PMID: 9443605Jan 27, 1998Paper

Positive and negative controls by protein kinases of sodium-dependent Ca2+ efflux from cultured bovine adrenal chromaffin cells stimulated by lysophosphatidic acid

Biochimica Et Biophysica Acta
A TokumuraM Oka

Abstract

We previously found that lysophosphatidic acid (LPA), a bioactive phospholipid, induced Na+-dependent Ca2+ efflux from cultured bovine adrenal chromaffin cells, possibly by activating a Na+/Ca2+ exchanger. The present study on the structure-activity relationship of its action revealed that 1-acyl type LPAs were stronger stimulants than the corresponding 1-O-alkyl type LPAs having a long alkyl moiety with the same chain length. Lysophosphatidylglycerol, suramin and N-palmitoyl-tyrosine phosphoric acid have all been reported to inhibit the action of LPA in some animal cells and platelets, but only lysophosphatidylglycerol was found to inhibit selectively LPA-induced Ca2+ efflux from chromaffin cells. LPA-induced Ca2+ extrusion was suggested to be involved in both acceleration of return of intracellular Ca2+ in Fura 2-loaded bovine chromaffin cells after addition of carbachol, and inhibition of carbachol-induced catecholamine release when the cells were co-incubated with LPA. The Ca2+ efflux from chromaffin cells stimulated by LPA was augmented by their pretreatment with staurosporine or calphostin C, inhibitors of protein kinase C, but reduced by their preincubation with phorbol 12-myristate 13-acetate. Furthermore, the response ...Continue Reading

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Citations

Apr 2, 2003·Pharmacology & Therapeutics·Philip D Marley
Jun 26, 2010·The Journal of Biological Chemistry·Ya-Chi YangLung-Sen Kao
May 23, 2008·Journal of Cellular and Molecular Medicine·Yan-Jun XuNaranjan S Dhalla
Apr 18, 2006·Neuropharmacology·Chien-Yuan PanChia-Lin Chen
May 1, 2001·The International Journal of Neuroscience·A M De Andrade PaesP C De Freitas Mathias
Mar 20, 1999·Biochimica Et Biophysica Acta·R DiPolo, L Beaugé

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