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

Citation
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
Citations number
43
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
ISSN journal
0006-291X → ACNP
Volume
275
Issue
2
Year of publication
2000
Pages
412 - 417
Database
ISI
SICI code
0006-291X(20000828)275:2<412:NOA3AB>2.0.ZU;2-4
Abstract
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.