Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-8-11
pubmed:abstractText
Our previous studies with fluoride have indicated that G-proteins may mediate the gating of Ca++ channels in vascular smooth muscle (VSM). We now present further studies on the relationship between G-proteins and Ca++ channels in VSM using guanosine-5'-(gamma-thio)triphosphate (GTP gamma S), a hydrolysis-resistant analog of GTP. Rat tail artery helical strips pretreated with GTP gamma S in a cytosol-like solution contracted in a Ca++-dependent manner in the absence of a depolarizing concentration of K+, hormones or any other Ca++ agonists. Contraction was dependent on the concentrations of applied GTP gamma S. The ability of strips pretreated with GTP gamma S to contract in response to Ca++ was not reversed by repeated washing. Incubation with 1 mM GTP applied extracellularly did not induce tension development. Treatment with a subthreshold concentration of GTP gamma S shifted the K+ concentration-related tension curve to the left but did not alter the maximum response. The contractions induced by GTP gamma S pretreatment and by submaximal (60 mM) KCI were additive at all levels of Ca++ tested. Extra tension development could be evoked from tissue maximally contracted with GTP gamma S by adding maximal K+ and norepinephrine. The relaxing sensitivity of the GTP gamma S-related contraction to reversal by nifedipine was between those for K+ depolarization and norepinephrine, and the GTP gamma S-induced rise in tension was partially inhibited by the Ca++ channel blocker nifedipine. Ca++-elicited contraction of the GTP gamma S-pretreated strips was relaxed by forskolin, an adenylate cyclase activator, 3-isobutyl-l-methyl-xanthanine, a cyclic nucleotide phosphodiesterase inhibitor, and dibutyryl cyclic AMP.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/1-Methyl-3-isobutylxanthine, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Bucladesine, http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channels, http://linkedlifedata.com/resource/pubmed/chemical/Forskolin, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Guanosine 5'-O-(3-Thiotriphosphate), http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Nifedipine, http://linkedlifedata.com/resource/pubmed/chemical/Norepinephrine, http://linkedlifedata.com/resource/pubmed/chemical/Thionucleotides
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0022-3565
pubmed:author
pubmed:issnType
Print
pubmed:volume
250
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
352-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:2473191-1-Methyl-3-isobutylxanthine, pubmed-meshheading:2473191-Adenosine Triphosphate, pubmed-meshheading:2473191-Animals, pubmed-meshheading:2473191-Arteries, pubmed-meshheading:2473191-Bucladesine, pubmed-meshheading:2473191-Calcium, pubmed-meshheading:2473191-Calcium Channels, pubmed-meshheading:2473191-Forskolin, pubmed-meshheading:2473191-GTP-Binding Proteins, pubmed-meshheading:2473191-Guanosine 5'-O-(3-Thiotriphosphate), pubmed-meshheading:2473191-Guanosine Triphosphate, pubmed-meshheading:2473191-Kinetics, pubmed-meshheading:2473191-Male, pubmed-meshheading:2473191-Muscle, Smooth, Vascular, pubmed-meshheading:2473191-Nifedipine, pubmed-meshheading:2473191-Norepinephrine, pubmed-meshheading:2473191-Rats, pubmed-meshheading:2473191-Rats, Inbred Strains, pubmed-meshheading:2473191-Thionucleotides, pubmed-meshheading:2473191-Vasoconstriction
pubmed:year
1989
pubmed:articleTitle
Guanine nucleotide binding proteins may modulate gating of calcium channels in vascular smooth muscle. II. Studies with guanosine 5'-(gamma)triphosphate.
pubmed:affiliation
Department of Physiology, University of Alberta, Edmonton, Canada.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't