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Am J Physiol Heart Circ Physiol (April 25, 2002). doi:10.1152/ajpheart.00890.2001
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Articles in PresS, published online ahead of print April 25, 2002
Am J Physiol Heart Circ Physiol, 10.1152/ajpheart.00890.2001
Submitted on October 12, 2001
Accepted on April 22, 2002

Ca2+-activation and Tension Cost in Myofilaments from Mouse Hearts Ectopically Expressing Enteric {gamma}-Actin

Anne F. Martin1*, Ronald M. Phillips1, Ajit Kumar2, Kelly Crawford2, Abbas Zainab2, James L. Lessard2, Pieter P. deTombe1, and R. John Solaro1

1 Physiology and Biophysics, University of Illinois at Chicago, Chicago, Illinois, USA
2 Developmental Biology, Children's Hospital Medical Center, Cincinnati, Ohio, USA

* To whom correspondence should be addressed. E-mail: afmartin{at}uic.edu.

To determine the significance of actin isoforms in chemo-mechanical coupling, we compared tension and ATPase rate in heart myofilaments from non-transgenic (NTG) and transgenic (TG) mice in which enteric {gamma}-actin replaced greater than 95% of the cardiac{alpha}-actin. Enteric {gamma}-actin was expressed against three backgrounds: mice expressing cardiac {alpha}-actin, heterozygous null cardiac {alpha}-actin mice, and homozygous null cardiac {alpha}-actin mice. There were no differences in maximum Ca2+ activated tension or maximum rate of tension redevelopment after a quick release and rapid re-stretch protocol (ktr) between TG and NTG skinned fiber bundles. However, compared to NTG controls, Ca2+-sensitivity of tension was significantly decreased and economy of tension development was significantly increased in myofilaments from all TG hearts. Shifts in myosin isoform population could not fully account for this increase in the economy of force production of TG myofilaments. Our results indicate that exchange of cardiac {alpha}-actin with an actin isoform differing in only 5 amino acids has a significant impact on both Ca2+ regulation of cardiac myofilaments and the crossbridge cycling rate.




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