GDP-mannose-4,6-dehydratase (GMDS) Deficiency Renders Colon Cancer Cells Resistant to Tumor Necrosis Factor-related Apoptosis-inducing Ligand (TRAIL) Receptor- and CD95-mediated Apoptosis by Inhibiting Complex II Formation

Moriwaki, Kazuo; Shinzaki, Shinichiro; Miyoshi, Eiji

doi:10.1074/jbc.m111.262741

Cited by 43 publications

(35 citation statements)

References 38 publications

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“…A role for fucosylation in TRAIL‐induced apoptosis of colon adenocarcinomas has been previously implicated . Wagner et al .…”

Section: Resultsmentioning

confidence: 99%

“…A role for fucosylation in TRAIL-induced apoptosis of colon adenocarcinomas has been previously implicated [24,35,36,43]. Wagner et al tested a panel of 36 colorectal adenocarcinoma cell lines and found that the sensitivity to TRAIL correlated with increased mRNA levels of the O-glycosylation initiating enzyme GALNT3, as well as the O-glycan processing fucosyltransferase enzymes FUT3 and FUT6 [24].…”

Section: Inhibition Of O-glycosylation Leads To Loss Of Fucosylation mentioning

confidence: 99%

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Death receptor 5 is activated by fucosylation in colon cancer cells

et al. 2019

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The remarkable pro‐apoptotic properties of tumour necrosis factor (TNF)‐related apoptosis‐inducing ligand (TRAIL) have led to considerable interest in this protein as a potential anticancer therapeutic. However, TRAIL is largely ineffective in inducing apoptosis in certain cancer cells, and the mechanisms underlying this selectivity are unknown. In colon adenocarcinomas, posttranslational modifications including O‐ and N‐ glycosylation of death receptors were found to correlate with TRAIL‐induced apoptosis. Additionally, mRNA levels of fucosyltransferase 3 (FUT3) and 6 (FUT6) were found to be high in the TRAIL‐sensitive colon adenocarcinoma cell line COLO 205. In this study, we use agonistic receptor‐specific TRAIL variants to dissect the contribution of FUT3 and FUT6‐mediated fucosylation to TRAIL‐induced apoptosis via its two death receptors, DR4 and DR5. Triggering of apoptosis by TRAIL revealed that the low FUT3/6‐expressing cells DLD‐1 and HCT 116 are insensitive to DR5 but not to DR4‐mediated apoptosis. By contrast, efficient apoptosis is mediated via both receptors in high FUT3/6‐expressing COLO 205 cells. The reconstitution of FUT3/6 expression in DR5‐resistant cells completely restored TRAIL sensitivity via this receptor, while only marginally enhancing apoptosis via DR4 at lower TRAIL concentrations. Interestingly, we observed that induction of the salvage pathway by external administration of l‐fucose restores DR5‐mediated apoptosis in both DLD‐1 and HCT 116 cells. Finally, we show that fucosylation influences the ligand‐independent receptor association that leads to increased death inducing signalling complex (DISC) formation and caspase‐8 activation. Taken together, these results provide evidence for the differential impact of fucosylation on signalling via DR4 or DR5. These findings provide novel opportunities to enhance TRAIL sensitivity in colon adenocarcinoma cells that are highly resistant to DR5‐mediated apoptosis.

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“…A role for fucosylation in TRAIL‐induced apoptosis of colon adenocarcinomas has been previously implicated . Wagner et al .…”

Section: Resultsmentioning

confidence: 99%

Section: Inhibition Of O-glycosylation Leads To Loss Of Fucosylation mentioning

confidence: 99%

Death receptor 5 is activated by fucosylation in colon cancer cells

et al. 2019

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“…It has been reported that FUT1/FUT4-knockdown by siRNA significantly diminishes cell proliferation and tumour growth both in vitro and in vivo [10]. Nevertheless, a deficiency in GDPmannose-4,6-dehydratase, resulting in a loss of fucosylation, has been shown to cause colon cancer cell metastasis by escaping from tumour immune surveillance [44,45]. Nevertheless, a deficiency in GDPmannose-4,6-dehydratase, resulting in a loss of fucosylation, has been shown to cause colon cancer cell metastasis by escaping from tumour immune surveillance [44,45].…”

Section: Discussionmentioning

confidence: 99%

Calreticulin activates β1 integrin via fucosylation by fucosyltransferase 1 in J82 human bladder cancer cells

Chen

Chu

et al. 2014

Biochemical Journal

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Fucosylation regulates various pathological events in cells. We reported that different levels of CRT (calreticulin) affect the cell adhesion and metastasis of bladder cancer. However, the precise mechanism of tumour metastasis regulated by CRT remains unclear. Using a DNA array, we identified FUT1 (fucosyltransferase 1) as a gene regulated by CRT expression levels. CRT regulated cell adhesion through α1,2-linked fucosylation of β1 integrin and this modification was catalysed by FUT1. To clarify the roles for FUT1 in bladder cancer, we transfected the human FUT1 gene into CRT-RNAi stable cell lines. FUT1 overexpression in CRT-RNAi cells resulted in increased levels of β1 integrin fucosylation and rescued cell adhesion to type-I collagen. Treatment with UEA-1 (Ulex europaeus agglutinin-1), a lectin that recognizes FUT1-modified glycosylation structures, did not affect cell adhesion. In contrast, a FUT1-specific fucosidase diminished the activation of β1 integrin. These results indicated that α1,2-fucosylation of β1 integrin was not involved in integrin-collagen interaction, but promoted β1 integrin activation. Moreover, we demonstrated that CRT regulated FUT1 mRNA degradation at the 3'-UTR. In conclusion, the results of the present study suggest that CRT stabilized FUT1 mRNA, thereby leading to an increase in fucosylation of β1 integrin. Furthermore, increased fucosylation levels activate β1 integrin, rather than directly modifying the integrin-binding sites.

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“…This pathway by GDP-mannose-4,6-dehydratase mutation could be a novel type of cancer progression through cellular fucosylation and natural killer cell-mediated tumor surveillance. However the cellular fucosylation type has not been determined yet (50,51). Fig.…”

Section: Discussionmentioning

confidence: 99%

A Novel Core Fucose-specific Lectin from the Mushroom Pholiota squarrosa

Kobayashi

Tateno

Dohra

et al. 2012

Journal of Biological Chemistry

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106

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Background: Fuc-␣1-6 oligosaccharide has a variety of biological functions. Results: Purification of a novel Fuc␣ 1-6-specific lectin from the mushroom Pholiota squarrosa. Conclusion: The lectin binds only to core ␣1-6-fucosylated N-glycans and not to the other types of fucosylated oligosaccharides. Significance: The lectin will be a promising tool for analyzing the biological functions of ␣1-6 fucosylation.

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GDP-mannose-4,6-dehydratase (GMDS) Deficiency Renders Colon Cancer Cells Resistant to Tumor Necrosis Factor-related Apoptosis-inducing Ligand (TRAIL) Receptor- and CD95-mediated Apoptosis by Inhibiting Complex II Formation

Cited by 43 publications

References 38 publications

Death receptor 5 is activated by fucosylation in colon cancer cells

Death receptor 5 is activated by fucosylation in colon cancer cells

Calreticulin activates β1 integrin via fucosylation by fucosyltransferase 1 in J82 human bladder cancer cells

A Novel Core Fucose-specific Lectin from the Mushroom Pholiota squarrosa

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