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Protein Kinase C Inhibition by ET-18-OCH3 and Related Analogs

A Target for Cancer Chemotherapy
  • Susan B. Pauig
  • Lary W. Daniel
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 416)

Abstract

Protein kinase C (PKC), is an important component of signal transduction mechanisms involving many physiological and pharmacological agonists1. While many isoforms are known2,3, those isoforms which are responsive to the phorbol ester, TPA4, and the lipid second messenger, diacylglycerol (DAG)5 are the most completely characterized. PKC activation is a necessary component for TPA induced differentiation of the human acute myelogenous leukemia cell line, HL-606–9. However, PKC activation does not appear to be required for tumor necrosis factor α (TNFα) induced differentiation10. PKC may be involved in differentiation induced by vitamin D3 and all-trans retinoic acid, since both cause upregulation of PKC isozyme levels11,12. Differentiation induction therapy provides an alternative therapeutic approach for patients with acute myeloid leukemia (AML) who are either unsuitable for or unreponsive to conventional cytotoxic chemotherapy13,14.

Keywords

Acute Myeloid Leukemia Phorbol Ester Ether Lipid Monocytic Differentiation Phorbol Diester 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1996

Authors and Affiliations

  • Susan B. Pauig
    • 1
  • Lary W. Daniel
    • 1
  1. 1.Department of Biochemistry Bowman Gray School of MedicineWake Forest UniversityWinston-SalemUSA

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