Publication: Suppressive effect of rebamipide, an antiulcer agent, against activation of human neutrophils exposed toformyl-methionyl-leucyl-phenylalanine
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Date
2000
Authors
Kobayashi, T. ; Zinchuk, V.S. ; García del Saz, E. ; Jiang, F. ; Yamasaki, Y. ; Kataoka, S. ; Okada, T. ; Tsunawaki, S ; 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
Rebamipide, an antiulcer agent, has been
shown to be able to prevent gastric mucosal injury
resulting in part from activation of neutrophils. The
mechanism of its suppressive action, however, remains
to be established. The present study aimed to determine
the effect of rebamipide on activation of isolated human
neutrophils and to identify the signal transduction
pathway involved in its regulation. In unstimulated cells,
alkaline phosphatase activity was found residing in short
rod-shaped intracellular granules. Upon stimulation with
a chemotactic peptide formyl-methionyl-leucylphenylalanine,
the granules fused to form elongated
tubular structures and spherical vacuoles. Rebamipide
inhibited reorganization of alkaline phosphatasecontaining
granules along with upregulation of alkaline
phosphatase activity and CD16, a marker of the
granules. It also suppressed chemotaxis, an increase in
intracellular calcium ion concentration, and NADPH
oxidase activation in cells stimulated with formylmethionyl-
leucyl-phenylalanine. In contrast, the drug
showed no inhibitory action toward upregulation of
alkaline phosphatase activity and CD16, and activation
of NADPH oxidase in cells stimulated with phorbol
myristate acetate, an activator of protein kinase C. These
findings demonstrate that rebamipide exerts a broad
spectrum of suppressive actions toward biological
functions of human neutrophils stimulated with formylmethionyl-
leucyl-phenylalanine, but not with phorbol myristate acetate, and suggest that the upstream point of
protein kinase C is the signal transduction pathway
involved in its regulation.
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