title: Altered expression of glycoproteins on the cell surface of Jurkat cells during etoposide-induced apoptosis: shedding and intracellular translocation of glycoproteins.
abstract: BACKGROUND
  The glycoproteins on the cell surface are altered during apoptosis and play an important role in phagocytic clearance of apoptotic cells.
  
  
  METHODS
  We classified Jurkat cells treated with etoposide as viable and early apoptotic cells, late apoptotic cells or secondary necrotic cells based on propidium iodide staining and scattered grams and estimated the expression levels of glycoproteins on the cell surface.
  
  
  RESULTS
  The cell surface expression levels of intercellular adhesion molecules (ICAM)-2 and -3 on the apoptotic cells were markedly lower, while those of calnexin, calreticulin, and lysosome-associated membrane proteins (LAMP)-1 and -2 were significantly higher compared to non-apoptotic cells. These decreases in ICAM-2 and -3 on the apoptotic cell surface were reduced in the presence of metalloproteinase inhibitors and caspase inhibitors, respectively. Confocal microscopic analysis revealed that calnexin and calreticulin were assembled around fragmented nuclei of blebbed apoptotic cells.
  
  
  CONCLUSIONS
  These results suggest that alteration of glycoproteins on the cell surface during apoptosis is associated with shedding and intracellular translocation of glycoproteins.
authors.affiliation: Department of Clinical Chemistry, School of Pharmaceutical Sciences, Toho University, 2-2-1 Miyama, Funabashi, Chiba 247-8510, Japan.
authors.forename: Hirotaka
authors.initials: H
authors.lastname: Sato
authors.forename: Yutaro
authors.initials: Y
authors.lastname: Azuma
authors.forename: Koji
authors.initials: K
authors.lastname: Higai
authors.forename: Kojiro
authors.initials: K
authors.lastname: Matsumoto
mesh_terms: D015703:Antigens, CD / Q000378:metabolism; D000972:Antineoplastic Agents, Phytogenic / Q000494:pharmacology; D017209:Apoptosis / Q000187:drug effects*; D015153:Blotting, Western; D037281:Calnexin / Q000378:metabolism; D037282:Calreticulin / Q000378:metabolism; D015815:Cell Adhesion Molecules / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D004151:Dipeptides / Q000494:pharmacology; D005047:Etoposide / Q000494:pharmacology*; D005434:Flow Cytometry; D006023:Glycoproteins / Q000378:metabolism*; D006801:Humans; D042541:Intracellular Space / Q000187:drug effects / Q000378:metabolism; D019169:Jurkat Cells; D052119:Lysosomal-Associated Membrane Protein 2; D051907:Lysosomal Membrane Proteins / Q000378:metabolism; D018613:Microscopy, Confocal; D009842:Oligopeptides / Q000494:pharmacology; D011480:Protease Inhibitors / Q000494:pharmacology; D021381:Protein Transport / Q000187:drug effects; D052118:Lysosomal-Associated Membrane Protein 1
chemical_list: D015703:Antigens, CD; D000972:Antineoplastic Agents, Phytogenic; D037281:Calnexin; D037282:Calreticulin; D015815:Cell Adhesion Molecules; D004151:Dipeptides; D005047:Etoposide; D006023:Glycoproteins; D052119:Lysosomal-Associated Membrane Protein 2; D051907:Lysosomal Membrane Proteins; D009842:Oligopeptides; D011480:Protease Inhibitors; C065289:ICAM2 protein, human; C483616:ICAM3 protein, human; C489116:LAMP1 protein, human; D052118:Lysosomal-Associated Membrane Protein 1; C497811:LAMP2 protein, human; C078131:N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide; C099158:acetyl-aspartyl-glutamyl-valyl-aspartal