| pubmed-article:10727417 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10727417 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:10727417 | lifeskim:mentions | umls-concept:C0005821 | lld:lifeskim |
| pubmed-article:10727417 | lifeskim:mentions | umls-concept:C1166758 | lld:lifeskim |
| pubmed-article:10727417 | lifeskim:mentions | umls-concept:C0086376 | lld:lifeskim |
| pubmed-article:10727417 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:10727417 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
| pubmed-article:10727417 | lifeskim:mentions | umls-concept:C1550548 | lld:lifeskim |
| pubmed-article:10727417 | lifeskim:mentions | umls-concept:C1555714 | lld:lifeskim |
| pubmed-article:10727417 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:10727417 | lifeskim:mentions | umls-concept:C1705654 | lld:lifeskim |
| pubmed-article:10727417 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:10727417 | pubmed:dateCreated | 2000-6-5 | lld:pubmed |
| pubmed-article:10727417 | pubmed:abstractText | We have investigated the mechanism of Ca(2+) entry into fura-2-loaded human platelets by preventing the prenylation of proteins such as small GTP-binding proteins. The farnesylcysteine analogues farnesylthioacetic acid (FTA) and N-acetyl-S-geranylgeranyl-L-cysteine (AGGC), which are inhibitors of the methylation of prenylated and geranylgeranylated proteins respectively, significantly decreased thrombin-evoked increases in intracellular free Ca(2+) concentration ([Ca(2+)](i)) in the presence, but not in the absence, of external Ca(2+), suggesting a relatively selective inhibition of Ca(2+) entry over internal release. Both these compounds and N-acetyl-S-farnesyl-L-cysteine, which had similar effects to those of FTA, also decreased Ca(2+) entry evoked by the depletion of intracellular Ca(2+) stores with thapsigargin. The inactive control N-acetyl-S-geranyl-L-cysteine was without effect. Patulin, an inhibitor of prenylation that is inert with respect to methyltransferases, also decreased store-regulated Ca(2+) entry. Cytochalasin D, an inhibitor of actin polymerization, significantly decreased store-regulated Ca(2+) entry in a time-dependent manner. Both cytochalasin D and the farnesylcysteine analogues FTA and AGGC inhibited actin polymerization; however, when evoking the same extent of decrease in actin filament formation, FTA and AGGC showed greater inhibitory effects on Ca(2+) entry, indicating a cytoskeleton-independent component in the regulation of Ca(2+) entry by small GTP-binding-protein. These findings suggest that prenylated proteins such as small GTP-binding proteins are involved in store-regulated Ca(2+) entry through actin cytoskeleton-dependent and cytoskeleton-independent mechanisms in human platelets. | lld:pubmed |
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| pubmed-article:10727417 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10727417 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10727417 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10727417 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10727417 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10727417 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10727417 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:10727417 | pubmed:author | pubmed-author:SageS OSO | lld:pubmed |
| pubmed-article:10727417 | pubmed:author | pubmed-author:RosadoJ AJA | lld:pubmed |
| pubmed-article:10727417 | pubmed:issnType | Print | lld:pubmed |
