Down‐regulation but not phosphorylation of stathmin is associated with induction of HL60 cell growth arrest and differentiation by physiological agents

FEBS Letters

Guest, Simon S.²  Jones, Neil A.²  Williams, Ann¹  Brown, Geoffrey²  Johnson, W.Eustace B.²  Rowlands, David C.¹ 

[1] Department of Pathology, University of Birmingham Medical School, Edgbaston, Birmingham B15 2TT, UK;Department of Immunology, University of Birmingham Medical School, Edgbaston, Birmingham B15 2TT, UK

关键词: Stathmin;    Cell proliferation;    Growth arrest;    Protein phosphorylation;    PMA;    phorbol 12-myristate 13-acetate;    ATRA;    all-trans retinoic acid;    hrG-CSF;    recombinant human granulocyte colony stimulating factor;    vitD3;    1α;    25-dihydroxyvitamin D3;   

DOI  :  10.1016/0014-5793(95)00416-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Stathmin is a cytosolic phosphoprotein that has an important but, as yet, undefined role in cell proliferation and differentiation. Induction of growth arrest and differentiation of HL60 cells to monocytes by phorbol 12-myristate 13-acetate is associated with rapid phosphorylation of the protein. Stathmin phosphorylation was not seen when HL60 cells were induced to differentiate to monocytes, by 1α,25-dihydroxyvitamin D3, and to neutrophils, by all-trans retinoic acid and granulocyte colony stimulating factor. In all the above instances, stathmin expression was down-regulated. Thus, increased stathmin phosphorylation is not required for cell growth arrest or differentiation or down-regulation of stathmin expression.

【 授权许可】

Unknown