Potentiation of the oxidative burst of human neutrophils. A signaling role for L-selectin

Production of reactive oxygen intermediates (ROI) by the NADPH oxidase of neutrophils is a major mechanism of bacterial killing and, in pathologic circumstances, tissue damage. Integrins and selectins participate in neutrophil adhesion but may also play a role in intracellular signaling. The role of...

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Bibliographic Details
Published in:The Journal of biological chemistry 1994-07, Vol.269 (28), p.18485-18491
Main Authors: WADDELL, T. K, FIALKOW, L, CHI KIN CHAN, KISHIMOTO, T. K, DOWNEY, G. P
Format: Article
Language:English
Subjects:
Antibodies - pharmacology
Biological and medical sciences
Calcium - blood
Cell Adhesion
Cell Adhesion Molecules - blood
Cell Adhesion Molecules - immunology
Cell Adhesion Molecules - physiology
Cell physiology
Cross-Linking Reagents
Egtazic Acid - analogs & derivatives
Egtazic Acid - pharmacology
Fluorescent Dyes
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Fura-2 - analogs & derivatives
Humans
Immunobiology
Immunoglobulin Fab Fragments - pharmacology
In Vitro Techniques
Kinetics
L-Selectin
Molecular and cellular biology
Myeloid cells: ontogeny, maturation, markers, receptors
N-Formylmethionine Leucyl-Phenylalanine - pharmacology
NADH, NADPH Oxidoreductases - blood
NADPH Oxidases
Neutrophils - drug effects
Neutrophils - metabolism
Neutrophils - physiology
Polynuclears
Rhodamines - pharmacology
Scopoletin - pharmacology
Signal transduction
Signal Transduction - drug effects
Spectrometry, Fluorescence
Superoxides - metabolism
Tumor Necrosis Factor-alpha - pharmacology
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Summary:Production of reactive oxygen intermediates (ROI) by the NADPH oxidase of neutrophils is a major mechanism of bacterial killing and, in pathologic circumstances, tissue damage. Integrins and selectins participate in neutrophil adhesion but may also play a role in intracellular signaling. The role of L-selectin in ROI production and Ca2+ signaling in suspended neutrophils was examined using the DREG series of anti-L-selectin antibodies. NADPH oxidase activation was assessed in three ways: H2O2 production using either scopoletin or dihydrorhodamine and O2- production using cytochrome c. Alterations in [Ca2+]i were measured using Fura 2-AM and fluorescence spectrophotometry. Cross-linking of L-selectin with DREG and 2 degrees antibody did not trigger production of H2O2 by itself but significantly enhanced the subsequent response to two soluble activating agents; the formyl peptide formyl-Met-Leu-Phe (fMLP) and tumor necrosis factor (TNF). Potentiation of the oxidative burst was observed using F(ab')2 fragments but not with irrelevant antibodies and was observed whether 2 degrees antibody was added before or after fMLP. Cross-linking of L-selectin also triggered a rise in [Ca2+]i, due, in part, to release from intracellular stores. The intracellular Ca2+ chelator BAPTA blocked both the rise in [Ca2+]i and the potentiation of the oxidative burst in response to fMLP or TNF. We conclude that cross-linking of L-selectin induces intracellular signals, including release of Ca2+, which may contribute to potentiation of the oxidative burst.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(17)32335-9