Phosphorylation of human topoisomerase I by protein kinase C in vitro and in phorbol 12-myristate 13-acetate-activated HL-60 promyelocytic leukaemia cells

Author:

Cardellini E1,Durban E1

Affiliation:

1. Department of Pharmacology, Baylor College of Medicine, Houston, TX 77030 U.S.A.

Abstract

Topoisomerase I was phosphorylated in vitro by protein kinase C (PKC) purified from rat brain with high affinity (Km about 0.1 microM). 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.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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