Linked Life Data

9726638

Source:http://linkedlifedata.com/resource/pubmed/id/9726638

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-11-9
pubmed:abstractText
On the background of the emerging concept of G protein-coupled sphingolipid receptors, Ca2+ mobilization by sphingosylphosphorylcholine (SPPC) in intact cells and SPPC-induced Ca2+ release in permeabilized cells, both occurring at similar, micromolar concentrations, were characterized and compared. In intact human embryonic kidney (HEK-293) cells, SPPC rapidly increased [Ca2+]i by mobilization of Ca2+ from thapsigargin-sensitive stores. In saponin-permeabilized HEK-293 cells, SPPC released stored Ca2+, in a manner similar to but independent of inositol 1,4,5-trisphosphate. Only the action of SPPC on intact cells, but not that in permeabilized cells, was, at least in part, sensitive to pertussis toxin. In addition and most important, Ca2+ release by SPPC in permeabilized cells was not stereoselective, whereas in intact cells only the naturally occurring D-erythro-SPPC, but not L-threo-SPPC, increased [Ca2+]i. Stereoselectivity of SPPC-induced [Ca2+]i increase was also demonstrated in bovine aortic endothelial cells. In conclusion, Ca2+ mobilization by SPPC in intact cells is independent of the previously described SPPC-gated Ca2+ channel on endoplasmic reticulum but probably mediated by a membrane sphingolipid receptor. Thus, SPPC can regulate Ca2+ homeostasis by acting apparently at two cellular targets, which exhibit clearly distinct recognition patterns.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-2999
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
354
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
113-22
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Discrimination between plasma membrane and intracellular target sites of sphingosylphosphorylcholine.
pubmed:affiliation
Institut für Pharmakologie, Universitätsklinikum Essen, Germany. meyer-heringdorf@uni-essen.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't