PHOSPHORYLATION-ASSOCIATED CONFORMATION SHIFT OF ANTIONCOGENE PHOSPHOPROTEIN P53 IN CONCANAVALIN-A ACTIVATED HUMAN LYMPHOCYTES-T

被引:6
作者
MCCLURE, JE
MCCLURE, JA
SHEARER, WT
机构
[1] BAYLOR COLL MED,DEPT MICROBIOL,HOUSTON,TX 77030
[2] BAYLOR COLL MED,DEPT IMMUNOL,HOUSTON,TX 77030
[3] BAYLOR COLL MED,DEPT MOLEC VIROL,HOUSTON,TX 77030
[4] TEXAS CHILDRENS HOSP,ALLERGY IMMUNOL SERV,HOUSTON,TX 77030
关键词
D O I
10.1016/0006-291X(92)90274-O
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
A new radioimmunoassay for p53, employing an anti-peptide antibody directed against conserved Domain V, exhibited specificity for a relatively dephosphorylated form of p53. This form, correlated with the monoclonal antibody PAB421+ conformation, appeared transiently in the cytosol of cycloheximide-treated T cells undergoing activation by concanavalin-A/serum. Concurrently, there were decreased levels of p53 in the nucleus that correlated with increased phosphorylation of p53. After 90 min nuclear levels of p53 increased steadily above levels of unstimulated cells. Anti-p53 antibodies introduced into cells prior to stimulation enhanced cell proliferation in response to mitogens. © 1992.
引用
收藏
页码:1701 / 1708
页数:8
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