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Research progress in the role and mechanism of GALNT3 in human diseases (Review).

Biomedical reports 2026 Vol.24(5) p. 64 🔓 OA Cell Adhesion Molecules Research
OpenAlex 토픽 · Cell Adhesion Molecules Research Glycosylation and Glycoproteins Research Complement system in diseases

Su L, Lin Y, Hu X, Liu Z

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Protein glycosylation is a crucial post-translational modification.

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APA Linhong Su, Yongxiu Lin, et al. (2026). Research progress in the role and mechanism of GALNT3 in human diseases (Review).. Biomedical reports, 24(5), 64. https://doi.org/10.3892/br.2026.2137
MLA Linhong Su, et al.. "Research progress in the role and mechanism of GALNT3 in human diseases (Review).." Biomedical reports, vol. 24, no. 5, 2026, pp. 64.
PMID 41993969

Abstract

Protein glycosylation is a crucial post-translational modification. Polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3) is a glycosyltransferase that plays an essential role in various human diseases by modifying proteins, including fibroblast growth factor 23 and mucins. In non-tumor conditions, mutations in GALNT3 result in hyperphosphatemia in familial tumoral calcinosis, and its dysregulation has been linked to coronary artery disease. Notably, GALNT3 plays a seemingly opposing role in influenza A virus infection by potentially aiding early viral replication, and later exerting antiviral effects. In cancer, the functions of GALNT3 vary by context: it acts as a tumor suppressor in lung cancer but promotes tumor progression in colorectal and ovarian cancer. GALNT3 plays a context-dependent, dual role by exerting both tumor-suppressive and tumor-promoting functions in specific subtypes of pancreatic and breast cancers. This duality is influenced by the tissue environment, substrate specificity, and regulatory networks. Therefore, GALNT3 is emerging as a promising biomarker and therapeutic target across different pathological conditions owing to its pivotal role in disease processes.

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