Sweet escape: Sialic acids in tumor immune evasion

Büll, Christian; Brok, Martijn H. den; Adema, Gosse J.

doi:10.1016/j.bbcan.2014.07.005

Cited by 109 publications

(130 citation statements)

References 96 publications

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“…Glycans capped with sLe X structures are enriched on the surface of cancer cells, and their presence is correlated with increased cancer progression and poor prognosis (Kannagi et al 2004;Läubli and Borsig 2010b;Pinho and Reis 2015). Work done by several groups suggests that cancer cells employ selectin-ligand interactions to adhere to and extravasate through the endothelium and that ablation or inhibition of selectins reduces metastasis and tumor growth [for example, Biancone et al (1996), Borsig et al (2002), Büll et al (2014a), Kim et al (1998), Läubli and Borsig (2010a, b), Läubli et al (2006)]. Notably, changes in sialylation have been observed following the induction of EMT, a process that allows cancer cells to break away from tumors, migrate and invade.…”

Section: Selectins and The Roles They Play In The Immune System And Cmentioning

confidence: 99%

Sialylation of N-glycans: mechanism, cellular compartmentalization and function

Bhide

Colley

2016

Histochem Cell Biol

182

149

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Sialylated N-glycans play essential roles in the immune system, pathogen recognition and cancer. This review approaches the sialylation of N-glycans from three perspectives. The first section focuses on the sialyltransferases that add sialic acid to N-glycans. Included in the discussion is a description of these enzymes' glycan acceptors, conserved domain organization and sequences, molecular structure and catalytic mechanism. In addition, we discuss the protein interactions underlying the polysialylation of a select group of adhesion and signaling molecules. In the second section, the biosynthesis of sialic acid, CMP-sialic acid and sialylated N-glycans is discussed, with a special emphasis on the compartmentalization of these processes in the mammalian cell. The sequences and mechanisms maintaining the sialyltransferases and other glycosylation enzymes in the Golgi are also reviewed. In the final section, we have chosen to discuss processes in which sialylated glycans, both N- and O-linked, play a role. The first part of this section focuses on sialic acid-binding proteins including viral hemagglutinins, Siglecs and selectins. In the second half of this section, we comment on the role of sialylated N-glycans in cancer, including the roles of β1-integrin and Fas receptor N-glycan sialylation in cancer cell survival and drug resistance, and the role of these sialylated proteins and polysialic acid in cancer metastasis.

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Section: Selectins and The Roles They Play In The Immune System And Cmentioning

confidence: 99%

Sialylation of N-glycans: mechanism, cellular compartmentalization and function

Bhide

Colley

2016

Histochem Cell Biol

182

149

View full text Add to dashboard Cite

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“…Recent reviews by Bull et al [105, 106] have described the specific tumor characteristics associated with the increased expression of sialic acid sugars on the surface of cancer cells. From a sialic acid perspective, the reviews describe evidence to support the role of sialic acids in cancer.…”

Section: Aberrant Sialylation In Cancer Progression and Metastasismentioning

confidence: 99%

“…From a sialic acid perspective, the reviews describe evidence to support the role of sialic acids in cancer. Here, tumor-derived sialic acids have been shown to disable cytotoxicity mechanisms of effector immune cells, trigger production of immune suppressive cytokines and dampen activation of antigen-presenting cells [106]. This aberrant sialylation would indeed favor tumor growth and progression.…”

Section: Aberrant Sialylation In Cancer Progression and Metastasismentioning

confidence: 99%

Neuraminidase-1: A novel therapeutic target in multistage tumorigenesis

2016

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Several of the growth factors and their receptor tyrosine kinases (RTK) such as epidermal growth factor (EGF), platelet-derived growth factor (PDGF), fibroblast growth factor (FGF), vascular endothelial growth factor (VEGF), nerve growth factor (NGF) and insulin are promising candidate targets for cancer therapy. Indeed, tyrosine kinase inhibitors (TKI) have been developed to target these growth factors and their receptors, and have demonstrated dramatic initial responses in cancer therapy. Yet, most patients ultimately develop TKI drug resistance and relapse. It is essential in the clinical setting that the targeted therapies are to circumvent multistage tumorigenesis, including genetic mutations at the different growth factor receptors, tumor neovascularization, chemoresistance of tumors, immune-mediated tumorigenesis and the development of tissue invasion and metastasis. Here, we identify a novel receptor signaling platform linked to EGF, NGF, insulin and TOLL-like receptor (TLR) activations, all of which are known to play major roles in tumorigenesis. The importance of these findings signify an innovative and promising entirely new targeted therapy for cancer. The role of mammalian neuraminidase-1 (Neu1) in complex with matrix metalloproteinase-9 and G protein-coupled receptor tethered to RTKs and TLRs is identified as a major target in multistage tumorigenesis. Evidence exposing the link connecting growth factor-binding and immune-mediated tumorigenesis to this novel receptor-signaling paradigm will be reviewed in its current relationship to cancer.

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“…Many cancer cells develop mechanisms such as increased surface sialylation to avoid detection by natural killer (NK) cells in the innate immune response (Büll et al, 2014; Fuster and Esko, 2005). Using glycan-functionalized polymers containing a terminal phospholipid, different carbohydrates were anchored to the surface of cancer cells (Figure 9A) (Hudak et al, 2013).…”

Section: De Novo Glycan Displaymentioning

confidence: 99%

Glycan Engineering for Cell and Developmental Biology

Griffin

Hsieh‐Wilson

2016

Cell Chemical Biology

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Cell-surface glycans are a diverse class of macromolecules that participate in many key biological processes, including cell-cell communication, development, and disease progression. Thus, the ability to modulate the structures of glycans on cell surfaces provides a powerful means not only to understand fundamental processes but also to direct activity and elicit desired cellular responses. Here, we describe methods to sculpt glycans on cell surfaces and highlight recent successes in which artificially engineered glycans have been employed to control biological outcomes such as the immune response and stem cell fate.

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Sweet escape: Sialic acids in tumor immune evasion

Cited by 109 publications

References 96 publications

Sialylation of N-glycans: mechanism, cellular compartmentalization and function

Sialylation of N-glycans: mechanism, cellular compartmentalization and function

Neuraminidase-1: A novel therapeutic target in multistage tumorigenesis

Glycan Engineering for Cell and Developmental Biology

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