Discordance between blood glucose and HbA1c – is an explanation possible according to the biokinetic model of glycation?

Czech version

Authors: Oliver Rácz ¹; Peter Dombrovský ¹; Vladimír Heriban ²; Marek Brenišin ¹; Katarína Muriová ³
Authors‘ workplace: Ústav patologickej fyziológie LF UPJŠ v Košiciach ¹; Všeobecná zdravotná poisťovňa, a. s., Bratislava ²; Nemocnica Poprad, a. s., Poprad ³
Published in: Diab Obez 2021; 21(41): 16-22
Category: Reviews

Overview

According to the biokinetic model of hemoglobin glycation, hyperglycemic episodes occured recently have a greater impact on HbA_1c levels as compared with those occured long ago. In the first part of this paper there are theoretical calculations of HbA_1c for stable blood glucose concentrations and for hyperglycemic episodes lasting 24 and 60 days occuring in different time before HbA_1c measurement. The second part is devoted to analysis of discordance between blood glucose values and HbA_1c assessed as glycation gap and glycation index in 158 patients with diabetes mellitus. The differences of HbA_1c calculated according to the biokinetic model and timing of hyperglycemic episodes can probably explain the discordance between blood glucose values and HbA_1c.

Keywords:

biokinetic model – diabetes mellitus – glycation index – glycation gap – HbA1c

Sources

Rácz O, Futáš E, Kuzmová D, Reiter et al. Význam matematického modelu glykácie hemoglobínu pre diabetologickú prax. In: Zborník súhrnov IX. patofyziologického kongresu. Košice 1987: 27.
Rácz O, Vícha T, Pačin J. Glykohemoglobín, glykácia bielkovín a diabetes mellitus. Osveta: Martin 1989. ISBN 80–217–0072–6.
Campbell L, Pepper T, Shipman K. HbA_1c: a review of non-glycaemic variables. J Clin Pathol 2019; 72(1): 12–19. Dostupné z DOI: <http://dx.doi.org/10.1136/jclinpath-2017–204755>.
Soros AA, Chalew SA, McCarter RJ et al. Hemoglobin glycation index: a robust measure of hemoglobin A1c in pediatric type 1 diabetes patients. Pediatric Diabetes 2010; 11(7): 455–461. Dostupné z DOI: <http://dx.doi.org/10.1111/j.1399–5448.2009.00630.x>.
Rodriguez-Segade S, Rodríguez J, García Lopez JM et al. Estimation of the glycation gap in diabetic patients with stable glycemic control Diabetes Care 2012; 35(12): 2447–2450. Dostupné z DOI: <http://dx.doi.org/10.2337/dc11–2450>.
van Steen SC, Schrieks IC, Hoekstra JB et al. The haemoglobin glycation index as predictor of diabetes-related complications in the AleCardio trial. Prevent Cardiol 2017; 24(8): 858–866. Dostupné z DOI: <http://dx.doi.org/10.1177/2047487317692664>.
Hempe JM, Liu S, Myers L et al. The hemoglobin glycation index identifies subpopulations with harms or benefits from intensive treatment in the ACCORD trial. Diabetes Care 2015; 38(6): 1067–1074. Dostupné z DOI: <http://dx.doi.org/10.2337/dc14–1844>.
Feng L, Nian S, Zhao Y et al. Higher HbA_1c and/or glucose levels alter the association patterns between glycated hemoglobin and fasting glucose levels. Diab Res Clin Pract 2018; 142: 353–362. Dostupné z DOI: <http://dx.doi.org/10.1016/j.diabres.2018.06.011>.
Nayak AU, Singh BM, Dunmore SJ. Potential clinical error arising from use of HbA_1c in diabetes: effects of the glycation gap. Endocrine Rev 2019; 40(4): 988–999. Dostupné z DOI: <http://dx.doi.org/10.1210/er.2018–00284>.
Beach KW. A theoretical model to predict the behaviour of glycosylated hemoglobin levels. J Theor Biol 1979; 81(3): 547–561. Dostupné z DOI: <http://dx.doi.org/10.1016/0022–5193(79)90052–3>.
Mortensen HB, Volund A. Application of a biokinetic model for prediction and assessment of glycated hemoglobins in diabetic patients. Scand J Clin Lab Invest 1988; 48(6): 595–602. Dostupné z DOI: <http://dx.doi.org/10.3109/00365518809085778>.
Ladyzynski P, Wójcicki JM, Bak M et al. Validation of hemoglobin glycation models using glycemia monitoring in vivo and culturing of erythrocytes in vitro. Ann Biomed Eng 2008; 36(7): 1188–1202. Dostupné z DOI: <http://dx.doi.org/10.1007/s10439–008–9508-x>.
Ladyzynski P, Wójcicki JM, Bak M et al. Hemoglobin glycation rate constant in non-diabetic individuals. Ann Biomed Eng 2011; 39(11):2721–34. Dostupné z DOI: >http://dx.doi.org/10.1007/s10439–011–0366–6>.
Ladyzynski P, Foltyński P, Sabalińska S et al. An analysis of the hemoglobin glycation rate in the A1C-derived average glucose study population applying a Monte Carlo method. In: 6th European Conference of the International Federation for Medical and Biological Engineering. IFMBE Proceedings book series (IFMBE) 2015; 45: 435–438. Dostupné z DOI: <https://doi.org/10.1007/978–3-319–11128–5_109>.
Advani A. Positioning time in range in diabetes management. Diabetologia 2020; 63(2): 242–252. Dostupné z DOI: <http://dx.doi.org/10.1007/s00125–019–05027–0>.
Virtue MA, Furne JK, Nuttall FQ et al. Relationship between GHb concentration and erythrocyte survival determined from breath carbon monoxide concentration. Diab Care 2004; 27(4): 931–935. Dostupné z DOI: <http://dx.doi.org/10.2337/diacare.27.4.931>.
Cohen RM, Franco RS, Joiner CH. Is poor glycemic control associated with reduced red blood cell lifespan? Diabetes Care 2004; 27: 1013–1014. Dostupné z DOI: <http://dx.doi.org/10.2337/diacare.27.4.1013>.
Cohen RM, Franco RS, Khera PK et al. Red cell life span heterogeneity in hematologically normal people is sufficient to alter HbA_1c. Blood 2008; 112(10): 4284–4291. Dostupné z DOI: <http://dx.doi.org/10.1182/blood-2008–04–154112>.
Willekens FL, Roerdinkholder-Stoelwinder YA, Groenen-Döpp HJ et al. Hemoglobin loss from erythrocytes in vivo results from spleen facilitated vesiculation. Blood 2003; 101(2): 747–751. Dostupné z DOI: <http://dx.doi.org/10.1182/blood-2002–02–0500>.
Delpierre GD, Vertommen D, Communi MH et al. Identification of fructosamine residues deglycated by fructosamine-3-kinase in human hemoglobin. J Biol Chem 2004; 279(26): 27613–27620. Dostupné z DOI: <http://dx.doi.org/10.1074/jbc.M402091200>.
Dunmore SJ, Al-Derawi AS, Nayak AU et al. Evidence that differences in fructosamine-3-kinase activity may be associated with the glycation gap in human diabetes. Diabetes 2018; 67(1): 131–136. Dostupné z DOI: <http://dx.doi.org/10.2337/db17–0441>.