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

FEBS Letters

Pontremoli, Sandro¹  Passalacqua, Mario¹  Patrone, Mauro¹  Sparatore, Bianca¹  Zicca, Antonio²  Melloni, Edon¹ 

[1] Institute of Biological Chemistry, University of Genoa, Viale Benedetto XV, 1-16132 Genoa, Italy;Institute of Human Anatomy, University of Genoa, Via De Toni, 14–16132 Genoa, Italy

关键词: HMG1 protein;    Murine erythroleukemia cell;    Cell differentiation;    HMG;    high mobility group;    MEL;    murine erythroleukemia;    HMBA;    hexamethylene bisacetamide;    PKC;    protein kinase C;   

DOI  :  10.1016/S0014-5793(96)01402-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown