Dataset Information

Role of aberrant glycosylation enzymes in oral cancer progression.

ABSTRACT:

Background

Carcinogenesis, a multistep process involves sequential changes during neoplastic transformation. The various hallmarks of cancer aid in cell survival, proliferation, and dissemination. Aberrant glycosylation, a recently defined hallmark of cancer, is influenced by glycosylation enzymes during carcinogenesis. Therefore, the present study measured ?-2,3 and ?-2,6 sialyltransferase (ST), sialidase, and ?-L-fucosidase activity in patients with oral precancerous conditions (OPC) and oral cancer patients.

Subjects

The study enrolled 100 oral cancer patients, 50 patients with OPC, 100 healthy controls, and 46 posttreatment follow-ups of oral cancer patients. Blood and saliva were collected from all the participants.

Materials and methods

Sialidase activity was measured by spectrofluorimetric method, ?-2,3 and ?-2,6 ST by ELISA using biotinylated lectins, and ?-L-fucosidase by spectrophotometric method.

Results

The results depicted increased levels of sialidase, ?-2,3 and ?-2,6 ST, ?-L-fucosidase in patients with OPC and oral cancer patients. Receiver operating characteristic curve indicated significant discriminatory efficacy in distinguishing controls and oral cancer patients for serum and salivary sialidase and ?-L-fucosidase activity, and serum ?-2,6 ST. Furthermore, serum and salivary ?-L-fucosidase activity and serum sialidase activity significantly distinguished controls and patients with OPC. Serum and salivary sialidase, ?-L-fucosidase, and serum ?-2,3 ST activity were higher in patients with metastasis as compared to nonmetastatic patients. Higher values of serum ?-L-fucosidase activity were significantly associated with low-overall survival.

Conclusion

The increased levels of enzymes correlated with tumor initiation, progression, and metastasis in oral cancer patients. The alterations in glycosyltransferases/glycosidases thus support the view of glycosylation as a hallmark of cancer.

SUBMITTER: Vajaria BN

PROVIDER: S-EPMC6166416 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature

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Publications

Role of aberrant glycosylation enzymes in oral cancer progression.

Vajaria Bhairavi N BN Patel Kinjal A KA Patel Prabhudas S PS

Journal of carcinogenesis 20180925

<h4>Background</h4>Carcinogenesis, a multistep process involves sequential changes during neoplastic transformation. The various hallmarks of cancer aid in cell survival, proliferation, and dissemination. Aberrant glycosylation, a recently defined hallmark of cancer, is influenced by glycosylation enzymes during carcinogenesis. Therefore, the present study measured α-2,3 and α-2,6 sialyltransferase (ST), sialidase, and α-L-fucosidase activity in patients with oral precancerous conditions (OPC) a ...[more]

PMID: 30294247

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Project description:BackgroundVascular endothelial growth factor (VEGF) signaling pathway plays an important role in the progression of diabetic retinopathy (DR). The glycosylation modification process of many key functional proteins in DR patients is abnormal. However, the potential involvement of abnormal N-glycoproteins in DR progression remains unclear.MethodsGlycoproteomic profiling of the vitreous humor was performed. The level of protein and N-glycoprotein was confirmed by Western blot and Lectin blot, respectively. The cell viability and migration efficiency were detected by CCK-8 and Transwell assay. Flow cytometry was conducted to analyze the level of cell apoptosis and reactive oxygen specie. Malondialdehyde, superoxide dismutase activity and VEGF content were detected by Enzyme linked immunosorbent assays. The interaction of metalloproteinase 1 (TIMP-1) with N-acetylglucosamine transferase V (GnT-V) was detected by GST pull-down. Hematoxylin and eosin staining and choroidal and retinal flat mount stained with fluorescein isothiocyanate-Dextran assay were used for functional research in vivo.ResultsWe found that N-glycosylation was up-regulated in DR rats and high glucose (HG)-induced human retinal pigment epithelium cell line ARPE-19. HG-induced inhibited the viability of ARPE-19 cells and promoted cell apoptosis and oxidative stress (OS), but these effects were reversed with kifunensine treatment, GnT-V knockdown and TIMP-1 mutation. Additionally, GnT-V binds to TIMP-1 to promote N-glycosylation of TIMP-1. Over-expression of GnT-V inhibited the viability of ARPE-19 cells and promoted cell apoptosis, OS and VEGF release, which these effects were reversed with TIMP-1 mutation. Interestingly, over-expression of GnT-V promoted retinal microvascular endothelial cells (RMECs) angiogenesis but was revered with TIMP-1 mutation, which was terminally boosted by VEGF-A treatment. Finally, knockdown of GnT-V relieved DR progression.ConclusionThe findings indicate that GnT-V can promote RMECs angiogenesis and ARPE-19 cells injury through activation VEGF signaling pathway by increasing TIMP-1 N-glycosylation level, which provides a new theoretical basis for the prevention of DR.

Dataset Information

Role of aberrant glycosylation enzymes in oral cancer progression.

Background

Subjects

Materials and methods

Results

Conclusion

Publications

Role of aberrant glycosylation enzymes in oral cancer progression.

Similar Datasets

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