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Up‐regulation of protein serine/threonine phosphatase type 2C during 1α,25‐dihydroxyvitamin D 3 ‐induced monocytic differentiation of leukemic HL‐60 cells
Author(s) -
Nishikawa Masakatsu,
Omay Serdar B.,
Nakai Keiji,
Kihira Hisakazu,
Kobayashi Takayasu,
Tamura Shinri,
Shiku Hiroshi
Publication year - 1995
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(95)01209-w
Subject(s) - serine , threonine , chemistry , phosphatase , protein phosphatase 2 , biochemistry , phosphorylation , microbiology and biotechnology , biology
Treatment with 20 nM 1α,25‐dihydroxyvitamin D 3 (1,25(OH) 2 D 3 ) caused a progressive increase in the activity of Mg 2+ ‐dependent protein serine/threonine phosphatase type 2C (PP2C) in subcellular fractions of HL‐60 cells, whereas PP2C activity was relatively constant throughout all‐ trans retinoic acid‐induced (1 μM) granulocytic differentiation. The increase in PP2C activity appeared to parallel the 1,25(OH) 2 D 3 ‐induced phenotypic and functional changes in HL‐60 cells. Immunoblot and Northern blot analysis indicated that the increase in PP2C activity corresponded to the increased expression of PP2C protein, which was preceded by an increase in the level of mRNA for PP2Cβ. No mRNA for PP2Cα was detected in resting or 1,25(OH) 2 D 3 ‐stimulated HL‐60 cells. These results suggest that the increased expression of PP2C is related with the 1,25(OH) 2 D 3 ‐induced monocytic differentiation of HL‐60 cells.