EXPRESSION; ACTIVATION; RELAXATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
A.B. Vaandrager et al., "ENDOGENOUS TYPE-II CGMP-DEPENDENT PROTEIN-KINASE EXISTS AS A DIMER INMEMBRANES AND CAN BE FUNCTIONALLY DISTINGUISHED FROM THE TYPE-I ISOFORMS", The Journal of biological chemistry, 272(18), 1997, pp. 11816-11823

Abstract

In mammalian tissues two types of cGMP-dependent protein kinase (cGK)have been identified. In contrast to the dimeric cGK I, cGK II purified from pig intestine was shown previously to behave as a monomer. However, recombinant rat cGK II was found to have hydrody namic parameters indicative of a homodimer. Chemical cross-linking studies showed that pig cGK II in intestinal membranes has a dimeric structure as well. However, after purification, cGK II was found to be partly proteolyzedinto C-terminal monomeric fragments. Phosphorylation studies in rat intestinal brush borders revealed that the potency of cGMP analogs to stimulate or inhibit native cGK II in vitro (i.e. 8-(4-chlorophenylthio)-cGMP > cGMP > beta-phenyl-1,N-2-etheno-8-bromoc-GMP > beta-phenyl-1,N-2-etheno-cGMP and R-p-8-(4-chlorophenylthio)-cGMPs > R-p-beta-phenyl-1,N-2-etheno-8-bromo-cGMPs, respectively) correlated well with their potency to stimulate or inhibit cGK II-mediated Cl- secretion across intestinal epithelium but differed strikingly from their potency to affect cGK I activity. These data show that the N terminus of cGK II is involved in dimerization and that endogenous cGK II displays a distinctactivation/inhibition profile with respect to cGMP analogs, which permits a pharmacological dissection between cGK II- and cGK I-mediated physiological processes.

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Documento generato il 30/09/20 alle ore 09:29:30