Elsevier

FEBS Letters

Volume 263, Issue 1, 9 April 1990, Pages 31-34
FEBS Letters

Research letters
Protein kinase C during differentiation of human promyelocytic leukemia cell line, HL-60

https://doi.org/10.1016/0014-5793(90)80698-IGet rights and content
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Abstract

Protein kinase C (PKC) from human promyelocytic leukemia HL-60 cells can be resolved into three fractions (peak a, b and c) by hydroxyapatite column chromatography. Peak a and c enzymes are indistinguishable from the brain type II PKC having β (βI and βII)-sequence and type III having α-sequence, respectively. Peak b enzyme is a previously unidentified PKC subspecies that has enzymological properties subtly different from type I (having γ-sequence), type II and type III PKC. Upon treatment of HL-60 cells with 1 μM retinoic add, this peak b enzyme is decreased dramatically within 24 h, whilst peak a enzyme (β-PKC) is increased, and peak c (α-PKC) enzyme is slightly decreased within 48 h. The result implies that the PKC subspecies in HL-60 cells have distinct functions during cell differentiation.

Keywords

Protein kinase C
Retinoic acid
Differentiation
(HL-60 cells)

Abbreviations

PKC, protein kinase C
RA, retinoic acid
DMSO, dimethyl sulfoxide
TPA, 12-O-tetradecanoylphorbol-13-acetate
PS, phosphatidylserine
DO diolein
EGTA [ethylenebis(oxyethylenenitrilo)]tetraacetic acid

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