These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: The priming effect of 12(S)-hydroxyeicosatetraenoic acid on lymphocyte phospholipase D involves specific binding sites.
    Author: Zakaroff-Girard A, Dubois M, Gilbert M, Meskini N, Némoz G, Lagarde M, Prigent AF.
    Journal: Life Sci; 1999; 64(23):2135-48. PubMed ID: 10372655.
    Abstract:
    We have previously shown that 12(S)-hydroxyeicosatetraenoic acid (12(S)-HETE)-enrichment primed human peripheral blood mononuclear cells for phospholipase D activation by mitogens. Given that 12(S)-HETE-enriched cells stimulated with concanavalin A released free 12(S)-HETE in the extracellular medium, and that the priming effect of 12(S)-HETE on phospholipase D was suppressed by the non-permeant drug, suramin, we hypothesized an extracellular mechanism for 12(S)-HETE-induced PLD activation. Using [3H]12(S)-HETE as a ligand and a rapid filtration technique, we have pointed out the presence of specific low-affinity 12(S)-HETE binding sites on intact human mononuclear cells and lymphocytes. [3H]12(S)-HETE binding was efficiently displaced by other monohydroxylated and n-3 fatty acids but not by oleate and arachidonate, and was also significantly inhibited by suramin and pertussis toxin. Furthermore, 12(S)-HETE-induced PLD activation was strongly inhibited by pertussis toxin and genistein, but was not PKC-dependent. In addition, 12(S)-HETE also potentiated the ConA-induced tyrosine phosphorylation of a 46-50 kDa protein, which was inhibited by genistein. Collectively, these results suggest that 12(S)-HETE binding sites on human lymphocytes may be coupled to phospholipase D through pertussis toxin sensitive G-proteins and tyrosine kinases.
    [Abstract] [Full Text] [Related] [New Search]