Progressive resistance training reduces myosin heavy chain coexpression in single muscle fibers from older men
Human Performance Laboratory, Ball State University, Muncie, Indiana 47306 The purpose of this study was to examine myosin heavy chain (MHC) and myosin light chain (MLC) isoforms following 12 wk of progressive resistance training (PRT). A needle biopsy was taken from the vastus lateralis to determin...
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| Veröffentlicht in: | Journal of applied physiology (1985) 2000-02, Vol.88 (2), p.627-633 |
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| container_title | Journal of applied physiology (1985) |
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| creator | Williamson, David L Godard, Michael P Porter, David A Costill, David L Trappe, Scott W |
| description | Human Performance Laboratory, Ball State University, Muncie, Indiana
47306
The
purpose of this study was to examine myosin heavy chain (MHC) and
myosin light chain (MLC) isoforms following 12 wk of progressive
resistance training (PRT). A needle biopsy
was taken from the vastus lateralis to determine fiber-type expression
[ATPase (pH 4.54) and MHC/MLC] in seven healthy men (age = 74.0 ± 1.8 yr). Subjects were also tested for 1-repetition maximum
(1-RM), pre- and posttraining. The progressive knee extensor protocol consisted of three sets at 80% of 1-RM 3 days/wk for 12 wk.
Freeze-dried, single muscle fibers were dissected for MHC and MLC
analysis and then subjected to SDS-PAGE and silver staining, pre- and
posttraining. MHC expression increased in the I (10.4%; P |
| doi_str_mv | 10.1152/jappl.2000.88.2.627 |
| format | Article |
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47306
The
purpose of this study was to examine myosin heavy chain (MHC) and
myosin light chain (MLC) isoforms following 12 wk of progressive
resistance training (PRT). A needle biopsy
was taken from the vastus lateralis to determine fiber-type expression
[ATPase (pH 4.54) and MHC/MLC] in seven healthy men (age = 74.0 ± 1.8 yr). Subjects were also tested for 1-repetition maximum
(1-RM), pre- and posttraining. The progressive knee extensor protocol consisted of three sets at 80% of 1-RM 3 days/wk for 12 wk.
Freeze-dried, single muscle fibers were dissected for MHC and MLC
analysis and then subjected to SDS-PAGE and silver staining, pre- and
posttraining. MHC expression increased in the I (10.4%; P < 0.05) and decreased in I/IIa (9.0%; P < 0.05), I/IIa/x
(0.9%; P < 0.05), and IIa/x (8.9%; P < 0.05)
isoforms, with no change in the IIa and IIx isoforms, pre- vs.
posttraining (total fibers = 3,059). The
MLC 3f -to-MLC 2 ratio did not change with the PRT
in either the MHC I or MHC IIa isoforms (total fibers = 902), pre- to
posttraining. ATPase fiber distribution did not significantly differ
following training (I: 50.4 ± 6.7 vs. 51.9 ± 7.9, IIa:
36.8 ± 5.3 vs. 41.1 ± 7.0, IIb: 12.8 ± 5.6 vs. 7.0 ± 4.0%;
pre- vs. posttraining, respectively). 1-RM increased (51.9%; P < 0.05) from pre- to posttraining. The PRT provide a stimulus for
alterations in MHC isoforms, which demonstrated a decrease in all
hybrid isoforms and an increase in MHC I expression (not found in the
ATPase results), unlike the MLC ratio (3:2), which was not altered with training.
hybrid; myosin light chain; adenosine triphosphatase histochemistry</description><identifier>ISSN: 8750-7587</identifier><identifier>EISSN: 1522-1601</identifier><identifier>DOI: 10.1152/jappl.2000.88.2.627</identifier><identifier>PMID: 10658030</identifier><identifier>CODEN: JAPHEV</identifier><language>eng</language><publisher>Bethesda, MD: Am Physiological Soc</publisher><subject>Adenosine Triphosphatases - metabolism ; Aged - physiology ; Biological and medical sciences ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. Psychology ; Humans ; Male ; Men ; Muscle Fibers, Skeletal - enzymology ; Muscle Fibers, Skeletal - metabolism ; Muscular system ; Myosin Heavy Chains - biosynthesis ; Myosin Light Chains - biosynthesis ; Older people ; Physical Exertion - physiology ; Physical fitness ; Protein Isoforms - biosynthesis ; Space life sciences ; Striated muscle. Tendons ; Vertebrates: osteoarticular system, musculoskeletal system</subject><ispartof>Journal of applied physiology (1985), 2000-02, Vol.88 (2), p.627-633</ispartof><rights>2000 INIST-CNRS</rights><rights>Copyright American Physiological Society Feb 2000</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c433t-43c07adf8c75b29bebde07f9ad5add1b8f9ed12969cbffbb1df3cbb07ebb3ff63</citedby><cites>FETCH-LOGICAL-c433t-43c07adf8c75b29bebde07f9ad5add1b8f9ed12969cbffbb1df3cbb07ebb3ff63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,3026,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1340992$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10658030$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Williamson, David L</creatorcontrib><creatorcontrib>Godard, Michael P</creatorcontrib><creatorcontrib>Porter, David A</creatorcontrib><creatorcontrib>Costill, David L</creatorcontrib><creatorcontrib>Trappe, Scott W</creatorcontrib><title>Progressive resistance training reduces myosin heavy chain coexpression in single muscle fibers from older men</title><title>Journal of applied physiology (1985)</title><addtitle>J Appl Physiol (1985)</addtitle><description>Human Performance Laboratory, Ball State University, Muncie, Indiana
47306
The
purpose of this study was to examine myosin heavy chain (MHC) and
myosin light chain (MLC) isoforms following 12 wk of progressive
resistance training (PRT). A needle biopsy
was taken from the vastus lateralis to determine fiber-type expression
[ATPase (pH 4.54) and MHC/MLC] in seven healthy men (age = 74.0 ± 1.8 yr). Subjects were also tested for 1-repetition maximum
(1-RM), pre- and posttraining. The progressive knee extensor protocol consisted of three sets at 80% of 1-RM 3 days/wk for 12 wk.
