Bryostatin, a non-phorbol macrocyclic lactone, activates intact human polymorphonuclear leukocytes and binds to the phorbol ester receptor

R. L. Berkow, Andrew Kraft

Research output: Contribution to journalArticle

152 Citations (Scopus)

Abstract

Bryostatin, is an antineoplastic agent with activity in both solid and liquid tumors. When added to tissue culture cells this agent shares a number of similarities with phorbol esters. In this report, we evaluate Bryostatin's effect on human polymorphonuclear leukocytes. Bryostatin stimulates the release of specific granules with a parallel dose response curve to phorbol 12-myristate 13-acetate (PMA), but induces release of superoxide at a significantly slower rate than PMA. Competition experiments demonstrate that Bryostatin, although sharing little structural similarity with PMA, can bind to the PMA receptor. In addition, both Bryostatin and PMA stimulate the phosphorylation of almost identical proteins in intact PMNs. These experiments suggest that Bryostatin may activate PMNs by binding to the PMA receptor, which is currently felt to be the calcium, phospholipid-dependent protein kinase.

Original languageEnglish (US)
Pages (from-to)1109-1116
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume131
Issue number3
DOIs
StatePublished - Sep 30 1985
Externally publishedYes

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Bryostatins
Lactones
Acetates
Neutrophils
Tissue culture
Phosphorylation
Phorbol Esters
Superoxides
Antineoplastic Agents
Protein Kinase C
phorbol ester receptor
phorbol-12-myristate
Tumors
Cell Culture Techniques
Experiments
Liquids

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

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abstract = "Bryostatin, is an antineoplastic agent with activity in both solid and liquid tumors. When added to tissue culture cells this agent shares a number of similarities with phorbol esters. In this report, we evaluate Bryostatin's effect on human polymorphonuclear leukocytes. Bryostatin stimulates the release of specific granules with a parallel dose response curve to phorbol 12-myristate 13-acetate (PMA), but induces release of superoxide at a significantly slower rate than PMA. Competition experiments demonstrate that Bryostatin, although sharing little structural similarity with PMA, can bind to the PMA receptor. In addition, both Bryostatin and PMA stimulate the phosphorylation of almost identical proteins in intact PMNs. These experiments suggest that Bryostatin may activate PMNs by binding to the PMA receptor, which is currently felt to be the calcium, phospholipid-dependent protein kinase.",
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