Advancing Oral Cancer Research: Creative Biolabs' Glycosylation Analysis Service
Oral cancer, particularly oral squamous cell carcinoma (OSCC), remains a devastating disease with high morbidity and mortality. Beyond genetic mutations, aberrant glycosylation - the altered attachment of sugar chains to proteins and lipids - is emerging as a crucial hallmark of cancer. Are you currently facing challenges in identifying reliable biomarkers for early detection or prognostic assessment of oral cancer, or struggling to uncover novel therapeutic targets? Our oral cancer research-related glycosylation analysis service helps clients revolutionize oral cancer understanding and accelerate therapeutic development through advanced glycomics and glycoprotein technologies. We provide in-depth glycan and glycopeptide profiling, enabling the discovery of novel biomarkers for early diagnosis, prognosis, and recurrence monitoring. Our service assists in identifying and validating specific glycosylation changes on proteins crucial for tumor progression, offering pathways for targeted therapeutic intervention.
Fig.1 DPAGT1/Wnt/E-cadherin network of the control group and oral cancer group.1
Discover How We Can Help
Our workflow is meticulously designed to provide robust and actionable data, guiding your oral cancer research from initial sample submission to insightful biological conclusions.
Project consultation
We begin with a detailed discussion to understand your specific research goals, sample types, and desired outcomes. This ensures a customized analytical strategy.
Sample processing
Rigorous preparation, including protein extraction, denaturation, and efficient glycan release (N-glycan, O-glycan, or targeted glycopeptide enrichment), is performed under optimized conditions to ensure high yields and purity.
Glycan or glycopeptide separation
Utilizing cutting-edge chromatography techniques (e.g., HILIC-UPLC) to resolve complex glycan mixtures into individual components based on their structural characteristics.
Analysis on state-of-the-art mass spectrometers (e.g., Q-TOF) to acquire highly accurate mass data for glycan and glycopeptide identification and quantification.
Data analysis and interpretation
Raw mass spectrometry data is processed using advanced glyco-bioinformatics software. Our experienced team performs qualitative and quantitative analysis, identifies differentially expressed glycans/glycoproteins, and provides biological interpretation of the findings in the context of oral cancer.
Comprehensive reporting and consultation
You receive a detailed report including raw data, processed results, statistical analyses, and a clear interpretation of the biological significance. Our scientists are available for follow-up consultations to discuss the findings and plan next steps.
What are the Glycosylation Analyses Related to Oral Cancer Research?
Creative Biolabs offers a suite of services specifically tailored for oral cancer glycosylation research:
01N-Glycan profiling
Comprehensive identification and quantification of N-linked glycans from tissue, cells, or biofluids.
02O-Glycan profiling
Detailed analysis of O-linked glycans, including mucin-type O-glycans, which are frequently altered in cancer.
03Site-specific glycosylation analysis (Glycoproteomics)
Identifying specific glycosylation sites on proteins and characterizing the glycans attached to them, crucial for understanding protein function.
04Glycosyltransferase activity assays
Measuring the activity levels of specific enzymes (e.g., sialyltransferases, fucosyltransferases) known to be dysregulated in oral cancer.
05Lectin array/western blotting
Utilizing lectins or glycan-specific antibodies to detect and quantify overall changes in specific glycan epitopes.
What are the Main Glycosylation Changes Observed in Oral Cancer?
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Increased sialylation and fucosylation: Elevated levels of sialyltransferases (e.g., α-2,3 and α-2,6 ST) and α-L-fucosidase activity are frequently observed in oral precancerous conditions and oral cancer, correlating with tumor progression and metastasis.
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Lewis antigen upregulation: Specific carbohydrate structures like Lewis y are often upregulated in OSCC cells. This upregulation can promote cancer cell migration by aberrantly glycosylating key receptors such as the epidermal growth factor receptor (EGFR), thereby modulating its signaling.
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Aberrant glycosylation of immune checkpoints: Glycoproteins involved in immune evasion show significant overexpression and aberrant N-glycosylation in OSCC. These modifications can impact immune response and are associated with increased tumor size and poor survival.
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O-Glycosylation changes: Alterations in O-glycosylation, particularly O-GlcNAc modifications, are correlated with hypoxia-inducible factor-1α (HIF-1α) expression, linking altered metabolism and the tumor microenvironment to aberrant glycosylation in oral cancer.
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Dysregulation of glycosyltransferases: Genes encoding glycosyltransferases, such as DPAGT1 (involved in N-glycosylation), can be dysregulated in oral cancer. This dysregulation impacts the glycosylation of critical proteins like E-cadherin, affecting intercellular adhesion and interacting with pathways like Wnt/β-catenin signaling, which collectively drive oral carcinogenesis.
