Linked Life Data

17804611

Source:http://linkedlifedata.com/resource/pubmed/id/17804611

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2007-11-6
pubmed:abstractText
The involvement of group VI Ca(2+)-independent PLA(2)s (iPLA(2)-VI) in in vitro ischemia [oxygen and glucose deprivation (OGD)] in mouse C2C12 myotubes was investigated. OGD induced a time-dependent (0-6 h) increase in bromoenol lactone (BEL)-sensitive iPLA(2) activity, which was suppressed by specific short interfering (si)RNA knockdown of iPLA(2)-VIA. OGD was associated with an increase in iPLA(2)-VIA protein levels, whereas mRNA levels were unchanged. The levels of iPLA(2)-VIB mRNA and protein were not increased by OGD. RT-PCR and Western blot analysis identified a mouse iPLA(2)-VIA homolog to catalytically inactive 50-kDa iPLA(2)-VIA-ankyrin variants previously identified in humans. Both the mRNA and protein levels of this approximately 50-kDa variant were reduced significantly within 1 h following OGD. In C2C12 myoblasts, iPLA(2)-VIA seemed to predominantly reside at the endoplasmatic reticulum, where it accumulated further during OGD. A time-dependent reduction in cell viability during the early OGD period (3 h) was partially prevented by iPLA(2)-VIA knockdown or pharmacological inhibition (10 microM BEL), whereas iPLA(2)-VIA overexpression had no effect on cell viability. Taken together, these data demonstrate that OGD in C2C12 myotubes is associated with an increase in iPLA(2)-VIA activity that decreases cell viability. iPLA(2)-VIA activation may be modulated by changes in the levels of active and inactive iPLA(2)-VIA isoforms.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0363-6143
pubmed:author
pubmed:issnType
Print
pubmed:volume
293
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
C1605-15
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:17804611-Animals, pubmed-meshheading:17804611-Arachidonic Acids, pubmed-meshheading:17804611-Cell Hypoxia, pubmed-meshheading:17804611-Cell Line, pubmed-meshheading:17804611-Cell Survival, pubmed-meshheading:17804611-Endoplasmic Reticulum, pubmed-meshheading:17804611-Enzyme Induction, pubmed-meshheading:17804611-Glucose, pubmed-meshheading:17804611-Group IV Phospholipases A2, pubmed-meshheading:17804611-Ischemia, pubmed-meshheading:17804611-Mice, pubmed-meshheading:17804611-Molecular Weight, pubmed-meshheading:17804611-Muscle, Skeletal, pubmed-meshheading:17804611-Muscle Fibers, Skeletal, pubmed-meshheading:17804611-Naphthalenes, pubmed-meshheading:17804611-Phosphodiesterase Inhibitors, pubmed-meshheading:17804611-Protein Isoforms, pubmed-meshheading:17804611-Pyrones, pubmed-meshheading:17804611-RNA, Messenger, pubmed-meshheading:17804611-RNA, Small Interfering, pubmed-meshheading:17804611-RNA Interference, pubmed-meshheading:17804611-Time Factors
pubmed:year
2007
pubmed:articleTitle
Induction of group VIA phospholipase A2 activity during in vitro ischemia in C2C12 myotubes is associated with changes in the level of its splice variants.
pubmed:affiliation
Dept. of Molecular Biology, Univ. of Copenhagen, Universitetsparken 13, Copenhagen Ø DK-2100, Denmark. kapoulsen@aki.ku.dk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't