Comparison of glycation degrees of HbG-Coushatta and HbG-Taipei with HbA using liquid chromatography with tandem mass spectrometry.

Background: Hemoglobin A _1c (HbA _1c ) is widely used to measure glycemic status and control in diabetes testing and treatment and is an important risk factor forcomplications of diabetes. Hemoglobin variants can interfere with the HbA _1c testing method by reducing the life span of erythrocytes or due to differences in glycation degrees. In this study, glycation levels of the HbA, HbG-Coushatta, and HbG-Taipei β-chains (βA, βG-Coushatta, and βG-Taipei, respectively) were examined.
Methods: Blood samples from heterozygotic patients (HbG-Coushatta/HbA, HbG-Taipei/HbA) were analyzed. Glycation rateswere determined using high-performance liquid chromatography with tandem mass spectrometry. Ratios of glycated βG-Coushatta to glycated βA and glycated βG-Taipei to glycated βA were calculated by comparingareas under the curves from extracted ion chromatograms.
Results: βG-Coushatta and βG-Taipei were 6.08 ± 1.38% and 5.95 ± 0.93% glycated (respectively), which were significantly higher than βA chains(4.55 ± 1.30% and 4.51 ± 0.91%, respectively; p = 0.000). The total glycation degree (α + β) in HbG-Coushatta and HbG-Taipei heterozygotes were estimated to be 9% and 8% higher than those of HbA homozygotes (P＜0.001), respectively.
Conclusion: βG-Coushatta and βG-Taipei glycation degrees were significantly higher than βA, while the differences in total hemoglobin (α + β) were small and unlikely to impact the clinical interpretation of HbA _1c results.
(Copyright © 2021. Published by Elsevier B.V.)