Aberrant protein glycosylation: Implications on diagnosis and Immunotherapy

Glycosylation-mediated post-translational modification is critical for regulating many fundamental processes like cell division, differentiation, immune response, and cell-to-cell interaction. Alterations in the N-linked or O-linked glycosylation pattern of regulatory proteins like transcription fac...

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Published in:Biotechnology advances 2023-09, Vol.66, p.108149-108149, Article 108149
Main Authors: Bangarh, Rashmi, Khatana, Chainika, Kaur, Simranjeet, Sharma, Anchita, Kaushal, Ankur, Siwal, Samarjeet Singh, Tuli, Hardeep Singh, Dhama, Kuldeep, Thakur, Vijay Kumar, Saini, Reena V., Saini, Adesh K.
Format: Article
Language:English
Subjects:
Cancer
glycans
Glycosylation
Glycosyltransferases - metabolism
Humans
Immunotherapy
Lectins - metabolism
Metastasis
Multi-omics
Neoplasms - diagnosis
Neoplasms - genetics
Neoplasms - therapy
Polysaccharides - chemistry
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Summary:Glycosylation-mediated post-translational modification is critical for regulating many fundamental processes like cell division, differentiation, immune response, and cell-to-cell interaction. Alterations in the N-linked or O-linked glycosylation pattern of regulatory proteins like transcription factors or cellular receptors lead to many diseases, including cancer. These alterations give rise to micro- and macro-heterogeneity in tumor cells. Here, we review the role of O- and N-linked glycosylation and its regulatory function in autoimmunity and aberrant glycosylation in cancer. The change in cellular glycome could result from a change in the expression of glycosidases or glycosyltransferases like N-acetyl-glucosaminyl transferase V, FUT8, ST6Gal-I, DPAGT1, etc., impact the glycosylation of target proteins leading to transformation. Moreover, the mutations in glycogenes affect glycosylation patterns on immune cells leading to other related manifestations like pro- or anti-inflammatory effects. In recent years, understanding the glycome to cancer indicates that it can be utilized for both diagnosis/prognosis as well as immunotherapy. Studies involving mass spectrometry of proteome, site- and structure-specific glycoproteomics, or transcriptomics/genomics of patient samples and cancer models revealed the importance of glycosylation homeostasis in cancer biology. The development of emerging technologies, such as the lectin microarray, has facilitated research on the structure and function of glycans and glycosylation. Newly developed devices allow for high-throughput, high-speed, and precise research on aberrant glycosylation. This paper also discusses emerging technologies and clinical applications of glycosylation. [Display omitted] •O- and N-linked glycosylation orchestrate proteoforms and their functions.•Incomplete/neosynthesis of glycan protein lead to immune dysregulation and cancer.•Signaling via PDGF, FGFR, EGFR, MET, RON, or IGFR receptors needs glycosylation.•Multi-omics of tumors reveal heterogeneity in the glycosylation pattern.•Tumor-specific glycans interact with CD43, CD45, selectins, galectins and siglecs.
ISSN:0734-9750
1873-1899
DOI:10.1016/j.biotechadv.2023.108149