Source:http://linkedlifedata.com/resource/pubmed/id/17276714
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2007-3-5
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pubmed:databankReference | |
pubmed:abstractText |
Although the calpain system has been studied extensively in mammalian animals, much less is known about the properties of mu-calpain, m-calpain, and calpastatin in lower vertebrates such as fish. These three proteins were isolated and partly characterized from rainbow trout, Oncorhynchus mykiss, muscle. Trout m-calpain contains an 80-kDa large subunit, but the approximately 26-kDa small subunit from trout m-calpain is smaller than the 28-kDa small subunit from mammalian calpains. Trout mu-calpain and calpastatin were only partly purified; identity of trout mu-calpain was confirmed by labeling with antibodies to bovine skeletal muscle mu-calpain, and identity of trout calpastatin was confirmed by specific inhibition of bovine skeletal muscle mu- and m-calpain. Trout mu-calpain requires 4.4+/-2.8 microM and trout m-calpain requires 585+/-51 microM Ca(2+) for half-maximal activity, similar to the Ca(2+) requirements of mu- and m-calpain from mammalian tissues. Sequencing tryptic peptides indicated that the amino acid sequence of trout calpastatin shares little homology with the amino acid sequences of mammalian calpastatins. Screening a rainbow trout cDNA library identified three cDNAs encoding for the large subunit of a putative m-calpain. The amino acid sequence predicted by trout m-calpain cDNA was 65% identical to the human 80-kDa m-calpain sequence. Gene duplication and polyploidy occur in fish, and the amino acid sequence of the trout m-calpain 80-kDa subunit identified in this study was 83% identical to the sequence of a trout m-calpain 80-kDa subunit described earlier. This is the first report of two isoforms of m-calpain in a single species.
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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/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calpain,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/calpastatin,
http://linkedlifedata.com/resource/pubmed/chemical/m-calpain,
http://linkedlifedata.com/resource/pubmed/chemical/mu-calpain
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1096-4959
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
146
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
445-55
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pubmed:meshHeading |
pubmed-meshheading:17276714-Amino Acid Sequence,
pubmed-meshheading:17276714-Animals,
pubmed-meshheading:17276714-Base Sequence,
pubmed-meshheading:17276714-Calcium,
pubmed-meshheading:17276714-Calcium-Binding Proteins,
pubmed-meshheading:17276714-Calpain,
pubmed-meshheading:17276714-Cattle,
pubmed-meshheading:17276714-Cloning, Molecular,
pubmed-meshheading:17276714-DNA, Complementary,
pubmed-meshheading:17276714-Molecular Sequence Data,
pubmed-meshheading:17276714-Muscle, Skeletal,
pubmed-meshheading:17276714-Oncorhynchus mykiss,
pubmed-meshheading:17276714-Sequence Homology, Amino Acid
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pubmed:year |
2007
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pubmed:articleTitle |
Purification and characterization of calpain and calpastatin from rainbow trout, Oncorhynchus mykiss.
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pubmed:affiliation |
Laboratory of Food Science and Technology, Kagawa Nutrition University, 3-9-21 Chiyoda, Saitama, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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