Why Choose Us?
Creative Biolabs stands at the forefront of glycosylation analysis, uniquely positioned to advance your oral cancer research. Our commitment to cutting-edge technology, rigorous scientific methodology, and unparalleled expertise ensures that your project benefits from the highest standards of quality and accuracy. Creative Biolabs is your dedicated partner in unraveling the complexities of oral cancer. Our team of experts is eager to discuss your project, provide detailed information, and tailor a solution that meets your specific needs. Please contact us to inquire about more details.
Published Data
In OSCC, the CTHRC1 protein is significantly overexpressed, a phenomenon driven by a collaborative interplay between N-glycosylation and canonical Wnt/β-catenin signaling. This study demonstrates that both the DPAGT1 gene (which regulates N-glycosylation) and canonical Wnt signaling pathways converge to increase CTHRC1 levels, ultimately promoting OSCC cell migration and tumor spread. The researchers analyzed human OSCC tissue samples alongside normal adjacent epithelia (AE) to observe the expression patterns of key proteins. They found a marked increase in β-catenin and GPT (the protein product of DPAGT1) in OSCC tissues compared to AE. Both proteins were widely expressed throughout tumor regions, contrasting with their more localized expression in the basal layer of normal epithelium. Importantly, CTHRC1 exhibited a dramatic surge in abundance (over 50-fold) in OSCC. Furthermore, the CTHRC1 protein in OSCC samples displayed a higher molecular weight form, indicating hyperglycosylation. These findings collectively suggest that the increased levels of CTHRC1 in OSCC are associated with enhanced N-glycosylation, implying a potential role for this modification in CTHRC1's function and stability.
Fig.2 Expression results of β-catenin, GPT, and CTHRC1 in OSCC.2
FAQs
Q1: What type of samples are suitable for Creative Biolabs' oral cancer glycosylation analysis service?
A1: We accept a wide range of biological samples, including fresh frozen or FFPE oral tissue biopsies (tumor and adjacent normal), various oral cancer cell lines, saliva, serum, plasma, and purified proteins or glycoproteins. Our team will guide you on optimal sample collection and preparation to ensure the best analytical outcomes.
Q2: How can this service help in identifying novel therapeutic targets for oral cancer?
A2: Our detailed glycan and glycoproteome profiling can pinpoint specific aberrant glycan structures or glycosylation patterns uniquely present in oral cancer cells. By identifying the proteins carrying these glycans or the enzymes responsible for their synthesis, you can uncover novel targets for drug development, leading to more precise and effective anti-cancer strategies.
Q3: Is Creative Biolabs' service capable of distinguishing between different stages or metastatic potential of oral cancer?
A3: Absolutely. Aberrant glycosylation patterns often correlate with tumor progression, invasiveness, and metastatic potential. Our advanced comparative glycomics and glycoproteomics analyses are designed to identify subtle yet significant glycan changes that can differentiate between various disease stages, potentially aiding in prognostic assessment and treatment stratification.
Customer Review
Enhanced Biomarker Discovery!
"Using Creative Biolabs's oral cancer research-related glycosylation analysis service in our preliminary studies has significantly improved our ability to identify novel diagnostic and prognostic glyco-biomarkers for oral cancer. The detailed glycan profiling provided an unparalleled level of specificity compared to our in-house assays." - Ms. E. Har***s.
Critical Mechanistic Insights!
"Creative Biolabs' analysis was instrumental in elucidating the role of specific glycosylation changes on critical signaling proteins in oral cancer cell migration. Their comprehensive report allowed us to connect aberrant glycosylation patterns directly to cellular functions, opening new avenues for therapeutic intervention." - Mr. G. Lew***s.
References
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Varelas, Xaralabos, Meghan P. Bouchie, and Maria A. Kukuruzinska. "Protein N-glycosylation in oral cancer: dysregulated cellular networks among DPAGT1, E-cadherin adhesion and canonical Wnt signaling." Glycobiology 24.7 (2014): 579-591. DOI: 10.1093/glycob/cwu031. Distributed under Open Access license CC BY, without modification.
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Liu, Gangli, et al. "N-glycosylation induces the CTHRC1 protein and drives oral cancer cell migration." Journal of Biological Chemistry 288.28 (2013): 20217-20227. DOI: 10.1074/jbc.M113.473785. Distributed under Open Access license CC BY 4.0, without modification.
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