Secretion and binding of HMG1 protein to the external surface of the membrane are required for murine erythroleukemia cell differentiation

FEBS Lett. 1997 Jan 6;400(3):275-9. doi: 10.1016/s0014-5793(96)01402-0.

Abstract

We show here that murine erythroleukemia (MEL) cells, following induction with hexamethylene bisacetamide, accumulate high mobility group (HMG)1 protein onto the external surface of the cell in a membrane-associated form detectable by immunostaining with a specific anti-HMG1 protein antibody. This association is maximal at a time corresponding to cell commitment. At longer times, immunostainable cells are progressively reduced and become almost completely undetectable along with the appearance of hemoglobin molecules. Binding to MEL cells does not affect the native molecular structure of HMG1 protein. The type of functional correlation between HMG1 protein and MEL cell differentiation is suggested by the observation that if an anti-HMG1 protein antibody is added at the same time of the inducer almost complete inhibition of cell differentiation is observed, whereas if the antibody is added within the time period in which cells undergo through irreversible commitment, inhibition progressively disappears. A correlation between MEL cell commitment and the biological effect of HMG1 protein can thus be consistently suggested.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetamides / pharmacology
  • Animals
  • Antibodies, Monoclonal
  • Cell Differentiation*
  • Cell Membrane / metabolism*
  • Endoplasmic Reticulum / metabolism
  • Erythrocytes / cytology*
  • Erythrocytes / metabolism
  • Golgi Apparatus / metabolism
  • High Mobility Group Proteins / immunology
  • High Mobility Group Proteins / metabolism*
  • Leukemia, Erythroblastic, Acute
  • Mice
  • Tumor Cells, Cultured

Substances

  • Acetamides
  • Antibodies, Monoclonal
  • High Mobility Group Proteins
  • hexamethylene bisacetamide