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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1982-12-18
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pubmed:abstractText |
The Ca2+ activation mechanism of the longitudinal body wall muscles of Parastichopus californicus (sea cucumber) was studied using skinned muscle fiber bundles. Reversible phosphorylation of the myosin light chains correlated with Ca2+-activated tension and relaxation. Pretreatment of the skinned fibers with AT-P gamma S and high Ca2+ (10(-5)M) resulted in irreversible thiophosphorylation of the myosin light chains and activation of a Ca2+ insensitive tension. In contrast, pretreatment with low Ca2+ (10(-8)M) and ATP gamma S results in no thiophosphorylation of the myosin light chains or irreversible activation of tension. These results are consistent with a Ca2+-sensitive myosin light chain kinase/phosphatase system being responsible for the activation of the muscle. Other agents known to have an effect upon the Ca2+-activated tension in skinned vertebrate smooth muscle fibers (trifluoperazine, catalytic subunit of the cyclic AMP-dependent protein kinase, and calmodulin) did not have an effect on myosin light chain phosphorylation or Ca2+-activated tension. These results suggest a different type of myosin light chain kinase than is found in vertebrate smooth muscle is responsible for the activation of parastichopus longitudinal body wall muscle.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin-Light-Chain Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Myosins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Thionucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/adenosine 5'-O-(3-thiotriphosphate)
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9541
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
112
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
307-15
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:6897068-Adenosine Triphosphate,
pubmed-meshheading:6897068-Animals,
pubmed-meshheading:6897068-Calcium,
pubmed-meshheading:6897068-Calmodulin,
pubmed-meshheading:6897068-Echinodermata,
pubmed-meshheading:6897068-Muscle, Smooth,
pubmed-meshheading:6897068-Muscle Contraction,
pubmed-meshheading:6897068-Myosin-Light-Chain Kinase,
pubmed-meshheading:6897068-Myosins,
pubmed-meshheading:6897068-Phosphorylation,
pubmed-meshheading:6897068-Protein Kinases,
pubmed-meshheading:6897068-Sea Cucumbers,
pubmed-meshheading:6897068-Thionucleotides
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pubmed:year |
1982
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pubmed:articleTitle |
Evidence that myosin light chain phosphorylation regulates contraction in the body wall muscles of the sea cucumber.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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