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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
1988-1-15
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pubmed:abstractText |
The effects of hypothyroidism on structural and functional properties of the actomyosin-ATPase complex of rat fast-twitch gastrocnemius muscle were examined and related to energetic and mechanical parameters. Hypothyroidism resulted in the appearance of a small band of the myosin heavy chain subunit of the slow form (MHCs) 8% of total MHC) which was absent in the euthyroid group. This observation corresponded with lower activities of myofibrillar ATPase (-14%) and Ca-activated myosin ATPase (-9%) in the hypothyroid group, although these changes were not significant. No effect of hypothyroidism on the Ca2+-sensitivity of the myofibrillar-ATPase activity was observed and tetanic force was not changed. Twitch force, however, was significantly increased by hypothyroidism. The degree of myosin P-light chain phosphorylation (percentage of total amount of P-light chain) determined after 5 and 10 s of tetanic stimulation (130 Hz, 35 degrees C), respectively, proved to be significantly lower in the hypothyroid group (5 s: 57%; 10 s: 61%) vs the euthyroid group (5 s: 79%; 10 s: 82%). There was no difference in P-light chain phosphorylation at rest between eu- and hypothyroids. The results suggest that a decreased actomyosin-ATPase activity can only in part contribute to the 30% lower energy turnover during force development found for fast-twitch skeletal muscle of hypothyroid rats. Moreover, the increase in twitch force by hypothyroidism cannot be explained by a change in myosin P-light chain phosphorylation. Isometric twitch tension potentiation after a 2 s tetanus and during low-frequency repetitive stimulation was reduced (up to -60%) in muscles of hypothyroid rats, which may well be related to the lower extent of P-light chain phosphorylation in hypothyroids.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0031-6768
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
410
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
48-54
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:2960952-Actomyosin,
pubmed-meshheading:2960952-Adenosine Triphosphatases,
pubmed-meshheading:2960952-Animals,
pubmed-meshheading:2960952-Electric Stimulation,
pubmed-meshheading:2960952-Hypothyroidism,
pubmed-meshheading:2960952-Male,
pubmed-meshheading:2960952-Muscle Contraction,
pubmed-meshheading:2960952-Muscles,
pubmed-meshheading:2960952-Myofibrils,
pubmed-meshheading:2960952-Myosins,
pubmed-meshheading:2960952-Rats,
pubmed-meshheading:2960952-Rats, Inbred Strains
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pubmed:year |
1987
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pubmed:articleTitle |
Structural and functional aspects of the actomyosin complex from fast-twitch muscle of euthyroid and hypothyroid rats.
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pubmed:affiliation |
Laboratory for Physiology, Free University, Amsterdam, The Netherlands.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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