EBV MEMBRANE-RECEPTOR (CR-2) IS PHOSPHORYLATED BY PROTEIN-KINASE-C (PKC) IN THE EARLY STAGES OF VIRUS ENTRY INTO LYMPHOBLASTOID-CELLS LINE (RAJI)

被引：11

作者：

AQUINO, A

LISI, A

POZZI, D

RAVAGNAN, G

GRIMALDI, S

机构：

[1] UNIV ROMA LA SAPIENZA,DIPARTIMENTO MED SPERIMENTALE,I-00185 ROME,ITALY

[2] CNR,IST MED SPERIMENTALE,I-00137 ROME,ITALY

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1993年 / 196卷 / 02期

关键词：

D O I：

10.1006/bbrc.1993.2319

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Labeling the EBV membrane with octadecilrhodamine-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. © 1993 Academic Press. All rights reserved.

引用

页码：794 / 802

页数：9

共 32 条

[1]

AQUINO A, 1988, CANCER RES, V48, P3324

[2]

BAICHWALL V, 1988, CELL, V52, P702

[3] ACTIVATORS OF PROTEIN KINASE-C DOWN-REGULATE AND PHOSPHORYLATE THE T3/T-CELL ANTIGEN RECEPTOR COMPLEX OF HUMAN LYMPHOCYTES-T [J].