Freeze-dried, single muscle fibers were dissected for MHC and MLC
analysis and then subjected to SDS-PAGE and silver staining, pre- and
posttraining. MHC expression increased in the I (10.4%; P < 0.05) and decreased in I/IIa (9.0%; P < 0.05), I/IIa/x
(0.9%; P < 0.05), and IIa/x (8.9%; P < 0.05)
isoforms, with no change in the IIa and IIx isoforms, pre- vs.
posttraining (total fibers = 3,059). The
MLC 3f -to-MLC 2 ratio did not change with the PRT
in either the MHC I or MHC IIa isoforms (total fibers = 902), pre- to
posttraining. ATPase fiber distribution did not significantly differ
following training (I: 50.4 ± 6.7 vs. 51.9 ± 7.9, IIa:
36.8 ± 5.3 vs. 41.1 ± 7.0, IIb: 12.8 ± 5.6 vs. 7.0 ± 4.0%;
pre- vs. posttraining, respectively). 1-RM increased (51.9%; P < 0.05) from pre- to posttraining. The PRT provide a stimulus for
alterations in MHC isoforms, which demonstrated a decrease in all
hybrid isoforms and an increase in MHC I expression (not found in the
ATPase results), unlike the MLC ratio (3:2), which was not altered with training.
hybrid; myosin light chain; adenosine triphosphatase histochemistry</description><subject>Adenosine Triphosphatases - metabolism</subject><subject>Aged - physiology</subject><subject>Biological and medical sciences</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Male</subject><subject>Men</subject><subject>Muscle Fibers, Skeletal - enzymology</subject><subject>Muscle Fibers, Skeletal - metabolism</subject><subject>Muscular system</subject><subject>Myosin Heavy Chains - biosynthesis</subject><subject>Myosin Light Chains - biosynthesis</subject><subject>Older people</subject><subject>Physical Exertion - physiology</subject><subject>Physical fitness</subject><subject>Protein Isoforms - biosynthesis</subject><subject>Space life sciences</subject><subject>Striated muscle. Tendons</subject><subject>Vertebrates: osteoarticular system, musculoskeletal system</subject><issn>8750-7587</issn><issn>1522-1601</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kU9v1DAQxSMEokvhEyAhCyF6SvCfJE6OVUWhUiU4lLNlO-PEKycO9qY03x6nu4gKidPInt-bGb2XZW8JLgip6Ke9nGdXUIxx0TQFLWrKn2W71KE5qTF5nu0aXuGcVw0_y17FuMeYlGVFXmZnBNdVgxneZdP34PsAMdp7QKnaeJCTBnQI0k526tNft2iIaFx9tBMaQN6vSA-pi7SHh_lR6yeU3qnfO0DjEnUqxioIEZngR-RdBwGNML3OXhjpIrw51fPsx_Xnu6uv-e23LzdXl7e5Lhk75CXTmMvONJpXirYKVAeYm1Z2lew6ohrTQkdoW7daGaMU6QzTSmEOSjFjanaefTzOnYP_uUA8iNFGDc7JCfwSBcdNy1pOE_j-H3DvlzCl2wSllJS8YjxB7Ajp4GMMYMQc7CjDKggWWxbiMQuxZSGaRlCRskiqd6fRixqhe6I5mp-ADydARi2dCcl5G_9yrMRtu514ccQG2w-_bAAxD2vy3Pl-3RY_3cj-T14vzt3Bw2GT_FGIORn3Gzzgt-w</recordid><startdate>20000201</startdate><enddate>20000201</enddate><creator>Williamson, David L</creator><creator>Godard, Michael P</creator><creator>Porter, David A</creator><creator>Costill, David L</creator><creator>Trappe, Scott W</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>20000201</creationdate><title>Progressive resistance training reduces myosin heavy chain coexpression in single muscle fibers from older men</title><author>Williamson, David L ; Godard, Michael P ; Porter, David A ; Costill, David L ; Trappe, Scott W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c433t-43c07adf8c75b29bebde07f9ad5add1b8f9ed12969cbffbb1df3cbb07ebb3ff63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Adenosine Triphosphatases - metabolism</topic><topic>Aged - physiology</topic><topic>Biological and medical sciences</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Male</topic><topic>Men</topic><topic>Muscle Fibers, Skeletal - enzymology</topic><topic>Muscle Fibers, Skeletal - metabolism</topic><topic>Muscular system</topic><topic>Myosin Heavy Chains - biosynthesis</topic><topic>Myosin Light Chains - biosynthesis</topic><topic>Older people</topic><topic>Physical Exertion - physiology</topic><topic>Physical fitness</topic><topic>Protein Isoforms - biosynthesis</topic><topic>Space life sciences</topic><topic>Striated