Control of actin conformation in AML myeloblasts: The effects of bryostatin and TPA

Ronald L. Sham, Charles H. Packman, Camille N. Abboud, Marshall A. Lichtman

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

Protein kinase C (PKC), an enzyme involved in signal transduction, is the receptor for both the tumor-promoting phorbol esters and the anti-neoplastic bryostatins. In many cells, phorbol esters and bryostatins cause similar effects; we have found that both agents increase actin polymerization in neutrophils. In some cells, however, the two agents result in different cell processes; we have found consistently different effects of these agents on actin conformation in myeloblasts obtained from leukemic patients. The patients tested all had increases in F-actin in response to 12-O-tetradecanoylphorbol-13-acetate (TPA) and most had decreases in F-actin in response to bryostatin. The data suggests that leukemic myeloblasts have a different cytoskeletal response to a tumor promoter and an antineoplastic agent despite their common receptor.

Original languageEnglish
Pages (from-to)863-868
Number of pages6
JournalLeukemia Research
Volume14
Issue number10
DOIs
StatePublished - 1990

Keywords

  • Actin
  • bryostatin
  • leukemia
  • myeloblast
  • phorbol ester
  • protein kinase C

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