Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2004-6-25
pubmed:abstractText
Ryanodine receptors (RyR) play an important role in the regulation of intracellular Ca(2+) concentration and in the control of vascular tone. However, the mechanism regulating the activity of RyR is poorly understood. The present study determined whether protein methylation participates in the control of RyR activity. Using a planar lipid bilayer clamping system, S-adenosyl-L-methionine (SAM), a methyl donor, significantly increased the activity of a 245-pS reconstituted Ca(2+) release channel from coronary arterial smooth muscle (CASM) in a concentration-dependent manner. Addition of the protein methylation blockers, 3-deazaadenosine, S-adenosylhomocysteine or sinefungin into the cis solution markedly attenuated SAM-induced activation of RyR/Ca(2+) release channels. By Western blot analysis, arginine N-methyltransferase (PRMT1) and FK506 binding protein (FKBP) were detected in the SR used for reconstitution of RyR. In the presence of anti-PRMT1 antibody (1:100), SAM-induced activation of RyR/Ca(2+) channel was completely abolished. In addition, this SAM-induced increase in RyR/Ca(2+) channel activity was blocked by 30 microM ryanodine and by FK506 (100 microM), a ligand for the RyR accessory protein. These results suggest that protein methylation activates RyR/Ca(2+) release channels and may participate in the control of intracellular Ca(2+) mobilization in CASM cells by transferring a methyl group to the arginine moiety of the RyR accessory protein, FKBP 12.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1018-1172
pubmed:author
pubmed:copyrightInfo
Copyright 2004 S. Karger AG, Basel
pubmed:issnType
Print
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
229-40
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:15118362-Adenosine, pubmed-meshheading:15118362-Animals, pubmed-meshheading:15118362-Antibodies, pubmed-meshheading:15118362-Arteries, pubmed-meshheading:15118362-Cattle, pubmed-meshheading:15118362-Coronary Vessels, pubmed-meshheading:15118362-Methylation, pubmed-meshheading:15118362-Muscle, Smooth, Vascular, pubmed-meshheading:15118362-Myocytes, Smooth Muscle, pubmed-meshheading:15118362-Protein-Arginine N-Methyltransferases, pubmed-meshheading:15118362-Ryanodine, pubmed-meshheading:15118362-Ryanodine Receptor Calcium Release Channel, pubmed-meshheading:15118362-S-Adenosylmethionine, pubmed-meshheading:15118362-Sarcoplasmic Reticulum, pubmed-meshheading:15118362-Tacrolimus, pubmed-meshheading:15118362-Tacrolimus Binding Protein 1A, pubmed-meshheading:15118362-Tubercidin
pubmed:articleTitle
Protein methylation activates reconstituted ryanodine receptor-ca release channels from coronary artery myocytes.
pubmed:affiliation
Department of Pharmacology and Toxicology, Medical College of Wisconsin, Milwaukee 53226, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't