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

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

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

The ability of the chemotactic peptide N-formylmethionyl-leucyl-phenylalanine (FMLP) to stimulate beta-glucuronidase release and 45Ca2+ release from rabbit neutrophils was studied. FMLP stimulated enzyme release from cytochalasin B-treated cells either in the presence or the absence of extracellular calcium. Depletion of cell calcium, by exposure to either ethyleneglycol-bis(beta-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)
JournalThe American journal of physiology
Volume245
Issue number3
StatePublished - Sep 1983

Fingerprint

N-Formylmethionine Leucyl-Phenylalanine
Neutrophils
Calcimycin
Calcium
Enzymes
Cytochalasin B
Calcium Ionophores
Glucuronidase
Rabbits
Peptides
Acids

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Chandler, D., Meusel, G., Schumaker, E., & Stapleton, C. (1983). FMLP-induced enzyme release from neutrophils: a role for intracellular calcium. The American journal of physiology, 245(3).

FMLP-induced enzyme release from neutrophils : a role for intracellular calcium. / Chandler, D.; Meusel, G.; Schumaker, E.; Stapleton, C.

In: The American journal of physiology, Vol. 245, No. 3, 09.1983.

Research output: Contribution to journalArticle

Chandler, D, Meusel, G, Schumaker, E & Stapleton, C 1983, 'FMLP-induced enzyme release from neutrophils: a role for intracellular calcium.', The American journal of physiology, vol. 245, no. 3.
Chandler, D. ; Meusel, G. ; Schumaker, E. ; Stapleton, C. / FMLP-induced enzyme release from neutrophils : a role for intracellular calcium. In: The American journal of physiology. 1983 ; Vol. 245, No. 3.
@article{6851ec425b8a43ca9c5a744acbf39307,
title = "FMLP-induced enzyme release from neutrophils: a role for intracellular calcium.",
abstract = "The ability of the chemotactic peptide N-formylmethionyl-leucyl-phenylalanine (FMLP) to stimulate beta-glucuronidase release and 45Ca2+ release from rabbit neutrophils was studied. FMLP stimulated enzyme release from cytochalasin B-treated cells either in the presence or the absence of extracellular calcium. Depletion of cell calcium, by exposure to either ethyleneglycol-bis(beta-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.",
author = "D. Chandler and G. Meusel and E. Schumaker and C. Stapleton",
year = "1983",
month = "9",
language = "English (US)",
volume = "245",
journal = "American Journal of Physiology - Endocrinology and Metabolism",
issn = "0193-1849",
publisher = "American Physiological Society",
number = "3",

}

TY - JOUR

T1 - FMLP-induced enzyme release from neutrophils

T2 - a role for intracellular calcium.

AU - Chandler, D.

AU - Meusel, G.

AU - Schumaker, E.

AU - Stapleton, C.

PY - 1983/9

Y1 - 1983/9

N2 - The ability of the chemotactic peptide N-formylmethionyl-leucyl-phenylalanine (FMLP) to stimulate beta-glucuronidase release and 45Ca2+ release from rabbit neutrophils was studied. FMLP stimulated enzyme release from cytochalasin B-treated cells either in the presence or the absence of extracellular calcium. Depletion of cell calcium, by exposure to either ethyleneglycol-bis(beta-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.

AB - The ability of the chemotactic peptide N-formylmethionyl-leucyl-phenylalanine (FMLP) to stimulate beta-glucuronidase release and 45Ca2+ release from rabbit neutrophils was studied. FMLP stimulated enzyme release from cytochalasin B-treated cells either in the presence or the absence of extracellular calcium. Depletion of cell calcium, by exposure to either ethyleneglycol-bis(beta-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.

UR - http://www.scopus.com/inward/record.url?scp=0020826091&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020826091&partnerID=8YFLogxK

M3 - Article

C2 - 6412560

AN - SCOPUS:0020826091

VL - 245

JO - American Journal of Physiology - Endocrinology and Metabolism

JF - American Journal of Physiology - Endocrinology and Metabolism

SN - 0193-1849

IS - 3

ER -