Recognition by TNF-α of the GPI-anchor glycan induces apoptosis of U937 cells

被引：6

作者：

Fukushima, K ^{[1
]}

Ishiyama, C ^{[1
]}

Yamashita, K ^{[1
]}

机构：

[1] Saskai Inst, Dept Biochem, Chiyoda Ku, Tokyo 1010062, Japan

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2004年 / 426卷 / 02期

关键词：

GPI anchor; beta-N-acetylglucosaminyl phosphate diester; apoptosis; TNF-alpha;

D O I：

10.1016/j.abb.2004.02.028

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Tumor necrosis factor-alpha (TNF-alpha) binds to TNF-alpha receptors (TNFR) to produce a hexameric (TNF-alpha)(3)-(TNFR)(3) structure that stimulates apoptosis. We found by using ELISA that TNF-a binds to the glycosylphosphatidylinositol (GPI) anchor glycans of carcinoembryonic antigen, human placental alkaline phosphatase (hAP), and Tamm-Horsfall glycoprotein. These binding abilities were inhibited by 10(-6) M mannose-6-phosphate. Treatment of hAP with mild acid and phosphatase, which releases the N-acetyl-glucosamine (GlcNAc) beta1 --> phosphate 6 residue from the GPI-anchor glycan of hAP, abrogated the binding of TNF-alpha to hAP. Thus, TNF-alpha binds to the GlcNAcbeta1 phosphate --> 6Man residue in GPI-anchor glycans. To investigate whether the carbohydrate-binding ability of TNF-alpha is related to its physiological functions, human lymphoma U937 cells were used. TNF-alpha stimulates U937 cell apoptosis in a dose-dependent manner and the presence of mannose-6-phosphate inhibited this. TNF-alpha-dependent tyrosine phosphorylation of several proteins in U937 cells was also diminished by mannose-6-phosphate. Phosphatidylinositol-specific phospholipase C-pretreatment also inhibited this tyrosine phosphorylation. These data suggest that TNF-alpha stimulates U937 cell apoptosis by forming a high-affinity nanomeric (TNF-alpha)(3)-(TNFR)(3)-(GPI-anchored glycan)(3) complex. The GPI-anchored glycoprotein involved remains to be identified. (C) 2004 Elsevier Inc. All rights reserved.

引用

页码：298 / 305

页数：8

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