pubmed-article:16956939 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16956939 | lifeskim:mentions | umls-concept:C0085274 | lld:lifeskim |
pubmed-article:16956939 | lifeskim:mentions | umls-concept:C0031667 | lld:lifeskim |
pubmed-article:16956939 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
pubmed-article:16956939 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
pubmed-article:16956939 | lifeskim:mentions | umls-concept:C1550548 | lld:lifeskim |
pubmed-article:16956939 | lifeskim:mentions | umls-concept:C1555714 | lld:lifeskim |
pubmed-article:16956939 | lifeskim:mentions | umls-concept:C1705654 | lld:lifeskim |
pubmed-article:16956939 | lifeskim:mentions | umls-concept:C0381321 | lld:lifeskim |
pubmed-article:16956939 | pubmed:issue | 22 | lld:pubmed |
pubmed-article:16956939 | pubmed:dateCreated | 2006-10-30 | lld:pubmed |
pubmed-article:16956939 | pubmed:abstractText | Recent reports demonstrated an association of human parvovirus B19 with inflammatory cardiomyopathy (iCMP), which is accompanied by endothelial dysfunction. As intracellular Ca(2+) activity is a key regulator of cell function and participates in mechanisms leading to endothelial dysfunction, the present experiments explored the effects of the B19 capsid proteins VP1 and VP2. A secreted phospholipase A2 (PLA2)-like activity has been located in the VP1 unique region of the B19 minor capsid protein. As PLA2 has recently been shown to activate the store-operated or capacitative Ca(2+) channel I(CRAC), we analyzed the impact of the viral PLA2 motif on Ca(2+) entry. We cloned the VP1 and VP2 genes isolated from a patient suffering from fatal B19 iCMP into eukaryotic expression vectors. We also generated a B19 replication-competent plasmid to demonstrate PLA2 activity under the control of the complete B19 genome. After the transfection of human endothelial cells (HMEC-1), cytosolic Ca(2+) activity was determined by utilizing Fura-2 fluorescence. VP1 and VP2 expression did not significantly modify basal cytosolic Ca(2+) activity or the decline of cytosolic Ca(2+) activity following the removal of extracellular Ca(2+). However, expression of VP1 and of the full-length B19 clone, but not of VP2, significantly accelerated the increase of cytosolic Ca(2+) activity following the readdition of extracellular Ca(2+) in the presence of thapsigargin, indicating an activation of I(CRAC.) The effect of VP1 was mimicked by the PLA2 product lysophosphatidylcholine and abolished by an inactivating mutation of the PLA2-encoding region of the VP1 gene. Our observations point to the activation of Ca(2+) entry by VP1 PLA2 activity, an effect likely participating in the pathophysiology of B19 infection. | lld:pubmed |
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pubmed-article:16956939 | pubmed:language | eng | lld:pubmed |
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pubmed-article:16956939 | pubmed:citationSubset | IM | lld:pubmed |
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