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We began analyzing https://link.springer.com/article/10.1007/s00018-022-04365-4, but it redirected us to https://link.springer.com/article/10.1007/s00018-022-04365-4. The analysis below is for the second page.

Title[redir]:
Inhibition of ALG3 stimulates cancer cell immunogenic ferroptosis to potentiate immunotherapy | Cellular and Molecular Life Sciences
Description:
Immune checkpoint blockade therapy has drastically improved the prognosis of certain advanced-stage cancers. However, low response rates and immune-related adverse events remain important limitations. Here, we report that inhibiting ALG3, an a-1,3-mannosyltransferase involved in protein glycosylation in the endoplasmic reticulum (ER), can boost the response of tumors to immune checkpoint blockade therapy. Deleting N-linked glycosylation gene ALG3 in mouse cancer cells substantially attenuates their growth in mice in a manner depending on cytotoxic T cells. Furthermore, ALG3 inhibition or N-linked glycosylation inhibitor tunicamycin treatment synergizes with anti-PD1 therapy in suppressing tumor growth in mouse models of cancer. Mechanistically, we found that inhibiting ALG3 induced deficiencies of post-translational N-linked glycosylation modification and led to excessive lipid accumulation through sterol-regulated element-binding protein (SREBP1)-dependent lipogenesis in cancer cells. N-linked glycosylation deficiency-mediated lipid hyperperoxidation induced immunogenic ferroptosis of cancer cells and promoted a pro-inflammatory microenvironment, which boosted anti-tumor immune responses. In human subjects with cancer, elevated levels of ALG3 expression in tumor tissues are associated with poor patient survival. Taken together, we reveal an unappreciated role of ALG3 in regulating tumor immunogenicity and propose a potential therapeutic strategy for enhancing cancer immunotherapy.

Matching Content Categories {📚}

  • Science
  • Education
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Content Management System {📝}

What CMS is doi.org built with?

Custom-built

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Traffic Estimate {📈}

What is the average monthly size of doi.org audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month


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Keywords {🔍}

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Topics {✒️}

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Schema {🗺️}

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         headline:Inhibition of ALG3 stimulates cancer cell immunogenic ferroptosis to potentiate immunotherapy
         description:Immune checkpoint blockade therapy has drastically improved the prognosis of certain advanced-stage cancers. However, low response rates and immune-related adverse events remain important limitations. Here, we report that inhibiting ALG3, an a-1,3-mannosyltransferase involved in protein glycosylation in the endoplasmic reticulum (ER), can boost the response of tumors to immune checkpoint blockade therapy. Deleting N-linked glycosylation gene ALG3 in mouse cancer cells substantially attenuates their growth in mice in a manner depending on cytotoxic T cells. Furthermore, ALG3 inhibition or N-linked glycosylation inhibitor tunicamycin treatment synergizes with anti-PD1 therapy in suppressing tumor growth in mouse models of cancer. Mechanistically, we found that inhibiting ALG3 induced deficiencies of post-translational N-linked glycosylation modification and led to excessive lipid accumulation through sterol-regulated element-binding protein (SREBP1)-dependent lipogenesis in cancer cells. N-linked glycosylation deficiency-mediated lipid hyperperoxidation induced immunogenic ferroptosis of cancer cells and promoted a pro-inflammatory microenvironment, which boosted anti-tumor immune responses. In human subjects with cancer, elevated levels of ALG3 expression in tumor tissues are associated with poor patient survival. Taken together, we reveal an unappreciated role of ALG3 in regulating tumor immunogenicity and propose a potential therapeutic strategy for enhancing cancer immunotherapy.
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      headline:Inhibition of ALG3 stimulates cancer cell immunogenic ferroptosis to potentiate immunotherapy
      description:Immune checkpoint blockade therapy has drastically improved the prognosis of certain advanced-stage cancers. However, low response rates and immune-related adverse events remain important limitations. Here, we report that inhibiting ALG3, an a-1,3-mannosyltransferase involved in protein glycosylation in the endoplasmic reticulum (ER), can boost the response of tumors to immune checkpoint blockade therapy. Deleting N-linked glycosylation gene ALG3 in mouse cancer cells substantially attenuates their growth in mice in a manner depending on cytotoxic T cells. Furthermore, ALG3 inhibition or N-linked glycosylation inhibitor tunicamycin treatment synergizes with anti-PD1 therapy in suppressing tumor growth in mouse models of cancer. Mechanistically, we found that inhibiting ALG3 induced deficiencies of post-translational N-linked glycosylation modification and led to excessive lipid accumulation through sterol-regulated element-binding protein (SREBP1)-dependent lipogenesis in cancer cells. N-linked glycosylation deficiency-mediated lipid hyperperoxidation induced immunogenic ferroptosis of cancer cells and promoted a pro-inflammatory microenvironment, which boosted anti-tumor immune responses. In human subjects with cancer, elevated levels of ALG3 expression in tumor tissues are associated with poor patient survival. Taken together, we reveal an unappreciated role of ALG3 in regulating tumor immunogenicity and propose a potential therapeutic strategy for enhancing cancer immunotherapy.
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      name:The Department of Biochemistry and Molecular Cell Biology, Molecular Cancer Research Center, School of Medicine, Sun Yat-Sen University, Shenzhen, China
      name:The Department of Biochemistry and Molecular Cell Biology, Molecular Cancer Research Center, School of Medicine, Sun Yat-Sen University, Shenzhen, China
      name:The Department of Biochemistry and Molecular Cell Biology, Molecular Cancer Research Center, School of Medicine, Sun Yat-Sen University, Shenzhen, China
      name:The Department of Biochemistry and Molecular Cell Biology, Molecular Cancer Research Center, School of Medicine, Sun Yat-Sen University, Shenzhen, China
      name:The Department of Biochemistry and Molecular Cell Biology, Molecular Cancer Research Center, School of Medicine, Sun Yat-Sen University, Shenzhen, China
      name:The Department of Biochemistry and Molecular Cell Biology, Molecular Cancer Research Center, School of Medicine, Sun Yat-Sen University, Shenzhen, China
      name:The Department of Biochemistry and Molecular Cell Biology, Molecular Cancer Research Center, School of Medicine, Sun Yat-Sen University, Shenzhen, China
      name:Molecular Diagnostic Laboratory of Cancer Center, Shanghai General Hospital, Shanghai Jiaotong University School of Medicine, Shanghai, China
      name:Department of Dermatology, Duke University Medical Center, Durham, USA
      name:The Department of Biochemistry and Molecular Cell Biology, Molecular Cancer Research Center, School of Medicine, Sun Yat-Sen University, Shenzhen, China
      name:The Department of Biochemistry and Molecular Cell Biology, Molecular Cancer Research Center, School of Medicine, Sun Yat-Sen University, Shenzhen, China
      name:The Department of Biochemistry and Molecular Cell Biology, Molecular Cancer Research Center, School of Medicine, Sun Yat-Sen University, Shenzhen, China
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