Inhibition of leukemic cell growth by the protein kinase C activator bryostatin 1 correlates with the dephosphorylation of cyclin-dependent kinase 21

Clement Asiedu, Joseph Biggs, Andrew Kraft, Andrew S. Kraft

Research output: Contribution to journalArticle

63 Citations (Scopus)

Abstract

Bryostatin 1 is a natural antineoplastic agent that activates protein kinase C. Treatment of U937 human leukemic cells with bryostatin 1 caused a 60% reduction in cell growth, whereas another protein kinase C activator, phorbol myristate acetate (PMA), completely inhibited U937 cell growth. Both bryostatin 1 and PMA induced inhibition of cyclin-dependent kinase 2 (cdk2) activity. The first phase of cdk2 inhibition correlated with the transient induction of p21, a known inhibitor of cdk2. In contrast, the second phase of cdk2 inhibition correlated with the dephosphorylation of cdk2 on threonine-160, which must be phosphorylated for cdk2 activity. The level of growth inhibition induced by these two compounds correlated with the degree of cdk2 dephosphorylation as follows: bryostatin 1, 60%; PMA, 100%.

Original languageEnglish (US)
Pages (from-to)3716-3720
Number of pages5
JournalCancer Research
Volume55
Issue number17
StatePublished - 1995
Externally publishedYes

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Cyclin-Dependent Kinase 2
Cyclin-Dependent Kinases
Protein Kinase C
Growth
Tetradecanoylphorbol Acetate
U937 Cells
Threonine
bryostatin 1
Antineoplastic Agents

ASJC Scopus subject areas

  • Cancer Research
  • Oncology

Cite this

Inhibition of leukemic cell growth by the protein kinase C activator bryostatin 1 correlates with the dephosphorylation of cyclin-dependent kinase 21. / Asiedu, Clement; Biggs, Joseph; Kraft, Andrew; Kraft, Andrew S.

In: Cancer Research, Vol. 55, No. 17, 1995, p. 3716-3720.

Research output: Contribution to journalArticle

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