Linked Life Data

18045856

Source:http://linkedlifedata.com/resource/pubmed/id/18045856

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2008-2-15
pubmed:abstractText
Phospholamban (PLB) inhibits the sarcoplasmic reticulum (SR) Ca(2+)-ATPase (SERCA), and this inhibition is relieved by Ca(2+) calmodulin-dependent protein kinase II (CaM kinase II) phosphorylation. We previously reported significant differences in contractility, SR Ca(2+) release, and CaM kinase II activity in gastric fundus smooth muscles as a result of PLB phosphorylation by CaM kinase II. In this study, we used PLB-knockout (PLB-KO) mice to directly examine the effect of PLB absence on contractility, CaM kinase II activity, and intracellular Ca(2+) waves in gastric antrum smooth muscles. The frequencies and amplitudes of spontaneous phasic contractions were elevated in antrum smooth muscle strips from PLB-KO mice. Bethanecol increased the amplitudes of phasic contractions in antrum smooth muscles from both control and PLB-KO mice. Caffeine decreased and cyclopiazonic acid (CPA) increased the basal tone of antrum smooth muscle strips from PLB-KO mice, but the effects were less pronounced compared with control strips. The CaM kinase II inhibitor KN-93 was less effective at inhibiting caffeine-induced relaxation in antrum smooth muscle strips from PLB-KO mice. CaM kinase II autonomous activity was elevated, and not further increased by caffeine, in antrum smooth muscles from PLB-KO mice. Similarly, the intracellular Ca(2+) wave frequency was elevated, and not further increased by caffeine, in antrum smooth muscles from PLB-KO mice. These findings suggest that PLB is an important modulator of gastric antrum smooth muscle contractility by modulation of SR Ca(2+) release and CaM kinase II activity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0363-6143
pubmed:author
pubmed:issnType
Print
pubmed:volume
294
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
C432-41
pubmed:meshHeading
pubmed-meshheading:18045856-Action Potentials, pubmed-meshheading:18045856-Animals, pubmed-meshheading:18045856-Caffeine, pubmed-meshheading:18045856-Calcium Signaling, pubmed-meshheading:18045856-Calcium-Binding Proteins, pubmed-meshheading:18045856-Calcium-Calmodulin-Dependent Protein Kinase Type 2, pubmed-meshheading:18045856-Down-Regulation, pubmed-meshheading:18045856-Enzyme Inhibitors, pubmed-meshheading:18045856-Indoles, pubmed-meshheading:18045856-Intracellular Fluid, pubmed-meshheading:18045856-Mice, pubmed-meshheading:18045856-Mice, Knockout, pubmed-meshheading:18045856-Muscle, Smooth, pubmed-meshheading:18045856-Muscle Contraction, pubmed-meshheading:18045856-Peristalsis, pubmed-meshheading:18045856-Phosphodiesterase Inhibitors, pubmed-meshheading:18045856-Pyloric Antrum, pubmed-meshheading:18045856-Sarcoplasmic Reticulum
pubmed:year
2008
pubmed:articleTitle
Phospholamban knockout increases CaM kinase II activity and intracellular Ca2+ wave activity and alters contractile responses of murine gastric antrum.
pubmed:affiliation
Department of Physiology and Cell Biology, University of Nevada School of Medicine, Reno, NV 89557, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural