| pubmed-article:2160245 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2160245 | lifeskim:mentions | umls-concept:C0006104 | lld:lifeskim |
| pubmed-article:2160245 | lifeskim:mentions | umls-concept:C0026969 | lld:lifeskim |
| pubmed-article:2160245 | lifeskim:mentions | umls-concept:C0001480 | lld:lifeskim |
| pubmed-article:2160245 | lifeskim:mentions | umls-concept:C0031686 | lld:lifeskim |
| pubmed-article:2160245 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
| pubmed-article:2160245 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:2160245 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:2160245 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:2160245 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2160245 | pubmed:dateCreated | 1990-6-26 | lld:pubmed |
| pubmed-article:2160245 | pubmed:abstractText | Protein kinase FA (an activating factor of ATP.Mg-dependent protein phosphatase) has been characterized to exist in two forms in the purified brain myelin. One form of kinase FA is spontaneously active and trypsin-labile, whereas the other form of kinase FA is inactive and trypsin-resistant, suggesting a different membrane topography with active FA exposed on the outer face of the myelin membrane and inactive FA buried within the myelin membrane. When myelin was solubilized in 1% Triton X-100, all kinase FA became active and trypsin-labile. Phospholipid reconstitution studies further indicated that when kinase FA was reconstituted in acidic phospholipids, such as phosphatidylinositol and phosphatidylserine, the enzyme activity was inhibited in a dose-dependent manner, suggesting that kinase FA interacts with acidic phospholipids which inhibit its activity. Furthermore, when myelin was incubated with exogenous phospholipase C, the inactive/trypsin-resistant FA could be converted to the active/trypsin-labile FA in a time- and dose-dependent manner. Taken together, it is concluded that membrane phospholipids play an important role in modulating the activity of kinase FA in the brain myelin. It is suggested that phospholipase C may mediate the activation-sequestration of inactive/trypsin-resistant kinase FA in the brain myelin through the phospholipase C-catalyzed degradation of acidic membrane phospholipids. The activation-sequestration of protein kinase FA may represent one mode of control modulating the activity of kinase FA in the central nervous system myelin. | lld:pubmed |
| pubmed-article:2160245 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2160245 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2160245 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2160245 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2160245 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2160245 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2160245 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2160245 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2160245 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2160245 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2160245 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2160245 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:2160245 | pubmed:issn | 0277-8033 | lld:pubmed |
| pubmed-article:2160245 | pubmed:author | pubmed-author:YuJ SJS | lld:pubmed |
| pubmed-article:2160245 | pubmed:author | pubmed-author:YangS DSD | lld:pubmed |
| pubmed-article:2160245 | pubmed:author | pubmed-author:HuaC WCW | lld:pubmed |
| pubmed-article:2160245 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2160245 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:2160245 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2160245 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2160245 | pubmed:pagination | 75-82 | lld:pubmed |
| pubmed-article:2160245 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:2160245 | pubmed:meshHeading | pubmed-meshheading:2160245-... | lld:pubmed |
| pubmed-article:2160245 | pubmed:meshHeading | pubmed-meshheading:2160245-... | lld:pubmed |
| pubmed-article:2160245 | pubmed:meshHeading | pubmed-meshheading:2160245-... | lld:pubmed |
| pubmed-article:2160245 | pubmed:meshHeading | pubmed-meshheading:2160245-... | lld:pubmed |
| pubmed-article:2160245 | pubmed:meshHeading | pubmed-meshheading:2160245-... | lld:pubmed |
| pubmed-article:2160245 | pubmed:meshHeading | pubmed-meshheading:2160245-... | lld:pubmed |
| pubmed-article:2160245 | pubmed:meshHeading | pubmed-meshheading:2160245-... | lld:pubmed |
| pubmed-article:2160245 | pubmed:meshHeading | pubmed-meshheading:2160245-... | lld:pubmed |
| pubmed-article:2160245 | pubmed:meshHeading | pubmed-meshheading:2160245-... | lld:pubmed |
| pubmed-article:2160245 | pubmed:meshHeading | pubmed-meshheading:2160245-... | lld:pubmed |
| pubmed-article:2160245 | pubmed:meshHeading | pubmed-meshheading:2160245-... | lld:pubmed |
| pubmed-article:2160245 | pubmed:meshHeading | pubmed-meshheading:2160245-... | lld:pubmed |
| pubmed-article:2160245 | pubmed:meshHeading | pubmed-meshheading:2160245-... | lld:pubmed |
| pubmed-article:2160245 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2160245 | pubmed:articleTitle | On the mechanism of activation of protein kinase FA (an activating factor of ATP.Mg-dependent protein phosphatase) in brain myelin. | lld:pubmed |
| pubmed-article:2160245 | pubmed:affiliation | Institute of Life Science, National Tsing Hua University, Hsinchu, Taiwan, ROC. | lld:pubmed |
| pubmed-article:2160245 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2160245 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
