Literature DB >> 8109327

Role of parvalbumin in relaxation of frog skeletal muscle.

T T Hou1, J D Johnson, J A Rall.   

Abstract

Experiments were done to test the hypothesis that parvalbumin (PA) promotes relaxation in frog skeletal muscle. Single fibers and purified PA from R. temporaria skeletal muscle were used to determine the relationship between Ca2+ and Mg2+ dissociation rates from PA and changes in relaxation rate as a function of isometric tetanus duration at 0 degrees C. Relaxation rate slows as a function of tetanus duration with a rate constant of 1.18 s-1. Recovery of relaxation rate after a prolonged tetanus exhibits a rate constant of 0.12 s-1. Dissociation rate constants for Mg2+ and Ca2+ from purified PA are 0.93 s-1 and 0.19 s-1, respectively. Thus rates of slowing and recovery of relaxation rate may be controlled by Mg2+ and Ca2+ dissociation from PA, respectively. The influence of temperature on relaxation rate and on Ca2+ and Mg2+ dissociation rates from purified PA also was examined. The magnitude of slowing of relaxation rate with increasing tetanus duration, relative to the final, steady value of relaxation rate, is greater at 0 than at 10 degrees C. In the 0 to 10 degrees C range, the Q10 for relaxation rate increases with increasing tetanus duration. Both of these observations can be explained if the Q10 for Ca2+ uptake by the sarcoplasmic reticulum is greater than the Q10 for Ca2+ sequestration by PA during relaxation. When Ca2+ and Mg2+ dissociation rates from PA at various temperatures are compared to other proposed indicators of PA function, it is concluded that PA facilitates relaxation of frog skeletal muscle in the 0 to 20 degrees C range.

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Year:  1993        PMID: 8109327     DOI: 10.1007/978-1-4615-2872-2_13

Source DB:  PubMed          Journal:  Adv Exp Med Biol        ISSN: 0065-2598            Impact factor:   2.622


  7 in total

1.  Tetanus relaxation of fast skeletal muscles of the mouse made parvalbumin deficient by gene inactivation.

Authors:  J M Raymackers; P Gailly; M C Schoor; D Pette; B Schwaller; W Hunziker; M R Celio; J M Gillis
Journal:  J Physiol       Date:  2000-09-01       Impact factor: 5.182

2.  The sensitivity of fast muscle contractile function to the major components of the sarcomere Ca(2+)-cycling system.

Authors:  C Golding; K Kelly; S T Kinsey; B R Locke
Journal:  Biophys Chem       Date:  2016-01-07       Impact factor: 2.352

3.  Engineering Parvalbumin for the Heart: Optimizing the Mg Binding Properties of Rat β-Parvalbumin.

Authors:  Jianchao Zhang; Vikram Shettigar; George C Zhang; Daniel G Kindell; Xiaotong Liu; Joseph J López; Vinatham Yerrimuni; Grace A Davis; Jonathan P Davis
Journal:  Front Physiol       Date:  2011-10-31       Impact factor: 4.566

4.  Juxtaposition of the changes in intracellular calcium and force during staircase potentiation at 30 and 37°C.

Authors:  Ian C Smith; Rene Vandenboom; A Russell Tupling
Journal:  J Gen Physiol       Date:  2014-12       Impact factor: 4.086

5.  Oncomodulin: The Enigmatic Parvalbumin Protein.

Authors:  Leslie K Climer; Andrew M Cox; Timothy J Reynolds; Dwayne D Simmons
Journal:  Front Mol Neurosci       Date:  2019-10-09       Impact factor: 5.639

6.  Magnesium Ions Moderate Calcium-Induced Calcium Release in Cardiac Calcium Release Sites by Binding to Ryanodine Receptor Activation and Inhibition Sites.

Authors:  Bogdan Iaparov; Iuliia Baglaeva; Ivan Zahradník; Alexandra Zahradníková
Journal:  Front Physiol       Date:  2022-01-25       Impact factor: 4.566

7.  Oxidative stress-induced dysregulation of excitation-contraction coupling contributes to muscle weakness.

Authors:  Rizwan Qaisar; Shylesh Bhaskaran; Pavithra Premkumar; Rojina Ranjit; Kavithalakshmi Satara Natarajan; Bumsoo Ahn; Kaitlyn Riddle; Dennis R Claflin; Arlan Richardson; Susan V Brooks; Holly Van Remmen
Journal:  J Cachexia Sarcopenia Muscle       Date:  2018-08-02       Impact factor: 12.910

  7 in total

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