FMLP-induced enzyme release from neutrophils: A role for intracellular calcium

D. Chandler, G. Meusel, E. Schumaker, C. Stapleton

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

The ability of the chemotactic peptide N-formylmethionyl-leucyl-phenylalanine (FMLP) to stimulate β-glucuronidase release and 45Ca2+ release from rabbit neutrophils was studied. FMLP stimulated enzyme release from cytochalasin B-treated cells either in the presence or absence of extracellular calcium. Depletion of cell calcium, by exposure to either ethyleneglycol-bis(β-aminoethylether)-N,N'-tetraacetic acid or the calcium ionophore A23187, blocked the ability of FMLP to stimulate enzyme release and 45Ca2+ release in the absence of extracellular calcium. The ability of A23187 to lower the 45Ca2+ content of neutrophils, to block FMLP-stimulated 45Ca2+ release, and to inhibit FMLP-stimulated enzyme release in the absence of calcium was dose dependent over the same concentration range (10-8 to 10-6 M A23187) for all three actions. In contrast, FMLP stimulated enzyme release from A23187-treated cells, provided that extracellular calcium was present. This secretory response was normal as judged by cell ultrastructure and FMLP dose-response relationships. It is concluded that A23187 depletes a pool of intracellular calcium usually released by FMLP and that release of calcium from this pool is necessary for initiation of enzyme secretion in the absence of extracellular calcium.

Original languageEnglish (US)
Pages (from-to)C196-C202
JournalAmerican Journal of Physiology - Cell Physiology
Volume14
Issue number2
StatePublished - Jan 1 1983

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

Fingerprint

Dive into the research topics of 'FMLP-induced enzyme release from neutrophils: A role for intracellular calcium'. Together they form a unique fingerprint.

Cite this