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  • Title: Troponin I and troponin T interact with troponin C to produce different Ca2+-dependent effects on actin-tropomyosin filament motility.
    Author: Bing W, Fraser ID, Marston SB.
    Journal: Biochem J; 1997 Oct 15; 327 ( Pt 2)(Pt 2):335-40. PubMed ID: 9359398.
    Abstract:
    We have developed an in vitro motility assay to make a detailed quantitative analysis of Ca2+ control of skeletal-muscle troponin-tropomyosin control of actin-filament movement over immobilized myosin. Ca2+ regulates both filament velocity and the fraction of filaments that are motile. We have demonstrated that the two effects are due to separate interactions of troponin C with troponin I and troponin T. When 64nM of the complex actin-tropomyosin-troponin I-troponin C was added at pCa 5, more than 80% of filaments were moving and their velocity did not change. At pCa 9, more than 20% of the filaments were moving. When 20nM of the complex actin-tropomyosin-troponin T+troponin I+troponin C was added at pCa 5, filament motility remained high, whereas velocity increased. The 30% increase in velocity observed when troponin T was present was also observed when heavy meromyosin fragment 1 labelled with N-ethylmaleimide (NEM S-1) was added after actin-tropomyosin filaments. The NEM S-1 effect was not additive with the troponin T-dependent velocity increase. The pattern of motile behaviour is characteristic of myosin on silicone-treated glass and different from the behaviour on nitrocellulose-coated glass.
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