PKC-dependent phosphorylation of Munc18a at Ser313 in activated RBL-2H3 cells

Protein Kinase C (PKC) regulates the release of pro-inflammatory compounds from IgE/antigen-activated mast cells by unknown mechanisms. In this study, we show for the first time that PKC inhibitor Ro-03-0432, which inhibits RBL-2H3 exocytosis/degranulation in a concentration-dependent fashion, preve...

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Veröffentlicht in:	Inflammation research 2018-01, Vol.67 (1), p.1-3
Hauptverfasser:	Adhikari, Pratikshya, Xu, Hao
Format:	Artikel
Sprache:	eng
Schlagworte:	Allergology Animals Biomedical and Life Sciences Biomedicine Cell Degranulation Cell Line, Tumor Degranulation Dermatology Exocytosis Immunoglobulin E Immunology Indoles - pharmacology Inflammation Kinases Mast cells Mast Cells - physiology Membrane fusion Munc18 Proteins - metabolism Neurology Pharmacology/Toxicology Phosphorylation Protein kinase C Protein Kinase C - antagonists & inhibitors Protein Kinase C - metabolism Pyrroles - pharmacology Rats Rheumatology Short Communication
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Beschreibung
Zusammenfassung:	Protein Kinase C (PKC) regulates the release of pro-inflammatory compounds from IgE/antigen-activated mast cells by unknown mechanisms. In this study, we show for the first time that PKC inhibitor Ro-03-0432, which inhibits RBL-2H3 exocytosis/degranulation in a concentration-dependent fashion, prevents the phosphorylation of membrane fusion factor Munc18a at Ser 313. Our study provides fresh evidence that PKC-dependent protein phosphorylation may contribute to the intricate regulation of mast cell degranulation by directly targeting the fusion factors.
ISSN:	1023-3830 1420-908X
DOI:	10.1007/s00011-017-1097-4