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Titolo:
RELATIONSHIP BETWEEN BIOCHEMICAL AND FUNCTIONAL-EFFECTS OF PROTEIN PHOSPHATASE-1 INHIBITORS IN RABBIT CARDIAC SKINNED FIBERS
Autore:
BERREBIBERTRAND I; BRUMENTLARIGNON N; CAMELIN JC; QUINIOU MJ; BRIL A;
Indirizzi:
SMITHKLINE BEECHAM LABS PHARMACEUT,4 RUE CHESNAY BEAUREGARD,BP 58 F-35760 ST GREGOIRE FRANCE
Titolo Testata:
Journal of Molecular and Cellular Cardiology
fascicolo: 10, volume: 30, anno: 1998,
pagine: 1945 - 1954
SICI:
0022-2828(1998)30:10<1945:RBBAFO>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
SARCOPLASMIC-RETICULUM; OKADAIC ACID; CALYCULIN-A; MONOCLONAL-ANTIBODY; PHOSPHOLAMBAN; PHOSPHORYLATION; SITE; STIMULATION; MECHANISMS; TAUTOMYCIN;
Keywords:
PHOSPHOLAMBAN; SKINNED FIBERS; PROTEIN PHOSPHATASE TYPE 1; TAUTOMYCIN; CALYCULIN A;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
I. Berrebibertrand et al., "RELATIONSHIP BETWEEN BIOCHEMICAL AND FUNCTIONAL-EFFECTS OF PROTEIN PHOSPHATASE-1 INHIBITORS IN RABBIT CARDIAC SKINNED FIBERS", Journal of Molecular and Cellular Cardiology, 30(10), 1998, pp. 1945-1954

Abstract

Tautomycin (TT) and calyculin A (CyA) are inhibitors of protein phosphatases type 1 and 2 (PP1, PP2). Inhibitors 1 and 2 are specific for PP1, which is the major phosphatase functionally relevant in heart and able to dephosphorylate phospholamban (PLB). TT and CyA maintain PLB in its phosphorylated state, thereby increasing calcium uptake. Rabbit saponin skinned fibers (SF) are used to assess calcium load of the sarcoplasmic reticulum (SR). The present investigation aimed to examine the effects of PP1 inhibitors on SR calcium load assessed by caffeine-induced tension transient (CITT), and to correlate this activity with the PLB phosphorylation state. TT and CyA (100 nM) applied during the uptake phase increased the amplitude of CITT by 10 and 20%, respectively, P<0.05 without effect on the release phase. Both CyA and TT were devoid of calcium sensitizing effect when studied on Triton X-100 SF. After skinning procedure, SF were grinded for biochemical studies. SDS-PAGE electrophoresis and immunoblots using a monoclonal PLB antibody showed that cAMP or Ca2+/calmodulin-dependent protein kinases phosphorylated PLB in an additive fashion. Inhibition of PP1 by inhibitor 1, CyAand TT maintained PLB in its phosphorylated state in a dose-dependentmanner. The results of this study in which functional and biochemicalexperiments in cardiac SF were combined demonstrate that strong correlation exists between the phosphorylation-dephosphorylation cycle of PLB and calcium uptake. (C) 1998 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/08/20 alle ore 19:52:26