Literature DB >> 7060747

Chemical Energetics of contraction in mammalian smooth muscle.

T M Butler, M J Siegman.   

Abstract

Measurements of high-energy phosphate utilization during isometric tetanic contractions were made on a rabbit taenia coli preparation that had been treated so that respiration and glycolysis were blocked without altering the mechanical response to the muscle. At 18 C the first sign of high-energy phosphate usage after electrical stimulation was a net breakdown of ATP with a subsequent net resynthesis when the rate of phosphocreatine breakdown was high. The average rate of chemical energy usage was more than four times as high during the period of initial force development compared to that during maximum force maintenance. This initial high rate of energy usage was not due only to the internal work done against the series elasticity during force development. Comparison of energetics and mechanics data for the rabbit taenia coli and frog sartorius showed that smooth muscle was 100-fold more economical in maintaining isometric force and probably had a cross-bridge cycle time that was about 150-fold slower. The rate of energy usage during relaxation from an isometric tetanus in smooth muscle was very low, and force was exerted with a lower expenditure of energy during relaxation than during maximum force maintenance. Phosphorylation of the 20,000-dalton light chain of myosin occurred to the extent of 32% during a maximally activated isometric tetanus and was not proportional to the rate of energy usage during different stages of the tetanus. During isometric relaxation, the degree of phosphorylation, rate of energy usage, and active state all decreased more quickly than did active force output.

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Year:  1982        PMID: 7060747

Source DB:  PubMed          Journal:  Fed Proc        ISSN: 0014-9446


  6 in total

1.  Creatine kinase activity in normal and hypertrophied rabbit urinary bladder tissue (following partial outlet obstruction).

Authors:  R M Levin; N Haugaard; S S Levin; A J Wein
Journal:  Mol Cell Biochem       Date:  1991-08-14       Impact factor: 3.396

2.  Regulation of isometric force and isotonic shortening velocity by phosphorylation of the 20,000 dalton myosin light chain of rat uterine smooth muscle.

Authors:  J R Haeberle; J W Hott; D R Hathaway
Journal:  Pflugers Arch       Date:  1985-02       Impact factor: 3.657

3.  Kinetic model for isometric contraction in smooth muscle on the basis of myosin phosphorylation hypothesis.

Authors:  S Kato; T Osa; T Ogasawara
Journal:  Biophys J       Date:  1984-07       Impact factor: 4.033

4.  Deletion of SM-B, the high ATPase isoform of myosin, upregulates the PKC-mediated signal transduction pathway in murine urinary bladder smooth muscle.

Authors:  Joseph A Hypolite; Shaohua Chang; Edward LaBelle; Gopal J Babu; Muthu Periasamy; Alan J Wein; Samuel Chacko
Journal:  Am J Physiol Renal Physiol       Date:  2008-12-03

5.  Skinned smooth muscle: time course of force and ATPase activity during contraction cycle.

Authors:  K Güth; M Gagelmann; J C Rüegg
Journal:  Experientia       Date:  1984-02-15

Review 6.  Regulation of actomyosin and contraction in smooth muscle.

Authors:  S Chacko; P A Longhurst
Journal:  World J Urol       Date:  1994       Impact factor: 4.226

  6 in total

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