| Autor: |
Ueyama T; Laboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University, Kobe, Japan., Lennartz MR, Noda Y, Kobayashi T, Shirai Y, Rikitake K, Yamasaki T, Hayashi S, Sakai N, Seguchi H, Sawada M, Sumimoto H, Saito N |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of immunology (Baltimore, Md. : 1950) [J Immunol] 2004 Oct 01; Vol. 173 (7), pp. 4582-9. |
| DOI: |
10.4049/jimmunol.173.7.4582 |
| Abstrakt: |
Protein kinase C (PKC) plays a prominent role in immune signaling. To elucidate the signal transduction in a respiratory burst and isoform-specific function of PKC during FcgammaR-mediated phagocytosis, we used live, digital fluorescence imaging of mouse microglial cells expressing GFP-tagged molecules. betaI PKC, epsilonPKC, and diacylglycerol kinase (DGK) beta dynamically and transiently accumulated around IgG-opsonized beads (BIgG). Moreover, the accumulation of p47(phox), an essential cytosolic component of NADPH oxidase and a substrate for betaI PKC, at the phagosomal cup/phagosome was apparent during BIgG ingestion. Superoxide (O(2)(-)) production was profoundly inhibited by Gö6976, a cPKC inhibitor, and dramatically increased by the DGK inhibitor, R59949. Ultrastructural analysis revealed that BIgG induced O(2)(-) production at the phagosome but not at the intracellular granules. We conclude that activation/accumulation of betaI PKC is involved in O(2)(-) production, and that O(2)(-) production is primarily initiated at the phagosomal cup/phagosome. This study also suggests that DGKbeta plays a prominent role in regulation of O(2)(-) production during FcgammaR-mediated phagocytosis. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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