| pubmed-article:3355829 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3355829 | lifeskim:mentions | umls-concept:C0018787 | lld:lifeskim |
| pubmed-article:3355829 | lifeskim:mentions | umls-concept:C1622418 | lld:lifeskim |
| pubmed-article:3355829 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:3355829 | lifeskim:mentions | umls-concept:C0025723 | lld:lifeskim |
| pubmed-article:3355829 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:3355829 | lifeskim:mentions | umls-concept:C0678640 | lld:lifeskim |
| pubmed-article:3355829 | lifeskim:mentions | umls-concept:C0597484 | lld:lifeskim |
| pubmed-article:3355829 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:3355829 | pubmed:dateCreated | 1988-5-26 | lld:pubmed |
| pubmed-article:3355829 | pubmed:abstractText | We have examined the effect of membrane methylation on the Na+-Ca2+ exchange activity of canine cardiac sarcolemmal vesicles using S-adenosyl-L-methionine as methyl donor. Methylation leads to approximately 40% inhibition of the initial rate of Nai+-dependent Ca2+ uptake. The inhibition is due to a lowering of the Vmax for the reaction. The inhibition is not due to an effect on membrane permeability and is blocked by S-adenosyl-L-homocysteine, an inhibitor of methylation reactions. The following experiments indicated that inhibition of Na+-Ca2+ exchange was due to methylation of membrane protein and not due to methylated phosphatidylethanolamine (PE) compounds (i.e., phosphatidyl-N-monomethylethanolamine (PMME) or phosphatidyl-N,N'-dimethylethanolamine (PDME]: (1) We solubilized sarcolemma and reconstituted activity into vesicles containing no PE. The inhibition by S-adenosyl-L-methionine was not diminished in this environment. (2) We reconstituted sarcolemma into vesicles containing PMME or PDME. These methylated lipid components had no effect on Na+-Ca2+ exchange activity. (3) We verified that many membrane proteins, probably including the exchanger, become methylated. | lld:pubmed |
| pubmed-article:3355829 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3355829 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3355829 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3355829 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3355829 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3355829 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3355829 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3355829 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3355829 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3355829 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3355829 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3355829 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:3355829 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:3355829 | pubmed:author | pubmed-author:PhilipsonK... | lld:pubmed |
| pubmed-article:3355829 | pubmed:author | pubmed-author:VemuriRR | lld:pubmed |
| pubmed-article:3355829 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3355829 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:3355829 | pubmed:volume | 939 | lld:pubmed |
| pubmed-article:3355829 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3355829 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3355829 | pubmed:pagination | 503-8 | lld:pubmed |
| pubmed-article:3355829 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:3355829 | pubmed:meshHeading | pubmed-meshheading:3355829-... | lld:pubmed |
| pubmed-article:3355829 | pubmed:meshHeading | pubmed-meshheading:3355829-... | lld:pubmed |
| pubmed-article:3355829 | pubmed:meshHeading | pubmed-meshheading:3355829-... | lld:pubmed |
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| pubmed-article:3355829 | pubmed:meshHeading | pubmed-meshheading:3355829-... | lld:pubmed |
| pubmed-article:3355829 | pubmed:meshHeading | pubmed-meshheading:3355829-... | lld:pubmed |
| pubmed-article:3355829 | pubmed:meshHeading | pubmed-meshheading:3355829-... | lld:pubmed |
| pubmed-article:3355829 | pubmed:meshHeading | pubmed-meshheading:3355829-... | lld:pubmed |
| pubmed-article:3355829 | pubmed:meshHeading | pubmed-meshheading:3355829-... | lld:pubmed |
| pubmed-article:3355829 | pubmed:meshHeading | pubmed-meshheading:3355829-... | lld:pubmed |
| pubmed-article:3355829 | pubmed:meshHeading | pubmed-meshheading:3355829-... | lld:pubmed |
| pubmed-article:3355829 | pubmed:meshHeading | pubmed-meshheading:3355829-... | lld:pubmed |
| pubmed-article:3355829 | pubmed:meshHeading | pubmed-meshheading:3355829-... | lld:pubmed |
| pubmed-article:3355829 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3355829 | pubmed:articleTitle | Protein methylation inhibits Na+-Ca2+ exchange activity in cardiac sarcolemmal vesicles. | lld:pubmed |
| pubmed-article:3355829 | pubmed:affiliation | Department of Medicine, University of California, Los Angeles, School of Medicine 90024-1760. | lld:pubmed |
| pubmed-article:3355829 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3355829 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3355829 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3355829 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3355829 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3355829 | lld:pubmed |
