EFFECT OF CALCIUM ION TRANSPORTED INTO UTERINE MUSCULAR CELL THROUGH CELL MENBRANE ON ACTOMYOSIN-ATPase OF UTERINE MUSCLE OF RAT

Kato, Koichi; Negishi, Toshio; Ueda, Sanae; Arai, Shihoko

doi:10.1540/jsmr1965.5.166

Cited by 2 publications

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“…Discovered in the 1960s (Ebashi 1963; Kato, Negishi et al 1969), vertebrate TnT is a 30~35kDa myofilament protein. Visualized by electron microscopy, TnT anchors troponin complex on the actin-tropomyosin thin filament at ~37 nm intervals (Otsuki, Masaki et al 1967).…”

Section: Introductionmentioning

confidence: 99%

TNNT1, TNNT2, and TNNT3: Isoform genes, regulation, and structure–function relationships

Wei

Jin

2016

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Troponin T (TnT) is a central player in the calcium regulation of actin thin filament function and is essential for the contraction of striated muscles. Three homologous genes have evolved in vertebrates to encode three muscle type-specific TnT isoforms: TNNT1 for slow skeletal muscle TnT, TNNT2 for cardiac muscle TnT, and TNNT3 for fast skeletal muscle TnT. Alternative splicing and posttranslational modifications confer additional structural and functional variations of TnT during development and muscle adaptation to various physiological and pathological conditions. This review focuses on the TnT isoform genes and their molecular evolution, alternative splicing, developmental regulation, structure-function relationships of TnT proteins, posttranslational modifications, and myopathic mutations and abnormal splicing. The goal is to provide a concise summary of the current knowledge and some perspectives for future research and translational applications.

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Section: Introductionmentioning

confidence: 99%