Poly peptide N-acetylgalactosaminyl transferase-catalyzed substrate glycomes: Analytical methods and strategies
10.13200/j.cnki.cjb.004635
- VernacularTitle:多肽N-乙酰氨基半乳糖转移酶催化底物糖组解析方法与策略的研究进展
- Author:
Lujie FENG
1
Author Information
1. Medical College of Dalian University, Dalian 116622, Liaoning Province, China
- Publication Type:Journal Article
- Keywords:
O-linked N-acetylgalactosamine glycosylation(O-GalNAc);
Poly peptide N-acetylgalactosaminyl transferases(ppGalNAc-Ts);
Analytical methods;
Inhibitor
- From:
Chinese Journal of Biologicals
2026;39(01):108-116
- CountryChina
- Language:Chinese
-
Abstract:
Poly peptide N-acetylgalactosaminyl transferases(ppGalNAc-Ts) serves as the key initiating enzyme for the synthesis of O-linked N-acetylgalactosamine glycosylation(O-GalNAc), also known as mucin-type O-glycosylation. This modification is widely present on the cell membrane proteins and secretory proteins of eukaryotes and is involved in regulating almost all cellular physiological processes, playing a particularly important role in tumorigenesis and development.The diversity of the ppGalNAc-T enzyme family members, the substrate specificity in catalysis, and the high heterogeneity of O-GalNAc glycosylation modifications present challenges in O-glycosylation research. In recent years, significant progress has been made in the study of ppGalNAc-Ts-catalyzed substrate glycomes, driven by the development and application of technologies such as gene editing, mass spectrometry, and bioinformatics. This review summarizes the current research on the analytical methods for ppGalNAc-Ts and their catalyzed substrate glycomes, substrate analysis strategies, and inhibitor development, providing new methods and strategies for elucidating the role of ppGalNAc-Ts in disease progression.
