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Pathophysiologic Significance

  • Chapter
Diabetes and Protein Glycosylation

Abstract

The amino-terminal of the P chain of hemoglobin, to which glucose attaches, is also a site where organic phosphates bind. 2,3-Diphos- phoglycerate (2,3-DPG), an important intermediate in red cell glycolysis, influences the affinity of hemoglobin for oxygen through its ability to bind to β chain residues of deoxyhemoglobin. Addition of organic phosphate decreases the oxygen affinity of hemoglobin, whereas removal of organic phosphate increases the oxygen affinities of Hb A and Hb A1c. The availability of this site for interaction with 2,3-DPG is compromised when it is covalently linked to glucose.1 Hence, Hb A1c exhibits greater oxygen affinity than Hb A in the presence of 2,3-DPG.2–4 Correspondent with the increase in the level of Hb A1c in the red cells of diabetic patients, the oxygen affinity of these cells in the presence of 2,3-DPG is slightly greater than that of red cells from nondiabetic subjects.5 This difference could be explained on the basis of the interference presented by the NH2-terminal glucose of Hb A1c to the binding of 2,3-DPG.

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  1. Division of Endocrinology and Metabolism, University of Medicine and Denstistry of New Jersey, 07103, Newark, New Jersey, USA

    Margo Panush Cohen (Professor of Medicine and Chair)

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Cohen, M.P. (1986). Pathophysiologic Significance. In: Diabetes and Protein Glycosylation. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-4938-2_5

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  • DOI: https://doi.org/10.1007/978-1-4612-4938-2_5

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