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

Andrew Kraft, C. Appling, R. L. Berkow

Research output: Contribution to journalArticle

8 Citations (Scopus)

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 comments that activate protein kinase C may increase nuclear binding of PE in situ.

Original languageEnglish (US)
Pages (from-to)393-401
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume144
Issue number1
DOIs
StatePublished - Apr 14 1987
Externally publishedYes

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Phorbol Esters
Protein Kinase C
Leukemia
HL-60 Cells
Egtazic Acid
Calcium
Cell Nucleus
Buffers
Experiments

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Specific binding of phorbol esters to nuclei of human promyelocytic leukemia cells. / Kraft, Andrew; Appling, C.; Berkow, R. L.

In: Biochemical and Biophysical Research Communications, Vol. 144, No. 1, 14.04.1987, p. 393-401.

Research output: Contribution to journalArticle

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