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EBV membrane receptor (CR2) is phosphorylated by protein kinase C (PKC) in the early stages of virus entry into lymphoblastoid cells line (Raji).
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1993 Oct 29; Vol. 196 (2), pp. 794-802. - Publication Year :
- 1993
-
Abstract
- Labeling the EBV membrane with octadecylrhodamine-b-chloride (R18) we were able to monitor spectrofluorometrically the early events of EBV fusion, under conditions in which we could affect PKC activity. Binding of EBV to Raji cells induces PKC translocation from the cytosol to the plasma membrane and 32P incorporation into its cellular receptor CR2. CR2 phosphorylation is completely inhibited when cells are preincubated with the PKC inhibitor calphostin c. This treatment also generates a strong inhibition of EBV fusion. Taken together this result suggests a key role of CR2 phosphorylation in the EBV entry into Raji cells.
- Subjects :
- Adenosine Triphosphate metabolism
Cytosol metabolism
Fluorescent Dyes
Humans
Ionomycin pharmacology
Kinetics
Lymphoma
Membrane Fusion drug effects
Phosphates metabolism
Phosphorus Radioisotopes
Phosphorylation
Polycyclic Compounds pharmacology
Protein Kinase C antagonists & inhibitors
Receptors, Complement 3d
Receptors, Virus drug effects
Rhodamines
Tetradecanoylphorbol Acetate pharmacology
Tumor Cells, Cultured
Cell Membrane metabolism
Herpesvirus 4, Human physiology
Naphthalenes
Protein Kinase C metabolism
Receptors, Virus metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 196
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 7694579
- Full Text :
- https://doi.org/10.1006/bbrc.1993.2319