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Titolo:
TROPONIN-T - GENETICS, PROPERTIES AND FUNCTION
Autore:
PERRY SV;
Indirizzi:
UNIV BIRMINGHAM,SCH MED,DEPT PHYSIOL BIRMINGHAM B15 2TT W MIDLANDS ENGLAND
Titolo Testata:
Journal of muscle research and cell motility
fascicolo: 6, volume: 19, anno: 1998,
pagine: 575 - 602
SICI:
0142-4319(1998)19:6<575:T-GPAF>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
SKELETAL-MUSCLE TROPONIN; PROTEIN-KINASE-C; ACTOMYOSIN MGATPASE ACTIVITY; METAL-BINDING CLUSTER; CHICKEN BREAST MUSCLE; AMINO-ACID SEQUENCES; ALPHA-TROPOMYOSIN; STRIATED-MUSCLE; THIN FILAMENT; HYPERTROPHIC CARDIOMYOPATHY;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
195
Recensione:
Indirizzi per estratti:
Citazione:
S.V. Perry, "TROPONIN-T - GENETICS, PROPERTIES AND FUNCTION", Journal of muscle research and cell motility, 19(6), 1998, pp. 575-602

Abstract

Troponin T (TnT) is present in striated muscle of vertebrates and invertebrates as a group of homologous proteins with molecular weights usually in the 31-36 kDa range. It occupies a unique role in the regulatory protein system in that it interacts with TnC and TnI of the troponin complex and the proteins of the myofibrillar thin filament, tropomyosin and actin. In the myofibril the molecule is about 18 nm long and for much its length interacts with tropomyosin. The ability of TnT to form a complex with tropomyosin is responsible for locating the troponin complex with a periodicity of 38.5 nm along the thin filament of the myofibril. In addition to its structural role, TnT has the importantfunction of transforming the TnI-TnC complex into a system, the inhibitory activity of which, on the tropomyosin-actomyosin MgATPase of themyofibril, becomes sensitive to calcium ions. Different genes controlthe expression of TnT in fast skeletal, slow skeletal and cardiac muscles. In all muscles, and particularly in fast skeletal, alternative splicing of mRNA produces a series of isoforms in a developmentally regulated manner. In consequence TnT exists in marry more isoforms than any of the other thin filament proteins, the TnT superfamily. Despite the general homology of TnT isoforms, this alternative splicing leads to variable regions close to the N- and C-termini. As the isoforms havelightly different effects on the calcium sensitivity of the actomyosin MgATPase, modulation of the contractile response to calcium can occur during development and in different muscle types. TnT has recently aroused clinical interest in its potential for detecting myocardial damage and the association of mutations in the cardiac isoform with hypertrophic cardiomyopathy. (C) Chapman & Hall Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 11:16:01