Aberrant Glycosylation in Cancer: A Novel Molecular Mechanism Controlling Metastasis

Magalhães, Ana; Duarte, Hugo; Reis, Celso A.

doi:10.1016/j.ccell.2017.05.012

Cited by 139 publications

(110 citation statements)

References 10 publications

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“…Cancer development and progression encompass major alterations in cell glycosylation, including incomplete synthesis of O ‐glycan structures, increased expression of branched N ‐glycans, expression of terminal sialylated glycans, and altered fucosylation. Reprinted from with permission.…”

Section: Aberrant Glycan Expressionmentioning

confidence: 99%

“…Glycans are also determining the interaction between cancer cells and tumor environment, especially the ECM. Glycan alternations are responsible for tumor progression because of modulation of oncogenic receptors, proteoglycans, and adhesion proteins .…”

Section: Analytical Approachesmentioning

confidence: 99%

“…It is certain that glycosylation does not only affect growth and survival directly, but also promotes tumor‐induced immunomodulation and possibly metastases . Aberrant glycosylation in tumors and tumor‐associated carbohydrate antigens is associated with oncogenic transformation and plays an important role in tumor progression and metastasis . At the molecular level, glycosylation actively regulates protein folding, activation and degradation, and interferes with proteolytic cleavage.…”

Section: Introductionmentioning

confidence: 99%

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Glycosylation and metastases

2018

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The change of cellular glycosylation is one of the key events in malignant transformation and neoplastic progression, and tumor‐related glycosylation alterations are promising targets in both tumor diagnosis and therapy. Both malignant transformation and neoplastic progression are the consequence of gene expression alterations and alterations in protein expression. Micro environmental factors such as extracellular matrix (ECM) also play an important role in their growth and metastasis. Tumor‐associated glycans are important biomarker candidates for cancer diagnosis and prognosis, and analytical methods for their detection were developed recently. Glycoproteomics that use mass spectrometry for identification of cancer antigens and structural analysis of glycans play a key role in the investigation of changes of glycosylation during malignant transformation and tumor development and metastasis. Deep understanding of glycan remodeling in cancer and the role of glycosyltransferases that are involved in this process will require a detailed profiling of glycosylation patterns of tumor cells, and corresponding analytical methods for their detection were developed.

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Section: Aberrant Glycan Expressionmentioning

confidence: 99%

Section: Analytical Approachesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Glycosylation and metastases

2018

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“…Altered N‐glycosylation is catalyzed by the specificity of glycosyltransferases, including FUTs, N‐acetylglucosaminyltransferases, galactosyltransferases, and sialyltransferases in the Golgi apparatus . Previous studies have shown that the expression levels of N‐glycan branching enzymes (such as α‐1,6‐mannosyl‐glycoprotein β‐1,2‐ N ‐acetylglucosaminyltransferase and α‐1,3‐mannosyl‐glycoprotein 4‐β‐ N ‐acetylglucosaminyltransferase A), sialyltransferases (such as ST6 β‐galactoside α‐2,6‐sialyltransferase [ST6GAL]1 and ST6GAL2) and β1,6‐branched N‐linked oligosaccharides, are increased in melanoma cells, and these increases in expression contribute to the invasive and metastatic potential of melanoma cells …”

Section: Introductionmentioning

confidence: 99%

“…9 Previous studies have shown that the expression levels of N-glycan branching enzymes (such as α-1,6-mannosyl-glycoprotein β-1,2-N-acetylglucosaminyltransferase and α-1,3-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase A), sialyltransferases (such as ST6 β-galactoside α-2,6-sialyltransferase [ST6GAL]1 and ST6GAL2) and β1,6-branched N-linked oligosaccharides, are increased in melanoma cells, and these increases in expression contribute to the invasive and metastatic potential of melanoma cells. 10,11 FUT enzymes serve an important role in the synthesis of fucosylated glycans. FUT1 and FUT2 catalyze the transfer of a fucose residue in an α-1,2-linkage to the terminal galactose (Gal) residue in N-glycans.…”

Section: Introductionmentioning

confidence: 99%

Role of fucosyltransferase IV in the migration and invasion of human melanoma cells

et al. 2020

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Malignant melanoma is one of the most aggressive human tumor types, mainly due to its high invasion capability, metastatic properties, and the absence of effective treatments. Glycosylation serves a pivotal role in the migration and invasion of melanoma. However, differences in glycosylation between high and low metastatic melanoma cells and how these regulate migration and invasion by altering the expression of fucosyltransferases (FUTs) remain unclear. In the present study, matrix‐assisted laser desorption/ionization‐time‐of‐flight‐mass spectrometry (MALDI‐TOF‐MS) analysis revealed that the composition profiling of fucosylated N‐glycans differed between high metastatic C8161 and low metastatic A375P cells. Further analysis revealed that FUT4 expression was significantly increased in C8161 cells. Melanoma tissue arrays further demonstrated that FUT4 was overexpressed in metastatic samples. Altered FUT4 expression was accompanied by a change in the migration and invasion capacity of the cells. In addition, the migration and invasion potential of melanoma cells were decreased in C8161 and increased in A375P cells upon altering FUT4 expression levels by small interfering RNA or complementary DNA transfection. Furthermore, regulating FUT4 expression markedly modulated the activity of the phosphoinositide‐3‐kinase/Akt (PI3K/Akt) signaling pathway, which affected melanoma cell migration and invasion. In conclusion, FUT4 is a novel biomarker and regulator of the migration and invasion of melanoma cells and may serve as a therapeutic target for melanoma.

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Surfaceome: a new era in the discovery of immune evasion mechanisms of circulating tumor cells

Masmoudi,

Vialaret,

Hirtz

et al. 2024

Molecular Oncology

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Circulating tumor cells (CTCs) are cancer cells that detach from the original site and reach the bloodstream. The most aggressive CTCs survive various immune system attacks and initiate metastasis formation. Importantly, CTCs are not specifically targeted by the current immunotherapies due to the limited knowledge on specific targets. Proteomic profiling can be a powerful tool for understanding some of the immune evasion mechanisms used by cancer cells and particularly CTCs. These mechanisms are generally linked to the expression of specific surface proteins/peptides (i.e. the surfaceome). The study of the peptides that bind to class I molecules of the major histocompatibility complex (MHC‐I) and of the various glycoproteins expressed on CTC surface may open a completely new avenue for the discovery of novel mechanisms of immune evasion. In this review, we discuss how immunopeptidomic and glycoproteomic studies of CTCs that interact with immune cells could help to better understand how metastasis‐initiator CTCs escape the host immune response. We also describe how immunopeptidomic and glycoproteomic studies are carried out.

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Aberrant Glycosylation in Cancer: A Novel Molecular Mechanism Controlling Metastasis

Cited by 139 publications

References 10 publications

Glycosylation and metastases

Glycosylation and metastases

Role of fucosyltransferase IV in the migration and invasion of human melanoma cells

Surfaceome: a new era in the discovery of immune evasion mechanisms of circulating tumor cells

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