Sialylation: an Avenue to Target Cancer Cells

Vajaria, Bhairavi N.; Patel, Kinjal D.; Begum, Rasheedunnisa; Patel, Prabhudas S.

doi:10.1007/s12253-015-0033-6

Cited by 103 publications

(57 citation statements)

References 34 publications

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“…Gangliosides are acid glycosphingolipids that carry one or more residues of sialic acid, and are more abundant in the brain [127, 130]. Sialin, a gene for sialic acid transporter, is upregulated in colon cancer CaCo-2M cells and breast cancer ZR-75-1 cells submitted to hypoxic conditions, and is related to enhanced gangliosides carrying N-glycolyl sialic acid (NeuGc) [131].…”

Section: Hypoxia Changes Membrane Glycoconjugates In Tumor Cellsmentioning

confidence: 99%

Glycobiology Modifications in Intratumoral Hypoxia: The Breathless Side of Glycans Interaction

Silva-filho¹,

Sena²,

Lima

et al. 2017

Cell Physiol Biochem

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Post-translational and co-translational enzymatic addition of glycans (glycosylation) to proteins, lipids, and other carbohydrates, is a powerful regulator of the molecular machinery involved in cell cycle, adhesion, invasion, and signal transduction, and is usually seen in both in vivo and in vitro cancer models. Glycosyltransferases can alter the glycosylation pattern of normal cells, subsequently leading to the establishment and progression of several diseases, including cancer. Furthermore, a growing amount of research has shown that different oxygen tensions, mainly hypoxia, leads to a markedly altered glycosylation, resulting in altered glycan-receptor interactions. Alteration of intracellular glucose metabolism, from aerobic cellular respiration to anaerobic glycolysis, inhibition of integrin 3α1β translocation to the plasma membrane, decreased 1,2-fucosylation of cell-surface glycans, and galectin overexpression are some consequences of the hypoxic tumor microenvironment. Additionally, increased expression of gangliosides carrying N-glycolyl sialic acid can also be significantly affected by hypoxia. For all these reasons, it is possible to realize that hypoxia strongly alters glycobiologic events within tumors, leading to changes in their behavior. This review aims to analyze the complexity and importance of glycoconjugates and their molecular interaction network in the hypoxic context of many solid tumors.

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Section: Hypoxia Changes Membrane Glycoconjugates In Tumor Cellsmentioning

confidence: 99%

Glycobiology Modifications in Intratumoral Hypoxia: The Breathless Side of Glycans Interaction

Silva-filho¹,

Sena²,

Lima

et al. 2017

Cell Physiol Biochem

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“…Although not included in the original and next generation hallmarks, aberrant glycosylation is now also widely recognised as a new hallmark of cancer causally associated with all of the hallmark capabilities (2,3,6). One of the most widely occurring cancer associated changes in glycosylation is abnormal sialylation, which is often driven by the altered expression of sialyltranserase enzymes (7)(8)(9) and is linked to poor patient prognosis and metastasis (10)(11)(12)(13). Several sialyltransferase enzymes are implicated in cancer, but in recent years ST6GAL1 (which catalyses the addition of α2,6-linked sialic acids onto terminal N-glycans) has become increasingly dominant in the literature.…”

Section: Introductionmentioning

confidence: 99%

ST6GAL1: A key player in cancer (Review)

et al. 2019

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Aberrant glycosylation is a universal feature of cancer cells and there is now overwhelming evidence that glycans can modulate pathways intrinsic to tumour cell biology. Glycans are important in all of the cancer hallmarks and there is a renewed interest in the glycomic profiling of tumours to improve early diagnosis, determine patient prognosis and identify targets for therapeutic intervention. One of the most widely occurring cancer associated changes in glycosylation is abnormal sialylation which is often accompanied by changes in sialyltransferase activity. Several sialyltransferases are implicated in cancer, but in recent years ST6 β-galactoside α-2,6-sialyltransferase 1 (ST6GAL1) has become increasingly dominant in the literature. ST6GAL1 catalyses the addition of α2,6-linked sialic acids to terminal N-glycans and can modify glycoproteins and/or glycolipids. ST6GAL1 is upregulated in numerous types of cancer (including pancreatic, prostate, breast and ovarian cancer) and can promote growth, survival and metastasis. The present review discusses ST6GAL in relation to the hallmarks of cancer, and highlights its key role in multiple mechanisms intrinsic to tumour cell biology.

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“…The alteration of cell membrane protein sialylation is often involved in the development of cancer and tumor metastasis (Pinho and Reis, 2015; Vajaria et al, 2015). Using specific lectin SNA, we found that UT-B1 from bladder cancer has defective alpha-2,6-sialylation.…”

Section: Discussionmentioning

confidence: 99%

Identification of a Novel UT-B Urea Transporter in Human Urothelial Cancer

Alemozaffar

Yang

et al. 2017

Front. Physiol.

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The urea transporter UT-B is widely expressed and has been studied in erythrocyte, kidney, brain and intestines. Interestingly, UT-B gene has been found more abundant in bladder than any other tissue. Recently, gene analyses demonstrate that SLC14A1 (UT-B) gene mutations are associated with bladder cancer, suggesting that urea transporter UT-B may play an important role in bladder carcinogenesis. In this study, we examined UT-B expression in bladder cancer with human primary bladder cancer tissues and cancer derived cell lines. Human UT-B has two isoforms. We found that normal bladder expresses long form of UT-B2 but was lost in 8 of 24 (33%) or significantly downregulated in 16 of 24 (67%) of primary bladder cancer patients. In contrast, the short form of UT-B1 lacking exon 3 was detected in 20 bladder cancer samples. Surprisingly, a 24-nt in-frame deletion in exon 4 in UT-B1 (UT-B1Δ24) was identified in 11 of 20 (55%) bladder tumors. This deletion caused a functional defect of UT-B1. Immunohistochemistry revealed that UT-B protein levels were significantly decreased in bladder cancers. Western blot analysis showed a weak UT-B band of 40 kDa in some tumors, consistent with UT-B1 gene expression detected by RT-PCR. Interestingly, bladder cancer associate UT-B1Δ24 was barely sialylated, reflecting impaired glycosylation of UT-B1 in bladder tumors. In conclusion, SLC14A1 gene and UT-B protein expression are significantly changed in bladder cancers. The aberrant UT-B expression may promote bladder cancer development or facilitate carcinogenesis induced by other carcinogens.

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Sialylation: an Avenue to Target Cancer Cells

Cited by 103 publications

References 34 publications

Glycobiology Modifications in Intratumoral Hypoxia: The Breathless Side of Glycans Interaction

Glycobiology Modifications in Intratumoral Hypoxia: The Breathless Side of Glycans Interaction

ST6GAL1: A key player in cancer (Review)

Identification of a Novel UT-B Urea Transporter in Human Urothelial Cancer

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