Down‐regulation by retinoic acid of the catalytic subunit of protein phosphatase type 2A during granulocytic differentiation of HL‐60 cells

FEBS Letters

Monta, Koichi³  Toyoda, Hideki³  Nagao, Minako¹  Tawara, Isao³  Kuno, Takayoshi²  Omay, Serdar B.³  Shirakawa, Shigeru³  Kobayashi, Kazuhiko³  Nishikawa, Masakatsu³  Shima, Hiroshi¹  Tanaka, Chikako² 

[1] Caranagenesis Division, National Cancer Center Research Institute, Tokyo, Japan;Department of Pharmacology, Kobe University School of Medicine, Kobe, Japan;The Second Department of Internal Medicine, Mie University School of Medicine, Tsu, Japan

关键词: HL-60 cell;    Retinoic acid;    Differentiation;    Phosphatase;   

DOI  :  10.1016/0014-5793(93)80113-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Activity of protein phosphatase measured in the absence of divalent cations was decreased by 50% during all-trans retinoic acid (ATRA)-induced HL-60 cell differentiation into the granulocytic phenotype. Treatment of HL-60 cells with ATRA led to a dramatic decrease in the amount of protein phosphatase type 2A (PP2A) protein, whereas that of protein phosphatase type l (PP1) protein was relatively constant, as detected by immunoblotting with antibodies specific to PP1 and PP2A. The decreased phosphatase activity may be mainly due to a decrease in the expression of the PP2A protein. The mRNA level ofPP2Aβ was markedly decreased within 5 h after addition of ATRA, but there was only a slight increase in the mRNA level of PP2Aα. Selective down-regulation of PP2Aβ mRNA clearly preceded the cell differentiation induced by ATRA treatment. Thus, PP2A is down-regulated during ATRA-induced differentiation of HL-60 cells into granulocytes.

【 授权许可】

Unknown