Specific binding of phorbol esters to nuclei of human promyelocytic leukemia cells.

Abstract:

:In this report, we demonstrate that HL-60 nuclei isolated in calcium but not EGTA containing buffers specifically bind PE and express approximately 37,000 receptor sites/nucleus. Nuclear phorbol ester binding is lost by isolation in the absence of calcium, but can be repleted by the addition of partially purified protein kinase C and calcium. When HL-60 cells are treated with bryostatin 1, a compound which activates protein kinase C in a similar fashion to phorbol esters but does not induce differentiation of HL-60 cells, and nuclei are isolated in the presence of EGTA, these nuclei continue to bind phorbol esters. These experiments suggest that HL-60 nuclei bind PE in vitro, and that compounds that activate protein kinase C may increase nuclear binding of PE in situ.

authors

Kraft AS,Appling C,Berkow RL

doi

10.1016/s0006-291x(87)80523-5

subject

Has Abstract

pub_date

1987-04-14 00:00:00

pages

393-401

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(87)80523-5

journal_volume

144

pub_type

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