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Related Experiment Videos

PADGEM protein in human erythroleukemia cells.

E Yeo1, B C Furie, B Furie

  • 1Division of Hematology-Oncology, New England Medical Center, Boston, MA 02111.

Blood
|February 15, 1989
PubMed
Summary

Platelet activation marker PADGEM (platelet alpha granule membrane glycoprotein) is expressed on human erythroleukemia (HEL) cells. Dimethyl sulfoxide (DMSO) significantly increases PADGEM expression on HEL cells, aiding functional studies.

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Area of Science:

  • Cell biology
  • Hematology
  • Molecular biology

Background:

  • PADGEM (platelet alpha granule membrane glycoprotein) is a 140,000 MW protein translocated to the plasma membrane during platelet activation.
  • Human erythroleukemia (HEL) cells share characteristics with activated platelets, including granule proteins and specific glycoproteins.

Purpose of the Study:

  • To investigate the expression and regulation of PADGEM protein in human erythroleukemia (HEL) cells.
  • To determine if HEL cells can serve as a model for studying PADGEM function.

Main Methods:

  • Flow cytometry to analyze surface PADGEM expression.
  • Radioimmunoassay to quantify total cellular PADGEM.
  • Monoclonal antibody binding assays to assess PADGEM interaction.

Main Results:

  • HEL cells express a protein identical in molecular weight to PADGEM and bind anti-PADGEM antibodies.
  • Dimethyl sulfoxide (DMSO) treatment significantly increased the number of PADGEM-expressing HEL cells and total cellular content (5.3-fold).
  • Monoclonal antibody KC4 showed specific, saturable binding to HEL cells, with increased binding sites after DMSO induction.

Conclusions:

  • HEL cells express PADGEM protein, and its surface expression can be upregulated by DMSO.
  • HEL cells provide a valuable model system for further elucidation of PADGEM protein function in the absence of platelet agonists or cytokines.

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