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Titolo:
HEAT-STABLE ENTEROTOXIN ACTIVATION OF IMMUNOPURIFIED GUANYLYL CYCLASE-C - MODULATION BY ADENINE-NUCLEOTIDES
Autore:
VAANDRAGER AB; VANDERWIEL E; DEJONGE HR;
Indirizzi:
ERASMUS UNIV ROTTERDAM,FAC MED,DEPT BIOCHEM,POB 1738 3000 DR ROTTERDAM NETHERLANDS
Titolo Testata:
The Journal of biological chemistry
fascicolo: 26, volume: 268, anno: 1993,
pagine: 19598 - 19603
SICI:
0021-9258(1993)268:26<19598:HEAOIG>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
INTESTINAL ELECTROLYTE TRANSPORT; PROTEIN-KINASE; DIARRHEAL DISEASE; HUMAN RECEPTOR; EXPRESSION; MEMBRANES; BINDING; DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
A.B. Vaandrager et al., "HEAT-STABLE ENTEROTOXIN ACTIVATION OF IMMUNOPURIFIED GUANYLYL CYCLASE-C - MODULATION BY ADENINE-NUCLEOTIDES", The Journal of biological chemistry, 268(26), 1993, pp. 19598-19603

Abstract

We studied the activation and inactivation of recombinant guanylyl cyclase (GC) C stably expressed in human kidney 293 cells. Activation ofGC-C by heat-stable enterotoxin (STa), Cd2+, hemin, or the detergent Triton X-100 was followed by a rapid inactivation of the enzyme. Adenine nucleotides were found to prevent the inactivation process in native membranes, as well as following enzyme solubilization and immunopurification. Inactivation of GC-C was not associated with dephosphorylation. However, the phosphorylation of GC-C was promoted by phorbol esters, known activators of protein kinase C. The activation of purified GC-C by STa required the presence of a nonspecific factor as exemplifiedby bovine serum albumin. When immunopurified GC-C, stabilized by ATP and bovine serum albumin, was analyzed by SDS-polyacrylamide gel electrophoresis under nonreducing conditions, proteins with almost twice the molecular mass (220 and 245 kDa) of the monomer were observed. The mobility of these high M(r) GC-C forms was reduced by STa, suggesting that STa induces a conformation change in a preexisting GC-C dimer. These results indicate that ATP interacts directly with GC-C, stabilizingits active conformation and that the activation of GC-C may occur in the absence of other specific regulatory factors.

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Documento generato il 30/09/20 alle ore 08:32:52