RRC ID 72994
Author Ando K, Hagiwara T, Beppu M, Kikugawa K.
Title Naturally occurring anti-band 3 antibody binds to apoptotic human T-lymphoid cell line Jurkat through sialylated poly-N-acetyllactosaminyl saccharide chains on the cell surface.
Journal Biochem Biophys Res Commun
Abstract Human T-lymphoid cell line Jurkat was treated with actinomycin D (ActD) and cycloheximide (CHX). The induction of apoptosis was confirmed by the chromatin condensation and DNA ladder fragmentation. Anti-band 3 IgG, purified from normal human plasma, bound to the ActD- or CHX-treated cells, and the binding was correlated to the degree of apoptosis. Antioxidants, N-acetylcysteine, pilloridine dithiocarbamate, and trolox, inhibited neither induction of DNA fragmentation of ActD-treated cells nor anti-band 3 IgG binding to ActD-treated cells, indicating that formation of the anti-band 3 IgG binding sites on the apoptotic cell surface is caused by nonoxidative mechanism. When Jurkat cells were treated with endo-beta-galactosidase to cleave sialylated poly-N-acetyllactosaminyl saccharide chains from the cell surface before induction of apoptosis, the binding of anti-band 3 IgG was abolished. The results indicate that sialylated poly-N-acetyllactosaminyl saccharide chains on the cell surface are requisite for the binding of anti-band 3 IgG to apoptotic cells.
Volume 275(2)
Pages 412-7
Published 2000-8-28
DOI 10.1006/bbrc.2000.3322
PII S0006-291X(00)93322-9
PMID 10964679
MeSH Amino Sugars / chemistry Amino Sugars / immunology* Anion Exchange Protein 1, Erythrocyte / immunology* Antioxidants / pharmacology Apoptosis* Binding Sites, Antibody Cell Membrane / chemistry Cell Membrane / drug effects Cycloheximide / pharmacology Dactinomycin / pharmacology Humans Jurkat Cells Oxidative Stress
IF 2.985
Human and Animal Cells Jurkat(RCB0806)