Depressed sliding velocity of isolated cardiac myosin from cardiomyopathic hamsters: Evidence for an alteration in mechanical interaction of actomyosin View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1993-03

AUTHORS

Hiroshi Yamashita, Seiryo Sugiura, Masataka Sata, Takashi Serizawa, Masahiko Iizuka, Teruo Shimmen, Shin-ichi Momomura

ABSTRACT

We measured the relative sliding velocity of cardiomyopathic hamster cardiac myosin on actin cables by using anin vitro motility assay system. We also investigated the relationship between the velocity and both myosin isozyme content and ATPase activity. Cardiac myosin was obtained from cardiomyopathic hamsters (BIO 14.6;B) aged 3,6,9, and 18 months and age-matched controls (F1B;F). Long well-organized actin cables of an alga,Nitellopsis, wer used for the motility assay. Small latex beads (2 μm in diameter) were coated with purified cardiac myosin. When myosin-coated beads were introduced into an algal cell in the presence of Mg-ATP, myosin interacted with actin and dragged the beads. Active movement of the beads along the actin cables was observed under a photomicroscope and the velocity was measured. The velocity was significantly lower in B than in F for each age group (0.47 vs. 0.71 μm/s at the age of 3 months, p<0.05; 0.44 vs. 0.88 μm/s at 6 months, p<0.01; 0.44 vs. 0.67 μm/s at 9 months, p<0.01; 0.35 vs. 0.52 μm/s at 18 months, p<0.05). Both Ca2+-activated ATPase activity and the percentage of α-myosin heavy chain were also lower in B than in F for each age group. When examined for individual specimens, there was a positive correlation between the velocity and both myosin Ca2+-activated ATPase activity (r=0.84) and percentage of α-myosin heavy chain (r=0.83). These data points of both control and cardiomyopathic hamsters were distributed near the regression line obtained from control and thyroxine-treated rabbits reported previously. The present results indicate that the difference in mechanical properties between control and cardiomyopathic cardiac myosin is attributed to isozyme redistribution and not to a qualitative change in each myosin molecule. More... »

PAGES

79-88

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00926857

DOI

http://dx.doi.org/10.1007/bf00926857

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1001658370

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8455590


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