| pubmed-article:8133281 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8133281 | lifeskim:mentions | umls-concept:C0026969 | lld:lifeskim |
| pubmed-article:8133281 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8133281 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:8133281 | pubmed:dateCreated | 1994-4-20 | lld:pubmed |
| pubmed-article:8133281 | pubmed:abstractText | Incubation of rat brainstem slices with [3H]-mevalonate ([3H]MVA) in the presence of lovastatin resulted in the incorporation of label into three groups of myelin-associated proteins with molecular masses of 47, 21-27, and 8 kDa, as revealed on sodium dodecyl sulfate-polyacrylamide rod gel electrophoresis. Although the gel patterns of [3H]MVA-derived prenylated proteins were similar, the relative level of 3H incorporated into each protein species differed between myelin and the brainstem homogenate. Immunoprecipitation studies identified the 47-kDa prenylated protein as a 2'-3'-cyclic nucleotide phosphodiesterase, whereas the 8-kDa protein proved to be the gamma subunit of membrane-associated guanine nucleotide regulatory protein. The 3H-labeled 21-27-kDa group in myelin corresponds to the molecular mass of the extensive Ras-like family of monomeric GTP-binding proteins known to be prenylated in other tissues. Increase in lovastatin concentration resulted in reduced levels of [3H]MVA-labeled species in myelin and concomitantly increased levels in the cytosol. A cold MVA chase restored to normality the appearance of [3H]MVA-labeled proteins in myelin. Furthermore, a high lovastatin concentration in the brainstem slice incubation mixture altered the appearance of newly synthesized nonprenylated myelin proteins, including proteolipid protein and the 17-kDa subspecies of myelin basic protein. Because other myelin proteins were unaffected by the high lovastatin concentration, restricting the availability of MVA in myelin-forming cells may selectively alter processes required for myelinogenesis.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
| pubmed-article:8133281 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8133281 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8133281 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8133281 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8133281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8133281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8133281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8133281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8133281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8133281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8133281 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8133281 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8133281 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8133281 | pubmed:issn | 0022-3042 | lld:pubmed |
| pubmed-article:8133281 | pubmed:author | pubmed-author:ColemanP SPS | lld:pubmed |
| pubmed-article:8133281 | pubmed:author | pubmed-author:Sepp-Lorenzin... | lld:pubmed |
| pubmed-article:8133281 | pubmed:author | pubmed-author:LaroccaJ NJN | lld:pubmed |
| pubmed-article:8133281 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8133281 | pubmed:volume | 62 | lld:pubmed |
| pubmed-article:8133281 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8133281 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8133281 | pubmed:pagination | 1539-45 | lld:pubmed |
| pubmed-article:8133281 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:8133281 | pubmed:meshHeading | pubmed-meshheading:8133281-... | lld:pubmed |
| pubmed-article:8133281 | pubmed:meshHeading | pubmed-meshheading:8133281-... | lld:pubmed |
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| pubmed-article:8133281 | pubmed:meshHeading | pubmed-meshheading:8133281-... | lld:pubmed |
| pubmed-article:8133281 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8133281 | pubmed:articleTitle | Isoprenylated proteins in myelin. | lld:pubmed |
| pubmed-article:8133281 | pubmed:affiliation | SKI Program in Cell Biology, Memorial Sloan-Kettering Cancer Center, New York, New York. | lld:pubmed |
| pubmed-article:8133281 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8133281 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8133281 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8133281 | lld:pubmed |
