Source:http://linkedlifedata.com/resource/pubmed/id/10085124
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
13
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| pubmed:dateCreated |
1999-4-29
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| pubmed:databankReference | |
| pubmed:abstractText |
Two new cloned human cDNAs encode paralogs of the 85-kDa cytosolic phospholipase A2 (cPLA2). We propose to call these cPLA2beta (114 kDa) and cPLA2gamma (61 kDa), giving the name cPLA2alpha to the well known 85-kDa enzyme. cPLA2beta mRNA is expressed more highly in cerebellum and pancreas and cPLA2gamma more highly in cardiac and skeletal muscle. Sequence-tagged site mapping places cPLA2beta on chromosome 15 in a region near a phosphoinositol bisphosphate phosphatase. The mRNA for cPLA2beta is spliced only at a very low level, and Northern blots in 24 tissues show exclusively the unspliced form. cPLA2beta has much lower activity on 2-arachidonoyl-phosphatidylcholine liposomes than either of the other two enzymes. Its sequence contains a histidine motif characteristic of the catalytic center of caspase proteases of the apoptotic cascade but no region characteristic of the catalytic cysteine. Sequence-tagged site mapping places cPLA2gamma on chromosome 19 near calmodulin. cPLA2gamma lacks the C2 domain, which gives cPLA2alpha its Ca2+ sensitivity, and accordingly cPLA2gamma has no dependence upon calcium, although cPLA2beta does. cPLA2gamma contains a prenyl group-binding site motif and appears to be largely membrane-bound. cPLA2alpha residues activated by phosphorylation do not appear to be well conserved in either new enzyme. In contrast, all three previously known catalytic residues, as well as one additional essential arginine, Arg-566 in cPLA2alpha, are conserved in both new enzyme sequences. Mutagenesis shows strong dependence on these residues for catalytic activity of all three enzymes.
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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 |
Mar
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
26
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| pubmed:volume |
274
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
8823-31
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| pubmed:dateRevised |
2007-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10085124-Amino Acid Sequence,
pubmed-meshheading:10085124-Base Sequence,
pubmed-meshheading:10085124-Binding Sites,
pubmed-meshheading:10085124-Chromosome Mapping,
pubmed-meshheading:10085124-Chromosomes, Human, Pair 15,
pubmed-meshheading:10085124-Cloning, Molecular,
pubmed-meshheading:10085124-Exons,
pubmed-meshheading:10085124-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:10085124-Humans,
pubmed-meshheading:10085124-Introns,
pubmed-meshheading:10085124-Isoenzymes,
pubmed-meshheading:10085124-Molecular Sequence Data,
pubmed-meshheading:10085124-Phospholipases A,
pubmed-meshheading:10085124-Phospholipases A2,
pubmed-meshheading:10085124-RNA, Messenger,
pubmed-meshheading:10085124-RNA Splicing,
pubmed-meshheading:10085124-Sequence Alignment,
pubmed-meshheading:10085124-Sequence Analysis, DNA,
pubmed-meshheading:10085124-Substrate Specificity
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| pubmed:year |
1999
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| pubmed:articleTitle |
Molecular cloning of two new human paralogs of 85-kDa cytosolic phospholipase A2.
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| pubmed:affiliation |
Lilly Research Laboratory, Indianapolis, Indiana 46285, USA.
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| pubmed:publicationType |
Journal Article
|