Glycosylation as a regulator of site-specific metastasis

Bindeman, Wendy; Fingleton, Barbara

doi:10.1007/s10555-021-10015-1

Cited by 16 publications

(8 citation statements)

References 142 publications

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“…It is widely known that N-linked protein glycosylation is an important cotranslational and post-translational modification in biology, playing an essential part in development, organ specific function and disease ( Zielinska et al, 2010 ; Esmail and Manolson, 2021 ). Tumor-related glycosylation alterations are connected with tumor progression, malignant transformation and immune evasion ( Rodrigues et al, 2018 ; Bindeman and Fingleton, 2022 ). In view of the important role of glycosylation in tumor development, glycosylation inhibition has exhibited huge potential as an auxiliary means of antitumor therapies ( Song et al, 2020 ).…”

Section: Discussionmentioning

confidence: 99%

Nascent Glycoproteome Reveals That N-Linked Glycosylation Inhibitor-1 Suppresses Expression of Glycosylated Lysosome-Associated Membrane Protein-2

Cao

Meng

Shao

et al. 2022

Front. Mol. Biosci.

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Glycosylation inhibition has great potential in cancer treatment. However, the corresponding cellular response, protein expression and glycosylation changes remain unclear. As a cell-permeable small-molecule inhibitor with reduced cellular toxicity, N-linked glycosylation inhibitor-1 (NGI-1) has become a great approach to regulate glycosylation in mammalian cells. Here for the first time, we applied a nascent proteomic method to investigate the effect of NGI-1 in hepatocellular carcinoma (HCC) cell line. Besides, hydrophilic interaction liquid chromatography (HILIC) was adopted for the enrichment of glycosylated peptides. Glycoproteomic analysis revealed the abundance of glycopeptides from LAMP2, NICA, and CEIP2 was significantly changed during NGI-1 treatment. Moreover, the alterations of LAMP2 site-specific intact N-glycopeptides were comprehensively assessed. NGI-1 treatment also led to the inhibition of Cathepsin D maturation and the induction of autophagy. In summary, we provided evidence that NGI-1 repressed the expression of glycosylated LAMP2 accompanied with the occurrence of lysosomal defects and autophagy.

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Section: Discussionmentioning

confidence: 99%

Nascent Glycoproteome Reveals That N-Linked Glycosylation Inhibitor-1 Suppresses Expression of Glycosylated Lysosome-Associated Membrane Protein-2

Cao

Meng

Shao

et al. 2022

Front. Mol. Biosci.

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“…Glycosylation is a ubiquitous feature of cellular proteins in which sugar groups are enzymatically added post-translationally to proteins and lipids in order to generate glycan chains ( 82 ). Alterations to glycosylation in cancer has been identified as a potential driver of metastasis, and moreover, may play a role in premeditating the site-preference exhibited by cancer cells when forming secondary metastatic tumours ( 83 , 84 ). Although not widely investigated, a cohort of studies have published findings indicating that changes to glycans and their associated glycosylation enzymes may play a role in predisposing PCa cells to establishing secondary tumours at the bone.…”

Section: Bone Metastases Formation In Prostate Cancermentioning

confidence: 99%

Prostate cancer bone metastases biology and clinical management (Review)

2023

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Prostate cancer (PCa) is one of the most prominent causes of cancer-related mortality in the male population. A highly impactful prognostic factor for patients diagnosed with PCa is the presence or absence of bone metastases. The formation of secondary tumours at the bone is the most commonly observed site for the establishment of PCa metastases and is associated with reduced survival of patients in addition to a cohort of life-debilitating symptoms, including mobility issues and chronic pain. Despite the prevalence of this disease presentation and the high medical relevance of bone metastases, the mechanisms underlying the formation of metastases to the bone and the understanding of what drives the osteotropism exhibited by prostate tumours remain to be fully elucidated. This lack of in-depth understanding manifests in limited effective treatment options for patients with advanced metastatic PCa and culminates in the low rate of survival observed for this sub-set of patients. The present review aims to summarise the most recent promising advances in the understanding of how and why prostate tumours metastasise to the bone, with the ultimate aim of highlighting novel treatment and prognostic targets, which may provide the opportunity to improve the diagnosis and treatment of patients with PCa with bone metastases.

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“…Furthermore, steric hindrance caused by cell surface polySia confers the anti-adhesive property to polySia-positive tumors and facilitates metastatic or invasive growth [ 37 ]. Overall, altered sialylation is involved in the spread of some malignancies [ 56 ] ( Figure 4 ).…”

Section: Sialylation and Cancer Metastasismentioning

confidence: 99%

Insights into the Role of Sialylation in Cancer Metastasis, Immunity, and Therapeutic Opportunity

Huang

Zhang

2022

Cancers

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Sialylation is an enzymatic process that covalently attaches sialic acids to glycoproteins and glycolipids and terminates them by creating sialic acid-containing glycans (sialoglycans). Sialoglycans, usually located in the outmost layers of cells, play crucial biological roles, notably in tumor transformation, growth, metastasis, and immune evasion. Thus, a deeper comprehension of sialylation in cancer will help to facilitate the development of innovative cancer therapies. Cancer sialylation-related articles have consistently increased over the last four years. The primary subjects of these studies are sialylation, cancer, immunotherapy, and metastasis. Tumor cells activate endothelial cells and metastasize to distant organs in part by the interactions of abnormally sialylated integrins with selectins. Furthermore, cancer sialylation masks tumor antigenic epitopes and induces an immunosuppressive environment, allowing cancer cells to escape immune monitoring. Cytotoxic T lymphocytes develop different recognition epitopes for glycosylated and nonglycosylated peptides. Therefore, targeting tumor-derived sialoglycans is a promising approach to cancer treatments for limiting the dissemination of tumor cells, revealing immunogenic tumor antigens, and boosting anti-cancer immunity. Exploring the exact tumor sialoglycans may facilitate the identification of new glycan targets, paving the way for the development of customized cancer treatments.

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Glycosylation as a regulator of site-specific metastasis

Cited by 16 publications

References 142 publications

Nascent Glycoproteome Reveals That N-Linked Glycosylation Inhibitor-1 Suppresses Expression of Glycosylated Lysosome-Associated Membrane Protein-2

Nascent Glycoproteome Reveals That N-Linked Glycosylation Inhibitor-1 Suppresses Expression of Glycosylated Lysosome-Associated Membrane Protein-2

Prostate cancer bone metastases biology and clinical management (Review)

Insights into the Role of Sialylation in Cancer Metastasis, Immunity, and Therapeutic Opportunity

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