K. Ando et al., Naturally occurring anti-band 3 antibody binds to apoptotic human T-lymphoid cell line Jurkat through sialylated poly-N-acetyllactosaminyl saccharidechains on the cell surface, BIOC BIOP R, 275(2), 2000, pp. 412-417
Biochemistry & Biophysics
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Human T-lymphoid cell line Jurkat was treated with actinomycin D (ActD) and
cycloheximide (CHX). The induction of apoptosis was confirmed by the chrom
atin condensation and DNA ladder fragmentation. Anti-band 3 IgG, purified f
rom normal human plasma, bound to the ActD- or CHX-treated cells, and the b
inding was correlated to the degree of apoptosis. Antioxidants, N-acetylcys
teine, 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; bindi
ng sites on the apoptotic cell surface is caused by nonoxidative mechanism.
When Jurkat cells were treated with endo-beta-galactosidase to cleave sial
ylated poly-N-acetyllactosaminyl saccharide chains from the cell surface be
fore induction of apoptosis, the binding of anti-band 3 IgG was abolished.
The results indicate that sialylated poly-N-acetyllactosaminyl saccharide c
hains on the cell surface are requisite for the binding of anti-band 3 IgG
to apoptotic cells. (C) 2000 Academic Press.