NMR-Based Quantification of GlycA and GlycB: Advancing Inflammatory Biomarkers in Clinical Diagnostics.

Methods Mol Biol

Precision Medicine & Metabolism, CIC bioGUNE, CIBERehd, BRTA, Bizkaia Technology Park, Derio, Spain.

Published: August 2025


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Article Abstract

GlycA and GlycB are composite proton H-NMR signals arising from the N-acetyl moieties of circulating acute-phase glycoproteins, chiefly α-acid glycoprotein, α-antichymotrypsin, haptoglobin, α1-antitrypsin, and transferrin. These signals have emerged as promising, noninvasive biomarkers of systemic inflammation and disease risk in a variety of clinical settings. Their quantification typically involves advanced NMR pulse sequences that enhance the separation of GlycA and GlycB from overlapping resonances and other interfering signals. Techniques such as CPMG (Carr-Purcell-Meiboom-Gill) spin-echo sequences are frequently used to suppress broad macromolecular backgrounds, while more specialized methods like DIfferential Relaxation (DIRE) and J-Edited Differential (JEDI) further refine the measurement of subtle spectral features. Elevated GlycA and GlycB levels have been linked to several inflammatory and cardiometabolic conditions, including cardiovascular disease, type 2 diabetes, rheumatoid arthritis, and obesity-related disorders. As their clinical utility continues to expand, standardized NMR-based protocols for GlycA and GlycB quantification offer a robust platform for identifying at-risk patients and monitoring disease progression or therapeutic efficacy.

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http://dx.doi.org/10.1007/978-1-0716-4722-6_9DOI Listing

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GlycA and GlycB are composite proton H-NMR signals arising from the N-acetyl moieties of circulating acute-phase glycoproteins, chiefly α-acid glycoprotein, α-antichymotrypsin, haptoglobin, α1-antitrypsin, and transferrin. These signals have emerged as promising, noninvasive biomarkers of systemic inflammation and disease risk in a variety of clinical settings. Their quantification typically involves advanced NMR pulse sequences that enhance the separation of GlycA and GlycB from overlapping resonances and other interfering signals.

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