Publication: Novel insight into current models of NADPH oxidase regulation, assembly and localization in human polymorphonuclear leukocytes
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Date
1999
Authors
Kobayashi, T. ; Seguchi, H.
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
We review herein the definition of the
NADPH oxidase-activating site in human neutrophils
and eosinophils, together with the new biochemical
findings of the assembly of NADPH oxidase
components and the signal transduction for the
activation of NADPH oxidase. The activation of this
enzyme is associated with multiple interrelated signaling
pathways. Upon cell stimulation, the second messengers
act on the assembly of NADPH oxidase components.
The cytosolic components are first phosphorylated, and
then associated with the membrane components. Small
GTP-binding proteins and cytoskeletal components also
participate in the activation of the NADPH oxidase. The
cytochemical findings demonstrate that the superoxide
generated by NADPH oxidase activity is initially
localized in distinct types of intracellular granules, and
not at the plasma membrane as previously believed.
Thus, the assembly of NADPH oxidase components
possibly occurs at the limiting membrane of the
intracellular compartments. The oxidant-producing
compartments mobilize and become associated with the
plasma membrane upon cell stimulation with soluble
stimulants, or fuse to phagosomes upon stimulation with
particulate stimulants. Accordingly, superoxide is
released to the extracellular space and into phagosomes
in proportion to the oxidant-producing intracellular
granule association with the plasma membrane and with
the phagosomal membrane, respectively.
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