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Titolo:
IDENTIFICATION OF A REGION OF THE N-TERMINAL OF THE HUMAN CCKA RECEPTOR ESSENTIAL FOR THE HIGH-AFFINITY INTERACTION WITH AGONIST CCK
Autore:
KENNEDY K; ESCRIEUT C; DUFRESNE M; CLERC P; VAYSSE N; FOURMY D;
Indirizzi:
CHU RANGUEIL,INST LOUIS BUGNARD,INSERM,U151,BIOL & PATHOL DIGEST LAB F-31054 TOULOUSE FRANCE
Titolo Testata:
Biochemical and biophysical research communications
fascicolo: 3, volume: 213, anno: 1995,
pagine: 845 - 852
SICI:
0006-291X(1995)213:3<845:IOAROT>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
PANCREATIC CHOLECYSTOKININ RECEPTOR; FUNCTIONAL EXPRESSION; MOLECULAR-CLONING; CHROMOSOMAL LOCALIZATION; HUMAN BRAIN; A RECEPTOR; BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
20
Recensione:
Indirizzi per estratti:
Citazione:
K. Kennedy et al., "IDENTIFICATION OF A REGION OF THE N-TERMINAL OF THE HUMAN CCKA RECEPTOR ESSENTIAL FOR THE HIGH-AFFINITY INTERACTION WITH AGONIST CCK", Biochemical and biophysical research communications, 213(3), 1995, pp. 845-852

Abstract

The discovery of an N-terminally truncated isoform of the cholecystokinin A subtype (CCKA) receptor exhibiting an atypical pharmacology ledus to study the effects of N-terminal truncation on the pharmacology of the human CCKA receptor. We cloned the cDNA encoding the full CCKA receptor and constructed two truncated forms, one which lacked the first 37 amino acids (CCKAT38) and another which lacked the first 42 amino acids (CCKAT43). Expression of the receptors in COS-7 cells showed that the CCKAT38 receptor displayed a pharmacological profile identicalto that of the full receptor. In contrast, the CCKAT43 receptor did not directly bind agonist CCK9; however,the agonist could compete for binding at low affinity sites. Binding of the partial agonist JMV180 and the antagonist JMV179 were unaffected. These results identify for the first time a part of the N-terminal, close to the membrane, of the human CCKA receptor that is essential for the high affinity interactionwith CCK. (C) 1995 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/10/20 alle ore 15:55:20