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Endothelin‐1 does not modulate O 2 · release and [Ca 2+ ] i variations in resting or differentiated HL‐60 cells
Author(s) -
Gallois A.,
Bueb JL,
Tschirhart E.
Publication year - 1996
Publication title -
fundamental and clinical pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.655
H-Index - 73
eISSN - 1472-8206
pISSN - 0767-3981
DOI - 10.1111/j.1472-8206.1996.tb00146.x
Subject(s) - phosphoramidon , chemotaxis , chemistry , neprilysin , superoxide , calcium , intracellular , endothelin 1 , biophysics , microbiology and biotechnology , endocrinology , medicine , biochemistry , biology , receptor , enzyme , organic chemistry
Summary— Endothelin‐1 (ET‐1) by itself was not an effective stimulus for inducing superoxide (O 2 *) generation in human resting or DMSO‐differentiated neutrophil‐like HL‐60 cells. ET‐1 (0.01 – 100 nM) was not able to modulate O 2 * generation stimulated by the chemotactic peptide N‐formyl‐L‐methionyl‐L‐leucyl‐L‐phenylalanine (fMLP, EC 50 = 4.24 ± 1.63 nM in the absence and 3.16 ± 1.95 nM in the presence of ET‐1). Neither did ET‐1 (0.01 – 100 nM) promote the mobilization of intracellular calcium ions or modulate fMLP‐induced [Ca 2+ ] i increase in this model of human neutrophils. Phosphoramidon, a neutral endopeptidase inhibitor, was not able to reveal any biological (O 2 *) or biochemical ([Ca 2+ ] i ) response to ET‐1 in the absence or in the presence of fMLP in these cells. These results indicate that DMSO‐differentiated neutrophil‐like HL‐60 cells are not sensitive to ET‐1 in terms of O 2 * generation or [Ca 2+ ] i variations.