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

A. S. Kraft, C. Appling, R. L. Berkow

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


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
Issue number1
StatePublished - Apr 14 1987

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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