S1.26 Sequential activation of glycosyltransferases during B cell differentiation

Taga, Samir; Tétaud, Cécile; Mangeney, Marianne; Tursz, Thomas; Wiels, Joëlle

doi:10.1007/bf01209827

Cited by 7 publications

(16 citation statements)

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“…Gb3/CD77 seems to be unusual because it can mediate various apoptotic signals in both normal cells and malignant tumor cells, although it does not contain the cytoplasmic domain (18,34). The observed rapid death of CD77 ϩ germinal center B cells in vitro suggests that endogenous ligand molecules interact with Gb3/CD77 to bring about the physiologic selection of immature B cells (12,35).…”

Section: Discussionmentioning

confidence: 99%

“…The observed rapid death of CD77 ϩ germinal center B cells in vitro suggests that endogenous ligand molecules interact with Gb3/CD77 to bring about the physiologic selection of immature B cells (12,35). Furthermore, the capability of the B subunit of VT to induce apoptosis of Gb3/CD77 ϩ cells (18) strongly encourages the investigation of Gb3/CD77-associating cytoplasmic molecules (34). Investigations of these ligands and signal transducers relevant to Gb3/CD77 might contribute in further understanding of the B cell selection and of the pathogenesis of hemolytic uremic syndrome caused by E. coli O157 infection.…”

Section: Discussionmentioning

confidence: 99%

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Molecular Cloning of Globotriaosylceramide/CD77 Synthase, a Glycosyltransferase That Initiates the Synthesis of Globo Series Glycosphingolipids

Kojima¹,

Fukumoto²,

Okajima³

et al. 2000

Journal of Biological Chemistry

129

120

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The expression cloning of a cDNA for globotriaosylceramide (Gb3)/CD77 synthase (␣1,4-galactosyltransferase) was achieved using an anti-Gb3 antibody and mouse L cells as a recipient cell line for the transfection. The isolated cDNA clone designated pVTR1 predicted a type II membrane protein with 19 amino acids of cytoplasmic domain, 26 amino acids of transmembrane region, and a catalytic domain with 308 amino acids. Introduction of the cDNA clone into L cells resulted in the neosynthesis of Gb3/CD77, and the extracts of the transfectant cells showed ␣1,4-galactosyltransferase activity only on lactosylceramide and galactosylceramide. In Northern blotting, a 2.3-kilobase mRNA was strongly expressed in heart, kidney, spleen, and placenta and weakly in colon, small intestine, and brain. Transfection of the cDNA into L cells resulted in the constitution of sensitivity to the apoptosis with Shiga-like toxins (verotoxins). Since Gb3/CD77 synthase initiates the synthesis of globo series glycolipids, the isolation of this cDNA will make possible further investigations into the function of its important series of glycolipids.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Molecular Cloning of Globotriaosylceramide/CD77 Synthase, a Glycosyltransferase That Initiates the Synthesis of Globo Series Glycosphingolipids

Kojima¹,

Fukumoto²,

Okajima³

et al. 2000

Journal of Biological Chemistry

129

120

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“…We previously reported that the ligation of Gb3/CD77 by specific monoclonal antibodies (mAb) induces apoptosis in Burkitt's lymphoma (BL) cells, the tumoral counterparts of Gb3/CD77(ϩ) germinal center B lymphocytes. We have also demonstrated that this apoptosis involves a rapid, sustained increase in intracellular Ca 2ϩ concentration, a rapid, transient increase in cAMP levels, protein kinase A activation, and, finally, ceramide accumulation (5,6).…”

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confidence: 99%

“…Recent reports have shed light on both toxin-and anti-Gb3/CD77 mAb-induced apoptotic pathways (6,18,19), but various questions remain unresolved: Is ligand binding to Gb3/CD77 sufficient to induce apoptosis? Do ligands trigger a single intracellular mechanism?…”

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confidence: 99%

Two Distinct Gb3/CD77 Signaling Pathways Leading to Apoptosis Are Triggered by Anti-Gb3/CD77 mAb and Verotoxin-1

Tétaud

Falguières

Carlier

et al. 2003

Journal of Biological Chemistry

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Globotriasosylceramide (Gb3), a neutral glycosphingolipid, is the B-cell differentiation antigen CD77 and acts as the receptor for most Shiga toxins, including verotoxin-1 (VT-1). We have shown that both anti-Gb3/ CD77 mAb and VT-1 induce apoptosis in Burkitt's lymphoma cells. We compared the apoptotic pathways induced by these two molecules by selecting cell lines sensitive to only one of these inducers or to both. In all these cell lines (including the apoptosis-resistant line), VT-1 was transported to the endoplasmic reticulum and inhibited protein synthesis similarly, suggesting that VT-1-induced apoptosis is dissociated from these processes. VT-1 triggered a caspase-and mitochondria-dependent pathway (rapid activation of caspases 8 and 3 associated with a loss of mitochondrial membrane potential (⌬ m ) and the release of cytochrome c from mitochondria). In contrast, the anti-Gb3/CD77 mAb-induced pathway was caspase-independent and only involved partial depolarization of mitochondria. Antioxidant compounds had only marginal effects on VT-1-induced apoptosis but strongly protected cells from antiGb3/CD77 mAb-induced apoptosis. VT-1-and anti-Gb3/ CD77 mAb-treated cells displayed very different features on electron microscopy. These results clearly indicate that the binding of different ligands to Gb3/ CD77 triggers completely different apoptotic pathways.

