Phorbol myristate acetate-induced NADPH oxidase activity in human neutrophils: only half the story has been told.

Abstract:

:The paradigm for activation of the neutrophil NADPH oxidase with the protein kinase C activator phorbol myristate acetate (PMA) states that the oxidase assembles the plasma membrane and that the metabolites generated are released extracellularly. This paradigm is challenged by the results presented. Most of the PMA-induced oxidase activity measured as chemiluminescence and dichlorofluorescein fluorescence was insensitive to scavengers of superoxide anion and hydrogen peroxide. This indicates that oxidase activity also takes place in a cellular compartment that the scavengers cannot reach. From the results obtained with granule-deficient HL-60 cells and cord blood neutrophils, we suggest that the scavenger-insensitive part of the NADPH oxidase activity in normal neutrophils resides in an intracellular compartment identical to or originating from granules. Our results also indicate that specific and azurophil granules have to be in very close contact to allow the generated oxygen metabolites to reach and react with myeloperoxidase.

journal_name

J Leukoc Biol

authors

Lundqvist H,Follin P,Khalfan L,Dahlgren C

doi

10.1002/jlb.59.2.270

subject

Has Abstract

pub_date

1996-02-01 00:00:00

pages

270-9

issue

2

eissn

0741-5400

issn

1938-3673

journal_volume

59

pub_type

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