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Titolo:
Regulation of smooth muscle actin-myosin interaction and force by calponin
Autore:
Winder, SJ; Allen, BG; Clement-Chomienne, O; Walsh, MP;
Indirizzi:
Univ Calgary, Smooth Muscle Res Grp, Calgary, AB T2N 4N1, Canada Univ Calgary Calgary AB Canada T2N 4N1 s Grp, Calgary, AB T2N 4N1, Canada Univ Calgary, Dept Biochem & Mol Biol, Calgary, AB T2N 4N1, Canada Univ Calgary Calgary AB Canada T2N 4N1 Biol, Calgary, AB T2N 4N1, Canada
Titolo Testata:
ACTA PHYSIOLOGICA SCANDINAVICA
fascicolo: 4, volume: 164, anno: 1998,
pagine: 415 - 426
SICI:
0001-6772(199812)164:4<415:ROSMAI>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE-C; LIGHT-CHAIN PHOSPHORYLATION; F-ACTIN; MOLECULAR-CLONING; THIN-FILAMENTS; ECHINOCOCCUS-GRANULOSUS; INTRACELLULAR CALCIUM; ACTOMYOSIN MGATPASE; FUNCTIONAL DOMAINS; CA2+ SENSITIVITY;
Keywords:
actin; calcium; calmodulin; calponin; myosin; protein kinase C; smooth muscle;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
119
Recensione:
Indirizzi per estratti:
Indirizzo: Walsh, MP UnivCanadary, Smooth Muscle Res Grp, 3300 Hosp Dr NW, Calgary, AB T2N 4N1, Univ Calgary 3300 Hosp Dr NW Calgary AB Canada T2N 4N1 T2N 4N1,
Citazione:
S.J. Winder et al., "Regulation of smooth muscle actin-myosin interaction and force by calponin", ACT PHYSL S, 164(4), 1998, pp. 415-426

Abstract

Smooth muscle contraction is regulated primarily by the reversible phosphorylation of myosin triggered by an increase in sarcoplasmic tree Ca2+ concentration ([Ca2+](i)). Contraction can, however, be modulated by other signal transduction pathways, one of which involves the thin filament-associatedprotein calponin. The hi (basic) isoform of calponin binds to actin with high affinity and is expressed specifically in smooth muscle at a molar ratio to actin of 1 : 7. Calponin inhibits (i) the actin-activated MgATPase activity of smooth muscle myosin (the cross-bridge cycling rate) via its interaction with actin, (ii) the movement of actin filaments over immobilized myosin in the in vitro motility assay, and (iii) force development or shortening velocity in permeabilized smooth muscle strips and single cells. These inhibitory effects of calponin can be alleviated by protein kinase C (PKC)catalysed phosphorylation and restored following dephosphorylation by a type2A phosphatase. Three physiological roles of calponin can be considered based on its in vitro functional properties: (i) maintenance of relaxation atresting [Ca2+]i, (ii) energy conservation during prolonged contractions, and (iii) Ca2+-independent contraction mediated by phosphorylation of calponin by PKC epsilon, a Ca2+-independent isoenzyme of PKC.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 14:30:14