Strongly binding myosin crossbridges regulate loaded shortening and power output in cardiac myocytes

Circulation Research

Volumn 87, Issue 9, 2000, Pages 768-773

  McDonald, Kerry S ^a   Moss, Richard L ^b  

^a University of Missouri   (United States)

^b UNIVERSITY OF WISCONSIN SCHOOL OF MEDICINE AND PUBLIC HEALTH   (United States)

Author keywords

Cardiac myocytes; Myosin; Power output

Indexed keywords

CALCIUM; MYOSIN; N ETHYLMALEIMIDE;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; HEART MUSCLE CELL; HEART OUTPUT; HEART STROKE VOLUME; HEART VENTRICLE EJECTION; HEART VENTRICLE PRESSURE; HEART WORK; NONHUMAN; PRIORITY JOURNAL; RAT; REGULATORY MECHANISM; THIN FILAMENT; VELOCITY;

EID: 0034721806     PISSN: 00097330     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.RES.87.9.768     Document Type: Article

References (26)

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4. Regulation of contraction in striated muscle
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7. 2+ sensitizers
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10. Altered interactions among thin filament proteins modulate cardiac function
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13. Cooperative turning on of myosin subfragment 1 ATPase by the Tn-Tm-Actin complex
14. Influence of a strong-binding myosin analog on calcium-sensitive mechanical properties of skinned skeletal muscle fibers
15. 2+ activation of rat ventricular myocytes
16. Sarcomere length-tension relations of frog skinned muscle fibres during calcium activation at short lengths
17. 2+-activated ventricular muscle of the guinea pig
18. Comparison of the effects of different inotropic interventions of force, velocity, and power in rabbit myocardium
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20. Effects of calcium on shortening velocity in frog chemically skinned atrial myocytes and in mechanically disrupted ventricular myocardium from rat
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24. Passive tension in cardiac muscle: Contribution of collagen, titin, microtubules, and intermediate filaments
25. 2+ regulation of mechanical properties of striated muscle: Mechanistic studies using extraction and replacement of regulatory proteins