muscle. Tendons</topic><topic>Vertebrates: osteoarticular system, musculoskeletal system</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Williamson, David L</creatorcontrib><creatorcontrib>Godard, Michael P</creatorcontrib><creatorcontrib>Porter, David A</creatorcontrib><creatorcontrib>Costill, David L</creatorcontrib><creatorcontrib>Trappe, Scott W</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>Williamson, David L</au><au>Godard, Michael P</au><au>Porter, David A</au><au>Costill, David L</au><au>Trappe, Scott W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Progressive resistance training reduces myosin heavy chain coexpression in single muscle fibers from older men</atitle><jtitle>Journal of applied physiology (1985)</jtitle><addtitle>J Appl Physiol (1985)</addtitle><date>2000-02-01</date><risdate>2000</risdate><volume>88</volume><issue>2</issue><spage>627</spage><epage>633</epage><pages>627-633</pages><issn>8750-7587</issn><eissn>1522-1601</eissn><coden>JAPHEV</coden><abstract>Human Performance Laboratory, Ball State University, Muncie, Indiana
47306
The
purpose of this study was to examine myosin heavy chain (MHC) and
myosin light chain (MLC) isoforms following 12 wk of progressive
resistance training (PRT). A needle biopsy
was taken from the vastus lateralis to determine fiber-type expression
[ATPase (pH 4.54) and MHC/MLC] in seven healthy men (age = 74.0 ± 1.8 yr). Subjects were also tested for 1-repetition maximum
(1-RM), pre- and posttraining. The progressive knee extensor protocol consisted of three sets at 80% of 1-RM 3 days/wk for 12 wk.
Freeze-dried, single muscle fibers were dissected for MHC and MLC
analysis and then subjected to SDS-PAGE and silver staining, pre- and
posttraining. MHC expression increased in the I (10.4%; P < 0.05) and decreased in I/IIa (9.0%; P < 0.05), I/IIa/x
(0.9%; P < 0.05), and IIa/x (8.9%; P < 0.05)
isoforms, with no change in the IIa and IIx isoforms, pre- vs.
posttraining (total fibers = 3,059). The
MLC 3f -to-MLC 2 ratio did not change with the PRT
in either the MHC I or MHC IIa isoforms (total fibers = 902), pre- to
posttraining. ATPase fiber distribution did not significantly differ
following training (I: 50.4 ± 6.7 vs. 51.9 ± 7.9, IIa:
36.8 ± 5.3 vs. 41.1 ± 7.0, IIb: 12.8 ± 5.6 vs. 7.0 ± 4.0%;
pre- vs. posttraining, respectively). 1-RM increased (51.9%; P < 0.05) from pre- to posttraining. The PRT provide a stimulus for
alterations in MHC isoforms, which demonstrated a decrease in all
hybrid isoforms and an increase in MHC I expression (not found in the
ATPase results), unlike the MLC ratio (3:2), which was not altered with training.
hybrid; myosin light chain; adenosine triphosphatase histochemistry</abstract><cop>Bethesda, MD</cop><pub>Am Physiological Soc</pub><pmid>10658030</pmid><doi>10.1152/jappl.2000.88.2.627</doi><tpages>7</tpages></addata></record> |
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| ispartof | Journal of applied physiology (1985), 2000-02, Vol.88 (2), p.627-633 |
| issn | 8750-7587 1522-1601 |
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| recordid | cdi_pubmed_primary_10658030 |
| source | MEDLINE; American Physiological Society; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Adenosine Triphosphatases - metabolism Aged - physiology Biological and medical sciences Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Humans Male Men Muscle Fibers, Skeletal - enzymology Muscle Fibers, Skeletal - metabolism Muscular system Myosin Heavy Chains - biosynthesis Myosin Light Chains - biosynthesis Older people Physical Exertion - physiology Physical fitness Protein Isoforms - biosynthesis Space life sciences Striated muscle. Tendons Vertebrates: osteoarticular system, musculoskeletal system |
| title | Progressive resistance training reduces myosin heavy chain coexpression in single muscle fibers from older men |
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