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Titolo:
ATP inhibits insulin-degrading enzyme activity
Autore:
Camberos, MC; Perez, AA; Udrisar, DP; Wanderley, MI; Cresto, JC;
Indirizzi:
CEDIE Endocrinol, Htal Ninos R Gutierrez, RA-1425 Buenos Aires, DF, Argentina CEDIE Endocrinol Buenos Aires DF Argentina RA-1425 s Aires, DF, Argentina Univ Pernambuco, Dept Physiol & Pharmacol, Recife, PE, Brazil Univ Pernambuco Recife PE Brazil Physiol & Pharmacol, Recife, PE, Brazil
Titolo Testata:
EXPERIMENTAL BIOLOGY AND MEDICINE
fascicolo: 4, volume: 226, anno: 2001,
pagine: 334 - 341
SICI:
1535-3702(200104)226:4<334:AIIEA>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
PARTIAL-PURIFICATION; HEPATOMA-CELLS; RAT ADIPOCYTES; DEGRADATION; GLUCAGON; PROTEASE; ASSOCIATION; MECHANISMS; BINDING; INVIVO;
Keywords:
insulin degradation; ATP inhibition; insulin-degrading activity;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Cresto, JC CEDIE Endocrinol, Htal Ninos R Gutierrez, Gallo 1330, RA-1425 Buenos Aires, DF, Argentina CEDIE Endocrinol Gallo 1330 Buenos Aires DF Argentina RA-1425 a
Citazione:
M.C. Camberos et al., "ATP inhibits insulin-degrading enzyme activity", EXP BIOL ME, 226(4), 2001, pp. 334-341

Abstract

We studied the ability of ATP to inhibit in vitro the degrading activity of insulin-degrading enzyme. The enzyme was purified from rat skeletal muscle by successive chromatographic steps. The last purification step showed two bands at 110 and 60 kDa in polyacrylamide gel. The enzyme was characterized by its insulin degradation activity, the substrate competition of unlabeled to labeled insulin, the profile of enzyme inhibitors, and the recognition by a specific antibody, One to 5 mM ATP induced a dose-dependent inhibition of insulin degradation (determined by trichloroacetic acid precipitation and insulin antibody binding). Inhibition by 3 mM adenosine 5' diphosphate, adenosine 5'-monophosphate, guanosine 5'-triphosphate, pyrophosphate, beta-gamma -methyleneadenosine 5'-triphosphate, adenosine 5'-O-(3 thiotriphosphate), and dibutiryl cyclic adenosine 5'-monophosphate was 74%, 4%, 38%, 46%, 65%, 36%, and 0%, respectively, of that produced by 3 mM ATP, Kinetic analysis of ATP inhibition suggested an allosteric effect as the plot of 1/v(insulin degradation) versus ATP concentration was not linear and the Hillcoefficient was more than 1 (1.51 and 2.44), The binding constant for allosteric inhibition was K-i(T) = 1.5 x 10(-7) M showing a decrease of enzyme affinity induced by ATP. We conclude that ATP has an inhibitory effect on the insulin degradation activity of the enzyme.

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Documento generato il 09/12/19 alle ore 14:51:24