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Down‐regulation by retinoic acid of the catalytic subunit of protein phosphatase type 2A during granulocytic differentiation of HL‐60 cells
Author(s) -
Tawara Isao,
Nishikawa Masakatsu,
Monta Koichi,
Kobayashi Kazuhiko,
Toyoda Hideki,
Omay Serdar B.,
Shima Hiroshi,
Nagao Minako,
Kuno Takayoshi,
Tanaka Chikako,
Shirakawa Shigeru
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80113-9
Subject(s) - protein phosphatase 2 , retinoic acid , phosphatase , protein subunit , acid phosphatase , chemistry , microbiology and biotechnology , messenger rna , cellular differentiation , biology , biochemistry , enzyme , gene
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.