Single Mutation (A162H) in Human Cardiac Troponin I Corrects Acid pH Sensitivity of Ca2+-regulated Actomyosin S1 ATPase

descriptionPublicationkeyboard_double_arrow_right Article 01 Sep 2002 English Publisher:Elsevier BVJournal:Journal of Biological Chemistry, volume 277, pages 34,662-34,665 (issn: 0021-9258,

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Authors: Roland, Dargis; Joyce R, Pearlstone; Isabelle, Barrette-Ng; Helena, Edwards; Lawrence B, Smillie;

doi: 10.1074/jbc.c200419200

pmid: 12151382

Single Mutation (A162H) in Human Cardiac Troponin I Corrects Acid pH Sensitivity of Ca2+-regulated Actomyosin S1 ATPase

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Abstract

In contrast to skeletal muscle, the efficiency of the contractile apparatus of cardiac tissue has long been known to be severely compromised by acid pH as in the ischemia of myocardial infarction and other cardiac myopathies. Recent reports (Westfall, M. V., and Metzger, J. M. (2001) News Physiol. Sci. 16, 278-281; Li, G., Martin, A. F., and Solaro, R. J. (2001) J. Mol. Cell. Cardiol. 33, 1309-1320) have indicated that the reduced Ca(2+) sensitivity of cardiac contractility at low pH (

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University of Alberta
Canada

Keywords

Myocardium, Troponin I, Humans, Point Mutation, Calcium, Hydrogen-Ion Concentration, Myosins

11 Research products, page 1 of 2

Cardiac troponin I
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Mutant cardiac troponin I
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TNNI3 protein
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Troponin I, cardiac muscle
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Structure and Dynamics of the Acidosis-Resistant A162H Mutant of the Switch Region of Troponin I Bound to the Regulatory Domain of Troponin C
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