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Phospholipase C‐mediated signalling is not required for histamine‐induced catecholamine secretion from bovine chromaffin cells
Author(s) -
Donald Amanda N.,
Wallace Damian J.,
McKenzie Sacha,
Marley Philip D.
Publication year - 2002
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.2002.00915.x
Subject(s) - histamine , medicine , endocrinology , phospholipase c , chemistry , inositol trisphosphate , biology , inositol , receptor , biochemistry
A possible role for signalling through phospholipase C in histamine‐induced catecholamine secretion from bovine adrenal chromaffin cells has been investigated. Secretion evoked by histamine over 10 min was not prevented by inhibiting inositol‐1,4,5‐trisphosphate receptors with 2‐APB, by blocking ryanodine receptors with a combination of ryanodine and caffeine, or by depleting intracellular Ca 2+ stores by pretreatment with thapsigargin. Inhibition of protein kinase C with Ro31‐8220 also failed to reduce secretion. Inhibition of phospholipase C with ET‐18‐OCH 3 reduced both histamine‐ and K + ‐induced inositol phosphate responses by 70–80% without reducing their secretory responses. Stimulating phospholipase C with Pasteurella multocida toxin did not evoke secretion or enhance the secretory response to histamine. The secretory response to histamine was little affected by tetrodotoxin or by substituting extracellular Na + with N ‐methyl‐ d ‐glucamine + or choline + , or by substituting external Cl – with nitrate – . Blocking various K + channels with apamin, charybdotoxin, Ba 2+ , tetraethylammonium, 4‐aminopyridine, tertiapin or glibenclamide failed to reduce the ability of histamine to evoke secretion. These results indicate that histamine evokes secretion by a mechanism that does not require inositol‐1,4,5‐trisphosphate‐mediated mobilization of stored Ca 2+ , diacylglycerol‐mediated activation of protein kinase C, or activation of phospholipase C. The results are consistent with histamine acting by depolarizing chromaffin cells through a phospholipase C‐independent mechanism.