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伴刀豆球蛋白A激活的人T淋巴细胞中抗癌基因磷酸蛋白p53的磷酸化相关构象转变

Phosphorylation-associated conformation shift of anti-oncogene phosphoprotein p53 in concanavalin-A activated human T lymphocytes.

作者信息

McClure J E, McClure J A, Shearer W T

机构信息

Department of Pediatrics, Baylor College of Medicine, Houston, TX 77030.

出版信息

Biochem Biophys Res Commun. 1992 Dec 30;189(3):1701-8. doi: 10.1016/0006-291x(92)90274-o.

DOI:10.1016/0006-291x(92)90274-o
PMID:1482375
Abstract

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.

摘要

一种新的针对p53的放射免疫分析方法,采用针对保守结构域V的抗肽抗体,对相对去磷酸化形式的p53具有特异性。这种形式与单克隆抗体PAB421+构象相关,在经环己酰亚胺处理、由伴刀豆球蛋白A/血清激活的T细胞胞质溶胶中短暂出现。同时,细胞核中p53水平降低,这与p53磷酸化增加相关。90分钟后,细胞核中p53水平稳定上升,高于未受刺激细胞的水平。在刺激前引入细胞的抗p53抗体可增强细胞对有丝分裂原的增殖反应。

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