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“…12,13) Some researchers have also suggested that the apoptosis involves a rapid, sustained increase in intracellular Ca 2ϩ concentration, a transient increase in cAMP levels, protein kinase A activation and ceramide accumulation. 14,15) Furthermore, it was reported that the up-regulation of Stx-receptor increases high renal cell sensitivity to the cytotoxic effects of Stx. 16) Stx binds to cell-surface glycosphingolipids, terminating in galactose-a1,4-galactose, whereupon the complex is internalized, with resultant inhibition of peptide elongation.…”

mentioning

confidence: 99%

Curcumin Decreases Binding of Shiga-Like Toxin-1B on Human Intestinal Epithelial Cell Line HT29 Stimulated with TNF-.ALPHA. and IL-1.BETA.: Suppression of p38, JNK and NF-.KAPPA.B p65 as Potential Targets

Moon

Jin

Lee

et al. 2006

Biological & Pharmaceutical Bulletin

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(Stx)-producing Escherichia coli (STEC) is an important cause of a range of illnesses from self-limiting watery diarrhea and hemorrhagic colitis to severe conditions such as hemolytic uremic syndrome (HUS) and thrombotic thrombocytopoenic purpura. 1,2) Recent research has partially documented how and where Stx has pathogenic effects in humans. Because STEC is a noninvasive intestinal pathogen, it has been shown that Stx in host intestinal lumen must cross the intestinal epithelial cells (IECs) to cause disease in distal organs. [3][4][5][6] The extent to which Stx is absorbed systemically may influence who is at risk for serious complications of the infection. Because the IECs are the first line in contact with Stx in a host, the interaction of Stx with epithelium may be a pivotal role in HUS 3) through induction of apoptosis in vivo and in vitro studies.7-10) Apoptosis of IECs could destroy the barriers in host lumen and permit Stx to enter the bloodstream and attack the central nervous and/or renal systems. 5,11) In many cells, Stx-induced apoptosis has been induced by cleavage of poly(ADP-ribose) polymerase, release of cytochrome C and capase-3 activities with mitogen-activated protein kinases (MAPKs).12,13) Some researchers have also suggested that the apoptosis involves a rapid, sustained increase in intracellular Ca 2ϩ concentration, a transient increase in cAMP levels, protein kinase A activation and ceramide accumulation.14,15) Furthermore, it was reported that the up-regulation of Stx-receptor increases high renal cell sensitivity to the cytotoxic effects of Stx. 16)Stx binds to cell-surface glycosphingolipids, terminating in galactose-a1,4-galactose, whereupon the complex is internalized, with resultant inhibition of peptide elongation. 2,17)The major glycosphingolipid that binds Stx-1 is galactosea1,4-galactose-b1,4-glucose ceramide (globotriaosylceramide: Gb3). These toxins are structurally similar heterodimers composed of one enzymatically active A subunit 18) that irreversibly inhibits protein synthesis by means of its Nglycosidase activity on ribosomal subunit and B subunit pentamers that binds Gb3. 19,20) TNF-a or IL-1b have been also known to be important cytokines to induce Gb3 to sensitivity of Stx.14-16) Therefore, we assume that down-regulation of Gb3 synthase decreases the sensitivity to the cytotoxicity of Stx.Curcumin has been shown to exhibit anti-inflammatory and anti-mutagenic activities, 21,22) the inhibition of chemical carcinogen-induced tumor formation in mice 23,24) and the anti-proliferation of various cultured tumor cells.25,26) Our previous study has also shown that curcumin significantly inhibited LPS-induced immunostimulation of murine dendritic cells through inhibition of MAPKs and NF-kB.27) These potent chemopreventive activities of curcumin may be attributed to the inhibition of certain signal transduction pathways critical to tumor cell growth, such as AP-1, NF-kB, MAPKs and protein kinase C. [28][29][30] However Gb3 expression by curcumin is not understood at all in IECs...

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S1.26 Sequential activation of glycosyltransferases during B cell differentiation

Cited by 7 publications

References 1 publication

Molecular Cloning of Globotriaosylceramide/CD77 Synthase, a Glycosyltransferase That Initiates the Synthesis of Globo Series Glycosphingolipids

Molecular Cloning of Globotriaosylceramide/CD77 Synthase, a Glycosyltransferase That Initiates the Synthesis of Globo Series Glycosphingolipids

Two Distinct Gb3/CD77 Signaling Pathways Leading to Apoptosis Are Triggered by Anti-Gb3/CD77 mAb and Verotoxin-1

Curcumin Decreases Binding of Shiga-Like Toxin-1B on Human Intestinal Epithelial Cell Line HT29 Stimulated with TNF-.ALPHA. and IL-1.BETA.: Suppression of p38, JNK and NF-.KAPPA.B p65 as Potential Targets

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