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Titolo:
EXPERIMENTAL DIABETES IS ASSOCIATED WITH FUNCTIONAL ACTIVATION OF PROTEIN-KINASE C-EPSILON AND PHOSPHORYLATION OF TROPONIN-I IN THE HEART, WHICH ARE PREVENTED BY ANGIOTENSIN-II RECEPTOR BLOCKADE
Autore:
MALHOTRA A; REICH D; REICH D; NAKOUZI A; SANGHI V; GEENEN DL; BUTTRICK PM;
Indirizzi:
UNIV ILLINOIS,SECT CARDIOL MC 787,RM 929,840 S WOOD ST CHICAGO IL 60612 ALBERT EINSTEIN COLL MED,DIV CARDIOL BRONX NY 10467
Titolo Testata:
Circulation research
fascicolo: 6, volume: 81, anno: 1997,
pagine: 1027 - 1033
SICI:
0009-7330(1997)81:6<1027:EDIAWF>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
MYOSIN LIGHT CHAIN-2; ACTOMYOSIN MGATPASE ACTIVITY; RAT VENTRICULAR MYOCYTES; CARDIAC MYOCYTES; ADULT-RAT; PHORBOL ESTER; CA2+-STIMULATED MGATPASE; RECONSTITUTED ACTOMYOSIN; ATPASE ACTIVITY; HIGHLY POTENT;
Keywords:
DIABETES MELLITUS; PROTEIN KINASE C; ANGIOTENSIN II TYPE-1 RECEPTOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
55
Recensione:
Indirizzi per estratti:
Citazione:
A. Malhotra et al., "EXPERIMENTAL DIABETES IS ASSOCIATED WITH FUNCTIONAL ACTIVATION OF PROTEIN-KINASE C-EPSILON AND PHOSPHORYLATION OF TROPONIN-I IN THE HEART, WHICH ARE PREVENTED BY ANGIOTENSIN-II RECEPTOR BLOCKADE", Circulation research, 81(6), 1997, pp. 1027-1033

Abstract

A cardiomyopathy that is characterized by an impairment in diastolic relaxation and a loss of calcium sensitivity of the isolated myofibrilhas been described in chronic diabetic animals and humans. To explorea possible role for protein kinase C (PKC)-mediated phosphorylation of myofibrillar proteins in this process, we characterized the subcellular distribution of the major PKC isoforms seen in the adult heart in cardiocytes isolated from diabetic rats and determined patterns of phosphorylation of the major regulatory proteins, including troponin I (TnI). Rats were made diabetic with a single injection of streptozotocin, and myocardiocytes were isolated and studied 3 to 4 weeks later. In nondiabetic animals, 76% of the PKC epsilon isoform was located in thecytosol and 24% was particulate, whereas in diabetic animals, 55% wascytosolic and 45% was particulate (P<.05). PKC delta, the other majorPKC isoform seen in adult cardiocytes, did not show a change in subcellular localization. In parallel, TnI phosphorylation was increased 5-fold in cardiocytes isolated from the hearts of diabetic animals relative to control animals (P<.01). The change in PKC epsilon distributionand in TnI phosphorylation in diabetic animals was completely prevented by rendering the animals euglycemic with insulin or by concomitant treatment with a specific angiotensin II type-1 receptor (AT(1)) antagonist. Since PKC phosphorylation of TnI has been associated with a loss of calcium sensitivity of intact myofibrils, these data suggest thatangiotensin II receptor-mediated activation of PKC may play a role inthe contractile dysfunction seen in chronic diabetes.

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Documento generato il 07/07/20 alle ore 14:35:28