Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
33
|
| pubmed:dateCreated |
1986-12-24
|
| pubmed:abstractText |
Protein kinase C has been shown to be a phospholipid/Ca2+-dependent enzyme activated by diacylglycerol (Nishizuka, Y. (1984) Nature 308, 693-697; Nishizuka, Y. (1984) Science 225, 1365-1370). We have reported that unsaturated fatty acids (oleic acid and arachidonic acid) can activate protein kinase C independently of Ca2+ and phospholipid (Murakami, K., and Routtenberg, A. (1985) FEBS Lett. 192, 189-193). This study shows that other cis-fatty acids such as linoleic acid also fully activate protein kinase C in the same manner. None of the saturated fatty acids (C:4 to C:18) nor the detergents (sodium dodecyl sulfate and Triton X-100) tested here were as effective as oleic acid. Unlike oleic acid, these detergents strongly inhibited protein kinase C activity induced by Ca2+/phosphatidylserine (PS) and diacylglycerol. Lowering the critical micelle concentration of oleic acid by increasing ionic strength also strongly inhibited oleic acid activation of protein kinase C activity. Dioleoylphosphatidylserine activated protein kinase C effectively (Ka = 7.2 microM). On the other hand, dimyristoylphosphatidylserine, which contains saturated fatty acids at both acyl positions, failed to activate protein kinase C even in the presence of Ca2+. These observations suggest that: protein kinase C activation by free fatty acid is specific to the cis-form and is not due to their detergent-like action, cis-fatty acid activation is due to the direct interaction of protein kinase C with the monomeric form of cis-fatty acids and not with the micelles of fatty acids, and cis-fatty acids at acyl positions in PS are also important for Ca2+/PS activation of protein kinase C.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arachidonic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Arachidonic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Detergents,
http://linkedlifedata.com/resource/pubmed/chemical/Diglycerides,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Linoleic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Linoleic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Micelles,
http://linkedlifedata.com/resource/pubmed/chemical/Oleic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Oleic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylserines,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
25
|
| pubmed:volume |
261
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
15424-9
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:3096987-Animals,
pubmed-meshheading:3096987-Arachidonic Acid,
pubmed-meshheading:3096987-Arachidonic Acids,
pubmed-meshheading:3096987-Calcium,
pubmed-meshheading:3096987-Detergents,
pubmed-meshheading:3096987-Diglycerides,
pubmed-meshheading:3096987-Enzyme Activation,
pubmed-meshheading:3096987-Fatty Acids,
pubmed-meshheading:3096987-Linoleic Acid,
pubmed-meshheading:3096987-Linoleic Acids,
pubmed-meshheading:3096987-Male,
pubmed-meshheading:3096987-Micelles,
pubmed-meshheading:3096987-Oleic Acid,
pubmed-meshheading:3096987-Oleic Acids,
pubmed-meshheading:3096987-Phosphatidylserines,
pubmed-meshheading:3096987-Phospholipids,
pubmed-meshheading:3096987-Protein Kinase C,
pubmed-meshheading:3096987-Rats,
pubmed-meshheading:3096987-Rats, Inbred Strains,
pubmed-meshheading:3096987-Stereoisomerism
|
| pubmed:year |
1986
|
| pubmed:articleTitle |
Protein kinase C activation by cis-fatty acid in the absence of Ca2+ and phospholipids.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|