Sialylation is involved in cell fate decision during development, reprogramming and cancer progression

Li, Fenjie; Ding, Junjun

doi:10.1007/s13238-018-0597-5

Cited by 129 publications

(99 citation statements)

References 128 publications

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“…It is important to note that the level of sialylation increased independently of the number of galactose residues, indicating that its increase was not merely an effect of increased antennarity, but likely due to the increased activity or presence of the sialyltransferases. These findings are in line with the current literature, as sialylation is known to play an important role in cellular recognition, cell adhesion and cell signaling [32][33][34]. Increased sialylation (both α2,3-and α2,6-linked) has been previously associated with different cancer types, including colon, stomach and ovarian cancer [10,35].…”

Section: Discussionsupporting

confidence: 90%

N-Glycomic Signature of Stage II Colorectal Cancer and Its Association With the Tumor Microenvironment

Boyaval

Zeijl

Dalebout

et al. 2021

Molecular & Cellular Proteomics

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The choice for adjuvant chemotherapy in stage II colorectal cancer (CRC) is controversial as many patients are cured by surgery alone and it is difficult to identify patients with high-risk of recurrence of the disease. There is a need for better stratification of this group of patients. Mass spectrometry imaging could identify patients at risk. We report here the N-glycosylation signatures of the different cell populations in a group of stage II CRC tissue samples. The cancer cells, compared to normal epithelial cells, have increased levels of sialylation and high-mannose glycans, as well as decreased levels of fucosylation and highly branched N-glycans. When looking at the interface between cancer and its microenvironment, it seems that the cancer N-glycosylation signature spreads into the surrounding stroma at the invasive front of the tumor. This finding was more outspoken in patients with a worse outcome within this sample group.

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Section: Discussionsupporting

confidence: 90%

N-Glycomic Signature of Stage II Colorectal Cancer and Its Association With the Tumor Microenvironment

Boyaval

Zeijl

Dalebout

et al. 2021

Molecular & Cellular Proteomics

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“…N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc) are the two major sialic acids in mammals [3]. Because of their negative electric charge, sialic acids play crucial roles in a variety of cellular functions, e.g., cell-cell interaction, determining conformation of glycoproteins on cell membranes, and masking antigenic determinants on receptor molecules [4][5][6][7][8][9][10][11].…”

Section: Introductionmentioning

confidence: 99%

Sialidase NEU1 suppresses progression of human bladder cancer cells by inhibiting fibronectin-integrin α5β1 interaction and Akt signaling pathway

et al. 2020

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Background: Sialic acids are widely distributed in animal tissues, and aberrantly expressed in a variety of cancer types. High expression of sialic acid contributes to tumor aggressiveness by promoting cell proliferation, migration, angiogenesis, and metastasis. Sialidases are responsible for removal of sialic acids from glycoproteins and glycolipids. Methods: N-glycomics of bladder cancer cells were detected by MALDI-TOF mass spectrometry. Sialic acid modification in bladder cancer tissue was determined by lectin blot. The down-regulation of NEU1 in bladder cancer cells was determined by high resolution liquid chromatography mass spectrometry (HR LC-MS). The effects of sialidase NEU1 expression on proliferation and apoptosis of human bladder cancer cells were examined by western blot, RT-PCR, confocal imaging and flow cytometry. Moreover, the function of sialic acids on fibronectinintegrin α5β1 interaction were assayed by immunoprecipitation and ELISA. The importance of NEU1 in tumor formation in vivo was performed using BALB/c-nu mice. Expression of NEU1 in primary human bladder cancer tissue samples was estimated using bladder cancer tissue microarray. Results: (1) Downregulation of NEU1 was primarily responsible for aberrant expression of sialic acids in bladder cancer cells. (2) Decreased NEU1 expression was correlated with bladder cancer progression. (3) NEU1 overexpression enhanced apoptosis and reduced proliferation of bladder cancer cells. (4) NEU1 disrupted FNintegrin α5β1 interaction and deactivated the Akt signaling pathway. (5) NEU1 significantly suppressed in vivo tumor formation in BALB/c-nu mice. Conclusions: Our data showed that NEU1 inhibited cancer cell proliferation, induced apoptosis, and suppressed tumor formation both in vitro and in vivo, by disrupting interaction of FN and integrin β1 and inhibiting the Akt signaling pathway. Our observations indicate that NEU1 is an important modulator of the malignant properties of bladder cancer cells, and is a potential therapeutic target for prognosis and treatment of bladder cancer.

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“…Another enzyme immediately downstream of GALNT1-20 is ST6GAL1 (β-galactoside α-2,6-sialyltransferase 1), which is necessary for the synthesis of the sialyl Tn-antigen. Both ST6GAL1 upregulation and enhanced expression of the sialyl TN-antigen are well-known biomarkers for several types of cancer (Li and Ding, 2018). ST6GAL1 protein levels are also not different in schizophrenia STG (unpublished results).…”

Section: Discussionmentioning

confidence: 87%

Altered protein expression of galactose and N-acetylgalactosamine transferases in schizophrenia superior temporal gyrus

Mueller

Mallepalli

Meador‐Woodruff

2019

Preprint

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Abnormal glycosylation in schizophrenia brain has been previously implicated in disruptions to protein trafficking, localization, and function. Glycosylation is an enzyme-mediated posttranslational modification and, along with reports of altered glycan biosynthesis and abnormal glycan levels in peripheral fluids, growing evidence for altered glycosylation pathway activity in schizophrenia prompted investigation of specific enzymes which may be responsible for these abnormalities. Glycosylation is a highly variable yet tightly controlled cellular process and, depending on the molecule(s) affected, altered glycan modifications can influence the trajectory of many key functional pathways. In a preliminary gene array study, abnormal transcript expression of 36 glycosylation-associated enzymes was identified in schizophrenia brain. Subsequently, protein expression abnormalities of enzymes which act on glucose (UGGT2), mannose (EDEM2), fucose (FUT8, POFUT2), and N-acetylglucosamine (MGAT4A, B3GNT8) have been reported in this illness. The current study investigates protein expression levels by western blot analysis of the galactose and N-acetylgalactosamine (GalNAc) transferases B3GALTL1, B4GALT1, C1GALT1, GALNT2, GALNT7, GALNT16, and GALNTL5, as well as a related chaperone protein, COSMC, in superior temporal gyrus of age-and sex-matched pairs of schizophrenia and non-psychiatrically ill comparison subjects (N = 16 pairs). In schizophrenia, reduced β-1,4-galactosyltransferase 1 (B4GALT1) and polypeptide GalNAc-transferase 16 (GALNT16) were identified. These findings add support to the hypothesis that dysregulated glycosylation-associated enzyme expression contributes to altered protein glycosylation and downstream substrate-specific defects in schizophrenia.

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Sialylation is involved in cell fate decision during development, reprogramming and cancer progression

Cited by 129 publications

References 128 publications

N-Glycomic Signature of Stage II Colorectal Cancer and Its Association With the Tumor Microenvironment

N-Glycomic Signature of Stage II Colorectal Cancer and Its Association With the Tumor Microenvironment

Sialidase NEU1 suppresses progression of human bladder cancer cells by inhibiting fibronectin-integrin α5β1 interaction and Akt signaling pathway

Altered protein expression of galactose and N-acetylgalactosamine transferases in schizophrenia superior temporal gyrus

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