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Priming of human neutrophils with N-formyl-methionyl-leucyl- phenylalanine
by a calcium-independent, pertussis toxin-insensitive pathway
AB Karnad, KL Hartshorn, J Wright, JB Myers, JH Schwartz and AI Tauber
William B. Castle Research Hematology Laboratory, Boston City Hospital, MA.
Resting neutrophils may be "primed" to augmented effector function, eg,
superoxide (O2-) production in the respiratory burst, upon a second
stimulation with a variety of soluble agonists including formylated
methionyl-leucyl-phenylalanine (FMLP) and phorbol myristate acetate (PMA).
At priming concentrations of FMLP (5 x 10(-9) mol/L) that did not initiate
O2- generation, two metabolic activities were noted: (1) approximately a
threefold increase in the baseline intracellular calcium (Ca++i) level,
that was not dependent on extracellular Ca++, and (2) a rapid rise in
intracellular pH that was blocked by 5-(N,N- dimethyl) amiloride (DA), that
had no effect on the Ca++i response to priming. Furthermore, there were no
significant increases in inositol metabolites in cells primed and
stimulated with FMLP compared with cells receiving the stimulating dose of
FMLP alone and pretreatment with pertussis toxin (PT) (before the addition
of the priming -5 x 10(- 9) mol/L dose of FMLP), whereas abolishing the
response to FMLP during the second stage of stimulation, had (1) no effect
on FMLP-primed cells subsequently stimulated with PMA, and (2) only
partially ablated the rise in Ca++i initiated with FMLP. That FMLP priming
involved distinctive processes to those of the well characterized
FMLP-coupled Ca++-dependent activation cascade was shown by the full
priming effect attained in a Ca++-free buffer, which did not sustain an O2-
response to a second-stage FMLP stimulation, but sustained a primed
response to PMA. These data demonstrate that FMLP primes human neutrophils
by a Ca++-independent and PT-insensitive pathway, offering a functional
model for studying heterogeneous FMLP receptor-coupled reactions.
Volume 74,
Issue 7,
pp. 2519-2526,
11/15/1989
Copyright © 1989 by The American Society of Hematology
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