Glycosylation Heterogeneity of α1-Acid Glycoprotein: Disease-Associated Glycoform Remodeling, Regulatory Mechanisms, and Clinical Translation
- 1College of Basic Medical Sciences, Dalian Medical University, 9-Western Section, Lvshun South Road, Dalian 116044, China
Abstract
α1-Acid glycoprotein (AGP) is a heavily glycosylated acute-phase protein whose N-linked glycan microheterogeneity plays an important regulatory role in pathophysiological processes. This review synthesizes decades of basic and clinical research, focusing on the five conserved N-glycosylation sites of AGP. Specifically, it summarizes disease-specific patterns of glycan remodeling in inflammation, cancer, and autoimmune diseases; discusses the molecular effects through which glycosylation modulates AGP conformation, receptor-binding properties, and downstream signaling pathways; examines disease-associated molecular fingerprints arising from site-specific glycosylation and their relationships with disease onset and progression; and highlights the translational potential of AGP glycosylation for early diagnosis, prognostic assessment, and targeted drug development. Current evidence indicates that most abnormalities in AGP glycosylation are associated with disease, whereas direct causal evidence for the involvement of glycosylation in disease progression remains incomplete. Important limitations also remain: the precise molecular mechanisms regulating AGP glycosylation under different pathological conditions have not been fully elucidated; experimental findings are inconsistent across cohorts and analytical platforms; and standardized analytical systems suitable for clinical application have yet to be established. By integrating the available evidence, this review provides a theoretical framework for advancing the translation of AGP glycosylation features into precision medicine.
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BibTeX
@article{liu2026glycosylation,
title = {{Glycosylation Heterogeneity of α1-Acid Glycoprotein: Disease-Associated Glycoform Remodeling, Regulatory Mechanisms, and Clinical Translation}},
author = {Gang Liu and Ning Fan and Yating Wang and Weijie Dong},
journal = {Biomolecules},
year = {2026},
month = oct,
doi = {10.3390/biom16101419},
url = {https://www.mdpi.com/2218-273X/16/10/1419},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Glycosylation Heterogeneity of α1-Acid Glycoprotein: Disease-Associated Glycoform Remodeling, Regulatory Mechanisms, and Clinical Translation
AU - Gang Liu
AU - Ning Fan
AU - Yating Wang
AU - Weijie Dong
PY - 2026
DA - 2026/10/01
JO - Biomolecules
DO - 10.3390/biom16101419
UR - https://www.mdpi.com/2218-273X/16/10/1419
AB - α1-Acid glycoprotein (AGP) is a heavily glycosylated acute-phase protein whose N-linked glycan microheterogeneity plays an important regulatory role in pathophysiological processes. This review synthesizes decades of basic and clinical research, focusing on the five conserved N-glycosylation sites of AGP. Specifically, it summarizes disease-specific patterns of glycan remodeling in inflammation, cancer, and autoimmune diseases; discusses the molecular effects through which glycosylation modulates AGP conformation, receptor-binding properties, and downstream signaling pathways; examines disease-associated molecular fingerprints arising from site-specific glycosylation and their relationships with disease onset and progression; and highlights the translational potential of AGP glycosylation for early diagnosis, prognostic assessment, and targeted drug development. Current evidence indicates that most abnormalities in AGP glycosylation are associated with disease, whereas direct causal evidence for the involvement of glycosylation in disease progression remains incomplete. Important limitations also remain: the precise molecular mechanisms regulating AGP glycosylation under different pathological conditions have not been fully elucidated; experimental findings are inconsistent across cohorts and analytical platforms; and standardized analytical systems suitable for clinical application have yet to be established. By integrating the available evidence, this review provides a theoretical framework for advancing the translation of AGP glycosylation features into precision medicine.
SN - 2218-273X
ER -