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

FEBS Lett. 1995 May 15;364(3):309-13. doi: 10.1016/0014-5793(95)00416-7.

Abstract

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 1 alpha, 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blotting, Western
  • Calcitriol / pharmacology
  • Cell Differentiation* / drug effects
  • Cell Division* / drug effects
  • Granulocyte Colony-Stimulating Factor / pharmacology
  • Humans
  • Leukemia, Promyelocytic, Acute
  • Microtubule Proteins*
  • Monocytes / cytology*
  • Neutrophils / cytology*
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Stathmin
  • Tetradecanoylphorbol Acetate / pharmacology
  • Tumor Cells, Cultured

Substances

  • Microtubule Proteins
  • Phosphoproteins
  • STMN1 protein, human
  • Stathmin
  • Granulocyte Colony-Stimulating Factor
  • Calcitriol
  • Tetradecanoylphorbol Acetate