Linked Life Data

18289524

Source:http://linkedlifedata.com/resource/pubmed/id/18289524

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-3-3
pubmed:abstractText
Transient receptor potential canonical (TRPC) proteins have been proposed to function as plasma membrane Ca2+ channels activated by store depletion and/or by receptor stimulation. However, their role in the increase in cytosolic Ca2+ activated by contractile agonists in vascular smooth muscle is not yet elucidated. The present study was designed to investigate the functional and molecular properties of the Ca2+ entry pathway activated by endothelin-1 in primary cultured aortic smooth muscle cells. Measurement of the Ca2+ signal in fura-2-loaded cells allowed to characterize endothelin-1-evoked Ca2+ entry, which was resistant to dihydropyridine, and was blocked by 2-aminoethoxydiphenylborate (2-APB) and micromolar concentration of Gd3+. It was not activated by store depletion, but was inhibited by the endothelin ETA receptor antagonist BQ-123, and by heparin. On the opposite, thapsigargin-induced store depletion activated a Ca2+ entry pathway that was not affected by 2-APB, BQ-123 or heparin, and was less sensitive to Gd3+ than was endothelin-1-evoked Ca2+ entry. Investigation of the gene expression of TRPC isoforms by real-time RT-PCR revealed that TRPC1 was the most abundant. In cells transfected with TRPC1 small interfering RNA sequence, TRPC1 mRNA and protein expression were decreased by 72+/-3% and 86+/-2%, respectively, while TRPC6 expression was unaffected. In TRPC1 knockdown cells, both endothelin-1-evoked Ca2+ entry and store-operated Ca2+ entry evoked by thapsigargin were blunted. These results indicate that in aortic smooth muscle cells, TRPC1 is not only involved in Ca2+ entry activated by store depletion but also in receptor-operated Ca2+ entry, which requires inositol (1,4,5) triphosphate receptor activation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-2999
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
583
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
135-47
pubmed:meshHeading
pubmed-meshheading:18289524-Animals, pubmed-meshheading:18289524-Anticoagulants, pubmed-meshheading:18289524-Calcium, pubmed-meshheading:18289524-Calcium Channel Agonists, pubmed-meshheading:18289524-Calcium Signaling, pubmed-meshheading:18289524-Cells, Cultured, pubmed-meshheading:18289524-Endothelin-1, pubmed-meshheading:18289524-Fluorescent Antibody Technique, pubmed-meshheading:18289524-Gene Expression Regulation, pubmed-meshheading:18289524-Heparin, pubmed-meshheading:18289524-Inositol 1,4,5-Trisphosphate Receptors, pubmed-meshheading:18289524-Male, pubmed-meshheading:18289524-Microinjections, pubmed-meshheading:18289524-Muscle, Smooth, Vascular, pubmed-meshheading:18289524-RNA, Messenger, pubmed-meshheading:18289524-RNA, Small Interfering, pubmed-meshheading:18289524-Rats, pubmed-meshheading:18289524-Rats, Wistar, pubmed-meshheading:18289524-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:18289524-TRPC Cation Channels, pubmed-meshheading:18289524-Transfection, pubmed-meshheading:18289524-Vasoconstrictor Agents
pubmed:year
2008
pubmed:articleTitle
Agonist-evoked calcium entry in vascular smooth muscle cells requires IP3 receptor-mediated activation of TRPC1.
pubmed:affiliation
Unit of Cellular Physiology, Université Catholique de Louvain, Bruxelles, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't