Abstract
Bistratene A (BisA) induced growth arrest in G2/M in HL60 cells. In addition, BisA-treated cells (50 nM for 48 h) became adherent and expressed the adhesion molecule CD11c, but did not express the monocyte enzyme alpha-napthyl acetate esterase or phagocytose complement coated yeasts. BisA activated protein kinase C (PKC)-delta and induced translocation of PKC-delta to the nucleus. This suggests that activation of PKC-delta can induce growth arrest and cell adhesion, but is insufficient to mediate full differentiation of HL60 cells. BisA has potential as a new probe for determining the function of PKC isoenzymes, specifically PKC-delta.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetamides*
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Cell Adhesion / drug effects
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Cell Compartmentation / drug effects
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Cell Differentiation / drug effects
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Cell Division / drug effects
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Enzyme Activation / drug effects
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Ethers, Cyclic / pharmacology*
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Fluorescent Antibody Technique, Indirect
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Growth Inhibitors / pharmacology*
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HL-60 Cells
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Humans
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Isoenzymes / metabolism*
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Phosphorylation
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Protein Kinase C / metabolism*
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Protein Kinase C-delta
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Pyrans*
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Spiro Compounds
Substances
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Acetamides
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Ethers, Cyclic
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Growth Inhibitors
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Isoenzymes
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Pyrans
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Spiro Compounds
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bistratene A
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PRKCD protein, human
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Protein Kinase C
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Protein Kinase C-delta