Comparative effects of polymyxin B, phorbol ester and bryostatin on protein phosphorylation, protein kinase C translocation, phospholipid metabolism and differentiation of HL60 cells

Zoltan Kiss; Eva Deli; Peggy R. Girard; George Pettit; J. F. Kuo

doi:10.1016/0006-291X(87)90712-1

Comparative effects of polymyxin B, phorbol ester and bryostatin on protein phosphorylation, protein kinase C translocation, phospholipid metabolism and differentiation of HL60 cells

Zoltan Kiss, Eva Deli, Peggy R. Girard, George Pettit, J. F. Kuo

Research output: Contribution to journal › Article › peer-review

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Abstract

The effects of protein kinase C (PKC) inhibitor polymyxin B (PMB) and PKC activators 12-0-tetradecanoylphorbol-13-acetate (TPA) and bryostatin on intact HL60 cells were examined. It was found that each of the three agents exhibited similar effects on phosphorylation of certain endogenous proteins, PKC translocation from cytoplasm to plasma membrane and formation of CDP-choline. TPA, however, was the only agent that stimulated phosphatidylcholine formation. Differentiation of HL60 cells was potently induced by TPA; in comparison bryostatin was a relatively weaker inducer and PMB was without effect. The data indicated that the effects of the PKC inhibitor PMB on intact cells could not be predicted by its in vitro activity, and that certain TPA-dependent but PKC-independent reactions might be crucial in HL60 cell differentiation.

Original language	English (US)
Pages (from-to)	208-215
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	146
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(87)90712-1
State	Published - Jul 15 1987

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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Comparative effects of polymyxin B, phorbol ester and bryostatin on protein phosphorylation, protein kinase C translocation, phospholipid metabolism and differentiation of HL60 cells. / Kiss, Zoltan; Deli, Eva; Girard, Peggy R. et al.
In: Biochemical and Biophysical Research Communications, Vol. 146, No. 1, 15.07.1987, p. 208-215.

Research output: Contribution to journal › Article › peer-review

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title = "Comparative effects of polymyxin B, phorbol ester and bryostatin on protein phosphorylation, protein kinase C translocation, phospholipid metabolism and differentiation of HL60 cells",

abstract = "The effects of protein kinase C (PKC) inhibitor polymyxin B (PMB) and PKC activators 12-0-tetradecanoylphorbol-13-acetate (TPA) and bryostatin on intact HL60 cells were examined. It was found that each of the three agents exhibited similar effects on phosphorylation of certain endogenous proteins, PKC translocation from cytoplasm to plasma membrane and formation of CDP-choline. TPA, however, was the only agent that stimulated phosphatidylcholine formation. Differentiation of HL60 cells was potently induced by TPA; in comparison bryostatin was a relatively weaker inducer and PMB was without effect. The data indicated that the effects of the PKC inhibitor PMB on intact cells could not be predicted by its in vitro activity, and that certain TPA-dependent but PKC-independent reactions might be crucial in HL60 cell differentiation.",

author = "Zoltan Kiss and Eva Deli and Girard, {Peggy R.} and George Pettit and Kuo, {J. F.}",

note = "Funding Information: ACKNOWLEDGEMENTS: We thank Ms. Beverly Burson the manuscript. The present work was supported HL-15696 and NS-17608 (J. F. K.), and CA-16094 for her skillful preparation by USPHS Grants CA-36777, and NOl-CM97262 (G. R. P.).",

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AU - Pettit, George

AU - Kuo, J. F.

N1 - Funding Information: ACKNOWLEDGEMENTS: We thank Ms. Beverly Burson the manuscript. The present work was supported HL-15696 and NS-17608 (J. F. K.), and CA-16094 for her skillful preparation by USPHS Grants CA-36777, and NOl-CM97262 (G. R. P.).

PY - 1987/7/15

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N2 - The effects of protein kinase C (PKC) inhibitor polymyxin B (PMB) and PKC activators 12-0-tetradecanoylphorbol-13-acetate (TPA) and bryostatin on intact HL60 cells were examined. It was found that each of the three agents exhibited similar effects on phosphorylation of certain endogenous proteins, PKC translocation from cytoplasm to plasma membrane and formation of CDP-choline. TPA, however, was the only agent that stimulated phosphatidylcholine formation. Differentiation of HL60 cells was potently induced by TPA; in comparison bryostatin was a relatively weaker inducer and PMB was without effect. The data indicated that the effects of the PKC inhibitor PMB on intact cells could not be predicted by its in vitro activity, and that certain TPA-dependent but PKC-independent reactions might be crucial in HL60 cell differentiation.

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Comparative effects of polymyxin B, phorbol ester and bryostatin on protein phosphorylation, protein kinase C translocation, phospholipid metabolism and differentiation of HL60 cells

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