Efforts have been made to estimate values similar to A1C levels, 40–45 however, clinical targets continue to be unclear. 38, 39Īn important limitation to the use of glycated proteins is the lack of established clinical cut points, standardization, and data on frequency of measurements in clinical practice. 37įA concentrations are more likely to be influenced by the concentrations of protein and low-molecular-weight substances coexisting in the blood (e.g., bilirubin, uric acid), 31 while GA reflects the proportion of GA to total serum albumin, expressed by a ratio (%), as a result, the changes in serum protein concentration have less of an impact on GA than in FA. GA is set lower in relation to plasma glucose levels in smokers, 33 hyperuricemia patients, 34 hypertriglyceridemia, 35 and men with nonalcoholic fatty liver disease (NAFLD), 36 the latter perhaps secondary to chronic microinflammation, where increase in albumin catabolism, particularly in obese subjects, shortens the half-life of albumin, decreasing glycated proteins relative to plasma glucose levels. 32 However, as the synthetic function of the liver declines with worsening cirrhosis, albumin levels fall, and therefore in liver failure as albumin goes lower, glycated proteins will also decrease. Glycated proteins present with higher values relative to plasma glucose levels in patients with liver cirrhosis, and attributed to a couple of mechanisms, (1) prolonged half-life of serum albumin originating from reduced capacities of albumin synthesis in vivo 30 and (2) increased immunoglobulin production in patients with cirrhosis, 31 (globulins tend to increase in patients with cirrhosis and hepatitis, thought to be secondary to shunting of bacterial antigens in portal venous blood away from the liver to lymphoid tissue, which induces immunoglobulin production). 29Īs the glycation rate depends on turnover of the protein of interest, any condition affecting its half-life will in turn influence the value independent of glucose control ( Table 1). 28 Other scenarios of their utility include the evaluation of earlier response to treatment changes or in pregnancy complicated by diabetes. Their glycation rate is unaffected by RBC life span and therefore used in conditions in which A1C may not be a reliable marker, such as in hemodialysis patients, in whom several studies have shown superiority compared to A1C 25–27 and in whom both elevated FA and GA are risk factors for cardiovascular (CV) events, all-cause and CV mortality, independent of other confounding variables. 13, 23, 24įA and GA are extracellular proteins that provide an index of average glucose over a period of 2–3 weeks, their average half-life, thus proposed as intermediate markers of glucose control. 22 Several prospective studies have shown their utility for patients at risk of developing micro- and macrovascular complications. Glycated proteins have been associated with micro- 13–15 and macrovascular complications 16–21 and mortality in people with DM. FA refers to several proteins, with albumin accounting for ∼90% GA refers exclusively to albumin. Glycated proteins are serum proteins that have permanently changed their composition when chronically exposed to glucose and turned into irreversible ketamines. In addition to hemoglobin, other proteins can become glycated.
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