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Force-calcium relationship depends on myosin heavy chain and troponin isoforms in rat diaphragm muscle fibers

Departments of Anesthesiology and Physiology and Biophysics, Mayo Clinic and Foundation, Rochester, Minnesota 55905 The present study examined Ca 2+ sensitivity of diaphragm muscle (Dia m ) fibers expressing different myosin heavy chain (MHC) isoforms. We hypothesized that Dia m fibers expressing th...

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Published in:Journal of applied physiology (1985) 1999-11, Vol.87 (5), p.1894-1900
Main Authors: Geiger, Paige C, Cody, Mark J, Sieck, Gary C
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container_issue 5
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container_title Journal of applied physiology (1985)
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creator Geiger, Paige C
Cody, Mark J
Sieck, Gary C
description Departments of Anesthesiology and Physiology and Biophysics, Mayo Clinic and Foundation, Rochester, Minnesota 55905 The present study examined Ca 2+ sensitivity of diaphragm muscle (Dia m ) fibers expressing different myosin heavy chain (MHC) isoforms. We hypothesized that Dia m fibers expressing the MHC slow isoform have greater Ca 2+ sensitivity than fibers expressing fast MHC isoforms and that this fiber-type difference in Ca 2+ sensitivity reflects the isoform composition of the troponin (Tn) complex (TnC, TnT, and TnI). Studies were performed in single Triton-X-permeabilized Dia m fibers. The Ca 2+ concentration at which 50% maximal force was generated (pCa 50 ) was determined for each fiber. SDS-PAGE and Western analyses were used to determine the MHC and Tn isoform composition of single fibers. The pCa 50 for Dia m fibers expressing MHC slow was significantly greater than that of fibers expressing fast MHC isoforms, and this greater Ca 2+ sensitivity was associated with expression of slow isoforms of the Tn complex. However, some Dia m fibers expressing MHC slow contained the fast TnC isoform. These results suggest that the combination of TnT, TnI, and TnC isoforms may determine Ca 2+ sensitivity in Dia m fibers. myosin heavy chain; troponin; diaphragm muscle; single fibers; calcium sensitivity; cooperativity
doi_str_mv 10.1152/jappl.1999.87.5.1894
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Psychology</topic><topic>Isomerism</topic><topic>Male</topic><topic>Muscle Contraction - physiology</topic><topic>Muscle Fibers, Skeletal - metabolism</topic><topic>Muscle Fibers, Skeletal - physiology</topic><topic>Muscle Fibers, Skeletal - ultrastructure</topic><topic>Muscular system</topic><topic>Myosin Heavy Chains - biosynthesis</topic><topic>Myosin Heavy Chains - metabolism</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Respiratory system: anatomy, metabolism, gas exchange, ventilatory mechanics, respiratory hemodynamics</topic><topic>Rodents</topic><topic>Troponin - biosynthesis</topic><topic>Troponin - metabolism</topic><topic>Vertebrates: respiratory system</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Geiger, Paige C</creatorcontrib><creatorcontrib>Cody, Mark J</creatorcontrib><creatorcontrib>Sieck, Gary C</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Physical Education Index</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of applied physiology (1985)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Geiger, Paige C</au><au>Cody, Mark J</au><au>Sieck, Gary C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Force-calcium relationship depends on myosin heavy chain and troponin isoforms in rat diaphragm muscle fibers</atitle><jtitle>Journal of applied physiology (1985)</jtitle><addtitle>J Appl Physiol (1985)</addtitle><date>1999-11-01</date><risdate>1999</risdate><volume>87</volume><issue>5</issue><spage>1894</spage><epage>1900</epage><pages>1894-1900</pages><issn>8750-7587</issn><eissn>1522-1601</eissn><coden>JAPHEV</coden><abstract>Departments of Anesthesiology and Physiology and Biophysics, Mayo Clinic and Foundation, Rochester, Minnesota 55905 The present study examined Ca 2+ sensitivity of diaphragm muscle (Dia m ) fibers expressing different myosin heavy chain (MHC) isoforms. We hypothesized that Dia m fibers expressing the MHC slow isoform have greater Ca 2+ sensitivity than fibers expressing fast MHC isoforms and that this fiber-type difference in Ca 2+ sensitivity reflects the isoform composition of the troponin (Tn) complex (TnC, TnT, and TnI). Studies were performed in single Triton-X-permeabilized Dia m fibers. The Ca 2+ concentration at which 50% maximal force was generated (pCa 50 ) was determined for each fiber. SDS-PAGE and Western analyses were used to determine the MHC and Tn isoform composition of single fibers. The pCa 50 for Dia m fibers expressing MHC slow was significantly greater than that of fibers expressing fast MHC isoforms, and this greater Ca 2+ sensitivity was associated with expression of slow isoforms of the Tn complex. However, some Dia m fibers expressing MHC slow contained the fast TnC isoform. 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subjects Air breathing
Anatomy & physiology
Animals
Biological and medical sciences
Blotting, Western
Calcium
Calcium - physiology
Diaphragm - cytology
Diaphragm - metabolism
Electrophoresis, Polyacrylamide Gel
Fundamental and applied biological sciences. Psychology
Isomerism
Male
Muscle Contraction - physiology
Muscle Fibers, Skeletal - metabolism
Muscle Fibers, Skeletal - physiology
Muscle Fibers, Skeletal - ultrastructure
Muscular system
Myosin Heavy Chains - biosynthesis
Myosin Heavy Chains - metabolism
Rats
Rats, Sprague-Dawley
Respiratory system: anatomy, metabolism, gas exchange, ventilatory mechanics, respiratory hemodynamics
Rodents
Troponin - biosynthesis
Troponin - metabolism
Vertebrates: respiratory system
title Force-calcium relationship depends on myosin heavy chain and troponin isoforms in rat diaphragm muscle fibers
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