Literature DB >> 1804969

Heat production in chemically skinned smooth muscle of guinea-pig taenia coli.

P Lönnbro1, P Hellstrand.   

Abstract

1. The rate of heat production of chemically skinned guinea-pig taenia coli smooth muscle at 25 degrees C was measured using microcalorimetric techniques. 2. Muscle strips were mounted isometrically and incubated in solutions containing MgATP (3.2 mM) and phosphocreatine (PCr, 12 mM), pH 6.9. Activation was obtained by the injection of Ca2+ into the sample compartment of the calorimeter. 3. The heat production rate of the resting preparation (pCa 9) was 0.40 +/- 0.03 mW g-1 wet weight (n = 23). During maximal activation (pCa 4.8) the heat rate increased to 1.12 +/- 0.07 mW g-1 (mean +/- S.E.M., n = 15). With stepwise increase in [Ca2+] from pCa 9 to 4.8 the energetic cost of force maintenance tended to increase at higher [Ca2+]. 4. After activation by Ca2+, the heat production rate reached its maximum while force was still increasing. 5. Changing ionic strength from 90 to 150 mM had no effect on either basal or activated heat rate. Oligomycin, amphotericin B and the adenylate kinase inhibitor Ap5A had no effect on the basal heat rate. 6. Exchanging ATP in the incubation medium for inosine triphosphate (ITP) reduced the force and heat production after injection of Ca2+. The basal heat production was not lowered when ATP was exchanged for ITP. 7. The observed enthalpy change for PCr splitting at 25 degrees C (pH 6.9, ionic strength 90 mM) was -28 +/- 3 kJ mol-1 (mean +/- S.E.M., n = 9). After correction for the phosphate equilibrium, buffer reactions, and Mg2+ binding to PCr and HPO42-, the net enthalpy change is calculated to be -39 +/- 3 kJ mol-1. 8. Heat production in the skinned smooth muscle consists of one basal component present in relaxed muscle, and one component associated with contraction. The nature of the basal heat production is unclear but does not seem to involve turnover of phosphate on the myosin light chains. The increase in the energetic tension cost with increasing activation by Ca2+ has implications for the understanding of the contractile mechanism in smooth muscle.

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Year:  1991        PMID: 1804969      PMCID: PMC1180158          DOI: 10.1113/jphysiol.1991.sp018714

Source DB:  PubMed          Journal:  J Physiol        ISSN: 0022-3751            Impact factor:   5.182


  30 in total

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Authors:  H Kühn; A Tewes; M Gagelmann; K Güth; A Arner; J C Rüegg
Journal:  Pflugers Arch       Date:  1990-07       Impact factor: 3.657

8.  Cross-bridge behaviour in skinned smooth muscle of the guinea-pig taenia coli at altered ionic strength.

Authors:  H Arheden; A Arner; P Hellstrand
Journal:  J Physiol       Date:  1988-09       Impact factor: 5.182

9.  Superprecipitation of gizzard actomyosin, and tension in gizzard muscle skinned fibers in the presence of nucleotides other than ATP.

Authors:  P Cassidy; W G Kerrick
Journal:  Biochim Biophys Acta       Date:  1982-07-12

10.  Myoplasmic free calcium concentration reached during the twitch of an intact isolated cardiac cell and during calcium-induced release of calcium from the sarcoplasmic reticulum of a skinned cardiac cell from the adult rat or rabbit ventricle.

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Journal:  J Gen Physiol       Date:  1981-11       Impact factor: 4.086

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