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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 |
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cites | cdi_FETCH-LOGICAL-c468t-d9d5f91faa60ca5a99f7cda3acd25a70bc32bb36108a1ce12e0ed491c0a96b463 |
container_end_page | 1900 |
container_issue | 5 |
container_start_page | 1894 |
container_title | Journal of applied physiology (1985) |
container_volume | 87 |
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 |
format | article |
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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</description><identifier>ISSN: 8750-7587</identifier><identifier>EISSN: 1522-1601</identifier><identifier>DOI: 10.1152/jappl.1999.87.5.1894</identifier><identifier>PMID: 10562634</identifier><identifier>CODEN: JAPHEV</identifier><language>eng</language><publisher>Bethesda, MD: Am Physiological Soc</publisher><subject>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</subject><ispartof>Journal of applied physiology (1985), 1999-11, Vol.87 (5), p.1894-1900</ispartof><rights>2000 INIST-CNRS</rights><rights>Copyright American Physiological Society Nov 1999</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c468t-d9d5f91faa60ca5a99f7cda3acd25a70bc32bb36108a1ce12e0ed491c0a96b463</citedby><cites>FETCH-LOGICAL-c468t-d9d5f91faa60ca5a99f7cda3acd25a70bc32bb36108a1ce12e0ed491c0a96b463</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1216039$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10562634$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Geiger, Paige C</creatorcontrib><creatorcontrib>Cody, Mark J</creatorcontrib><creatorcontrib>Sieck, Gary C</creatorcontrib><title>Force-calcium relationship depends on myosin heavy chain and troponin isoforms in rat diaphragm muscle fibers</title><title>Journal of applied physiology (1985)</title><addtitle>J Appl Physiol (1985)</addtitle><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</description><subject>Air breathing</subject><subject>Anatomy & physiology</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Calcium</subject><subject>Calcium - physiology</subject><subject>Diaphragm - cytology</subject><subject>Diaphragm - metabolism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Isomerism</subject><subject>Male</subject><subject>Muscle Contraction - physiology</subject><subject>Muscle Fibers, Skeletal - metabolism</subject><subject>Muscle Fibers, Skeletal - physiology</subject><subject>Muscle Fibers, Skeletal - ultrastructure</subject><subject>Muscular system</subject><subject>Myosin Heavy Chains - biosynthesis</subject><subject>Myosin Heavy Chains - metabolism</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Respiratory system: anatomy, metabolism, gas exchange, ventilatory mechanics, respiratory hemodynamics</subject><subject>Rodents</subject><subject>Troponin - biosynthesis</subject><subject>Troponin - metabolism</subject><subject>Vertebrates: respiratory system</subject><issn>8750-7587</issn><issn>1522-1601</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNqFkVGL1DAUhYMo7rj6D0SCiPjSmrRN2jzKsqPCgi_rc7hN0mmGtolJu9p_v6kzuIsgPuWGfOecGw5CrynJKWXFxyN4P-RUCJE3dc5y2ojqCdqlpyKjnNCnaNfUjGQ1a-oL9CLGIyG0qhh9ji4oYbzgZbVD494FZTIFg7LLiIMZYLZuir31WBtvJh2xm_C4umgn3Bu4W7HqIc0waTwH592ULja6zoUx4jQHmLG24PsAhxGPS1SDwZ1tTYgv0bMOhmhenc9L9H1_fXv1Jbv59vnr1aebTFW8mTMtNOsE7QA4UcBAiK5WGkpQumBQk1aVRduWnJIGqDK0MMToSlBFQPC24uUlen_y9cH9WEyc5WijMsMAk3FLlFwUDRON-C9Ia97wZJjAt3-BR7eEKX1CFkVBec3FBlUnSAUXYzCd9MGOEFZJidxKk79Lk1tpsqklk1tpSfbm7L20o9GPRKeWEvDuDEBMTXUBJmXjA5fySSke4nt76H_aYKTv12jd4A6r3C_DcGt-zdsKf6Kl112Sffi3LNGPNr0HW9bEKA</recordid><startdate>19991101</startdate><enddate>19991101</enddate><creator>Geiger, Paige C</creator><creator>Cody, Mark J</creator><creator>Sieck, Gary C</creator><general>Am Physiological Soc</general><general>American Physiological Society</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TS</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19991101</creationdate><title>Force-calcium relationship depends on myosin heavy chain and troponin isoforms in rat diaphragm muscle fibers</title><author>Geiger, Paige C ; Cody, Mark J ; Sieck, Gary C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c468t-d9d5f91faa60ca5a99f7cda3acd25a70bc32bb36108a1ce12e0ed491c0a96b463</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Air breathing</topic><topic>Anatomy & physiology</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Calcium</topic><topic>Calcium - physiology</topic><topic>Diaphragm - cytology</topic><topic>Diaphragm - metabolism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. 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 & 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. 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</abstract><cop>Bethesda, MD</cop><pub>Am Physiological Soc</pub><pmid>10562634</pmid><doi>10.1152/jappl.1999.87.5.1894</doi><tpages>7</tpages></addata></record> |
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ispartof | Journal of applied physiology (1985), 1999-11, Vol.87 (5), p.1894-1900 |
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source | American Physiological Society:Jisc Collections:American Physiological Society Journals ‘Read Publish & Join’ Agreement:2023-2024 (Reading list); American Physiological Society Free |
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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