Unknown

Dataset Information

0

Protein kinase C-beta contributes to NADPH oxidase activation in neutrophils.


ABSTRACT: We have analysed the involvement of the beta isotype of the protein kinase C (PKC) family in the activation of NADPH oxidase in primary neutrophils. Using immunofluorescence and cell fractionation, PKC-beta is shown to be recruited to the plasma membrane upon stimulation with phorbol ester and to the phagosomal membrane upon phagocytosis of IgG-coated particles (Fcgamma-receptor stimulus). The time course of recruitment is similar to that of NADPH oxidase activation by these stimuli. The PKC-beta specific inhibitor 379196 inhibits the response to PMA as well as to IgG-coated bacteria. Partial inhibition occurs between 10 and 100 nM of inhibitor, the concentration at which PKC-beta, but not other PKC isotypes, is targeted. Neutrophils isolated from a mouse that lacks PKC-beta also showed an inhibition of NADPH oxidase activation by PMA and IgG-coated particles. The level of inhibition is comparable to that achieved with 379196 in human neutrophils. Thus the PKC-beta isotype mediates activation of NADPH oxidase by PMA and by stimulation of Fcgamma receptors in neutrophils.

SUBMITTER: Dekker LV 

PROVIDER: S-EPMC1220958 | biostudies-other | 2000 Apr

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC5123718 | biostudies-literature
| S-EPMC1222456 | biostudies-other
| S-EPMC6829599 | biostudies-literature
| S-EPMC3666735 | biostudies-literature
| S-EPMC3914983 | biostudies-literature
| S-EPMC6320503 | biostudies-literature
| S-EPMC5133656 | biostudies-literature
| S-EPMC6770146 | biostudies-literature
| S-EPMC3534805 | biostudies-literature
| S-EPMC1137813 | biostudies-other