PHOSPHORYLATION OF HUMAN TOPOISOMERASE-I BY PROTEIN-KINASE-C INVITRO AND IN PHORBOL 12-MYRISTATE 13-ACETATE-ACTIVATED HL-60 PROMYELOCYTIC LEUKEMIA-CELLS

被引：33

作者：

CARDELLINI, E ^{[1
]}

DURBAN, E ^{[1
]}

机构：

[1] BAYLOR COLL MED, DEPT PHARMACOL, HOUSTON, TX 77030 USA

来源：

BIOCHEMICAL JOURNAL | 1993年 / 291卷

关键词：

D O I：

10.1042/bj2910303

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：

Topoisomerase I was phosphorylated in vitro by protein kinase C (PKC) purified from rat brain with high affinity (K(m) about 0.1 muM). Tryptic phosphopeptide mapping indicated that two major topoisomerase I peptides phosphorylated in vivo were comigrating with minor peptides phosphorylated by PKC in vitro. Topoisomerase I phosphorylation was stimulated 3-fold in HL-60 cells exposed to the tumour promoter phorbol 12-myristate 13-acetate. The results suggest that topoisomerase I phosphorylation in HL-60 cells is indirectly controlled by PKC.

引用

页码：303 / 307

页数：5

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