Glycated albumin: an overview of the In Vitro models of an In Vivo potential disease marker

Abstract

Glycation is a general spontaneous process in proteins which has significant impact on their physical and functional properties. These changes in protein properties could be related to several pathological consequences such as cataract, arteriosclerosis and Alzheimer’s disease. Among the proteins, glycation of Human serum albumin (HSA) is of special interest. Human serum albumin is the most abundant protein in the plasma and because of its high sensitivity for glycation, undergoes structural and functional changes due to binding of reducing sugars in vitro. The glycation process occurs by plasma glucose in vivo which has great impacts on the three dimensional structure of protein. These changes are efficient and stable enough which makes the protein to be considered as a new special disease marker instead of HbA1C for diabetes. In some cases, glycated albumin was used as an alternative marker for glycemic control. Glycated albumin reacts with glucose ten times more rapidly than HbA1C and has shorter half-life which makes it more reliable for indicating glycemic states. In this review, glycation of Human Serum Albumin has been overviewed, starting from overall concepts of glycation, followed by some Examples of pathological consequences of protein glycation. The BSA aggregation was reviewed in terms of structural and biological impacts of glycation on the protein followed by reporting documents which indicate possibility of glycated albumin to be used as specific marker for diabetes. Finally, some of the studies related to the models of glycated albumin have been briefly described, with an emphasis on In vitro studies. It is interesting to note the relationship found between in vitro glycation experiments and the propensity of proteins to form amyloid structures, a point that could be further explored as to its significance in hyperglycemic states.

Data-analytically derived flexible HbA1c thresholds for type 2 diabetes mellitus diagnostic

“…This is partially explained by the relatively small size of this protein, so that produced in large quantities it helps to maintain the plasma osmotic pressure, as reviewed. [61] The homeostasis otherwise requires that the excessive glucose was flushed out, which is indeed what is observed in DM and for what it gets its name -siphoning out of the sweet. Hence, albumin is BP regulator in DM.…”

“…Methods are also available for the quantification of glycated albumin specifically." Albumin is particularly attractive for its deemed high potential as a marker for DM: [1,61] it has a shorter half-life (21 days) compared with haemoglobin, so it could be used as a shorter-term glycaemic control; it is not easily altered by an abnormal haemoglobin metabolism; the amount of non-enzymatic glycation of albumin is nine times more than in the case of HbA1c; glycation of albumin is ten times faster than of haemoglobin.…”

Glycated albumin: a potential biomarker in diabetes

“…NF-κB modulates the gene transcription of pro-inflammatory molecules such as interleukins 1, 6 and 8 and tumor necrosis factor-α, and also the vascular cell adhesion molecule-1 and intercellular adhesion molecule-1 (26). As a consequence of this cascade, there is an increased production of reactive oxygen species, which is directly associated with the pathogenesis and longterm complications in DM (21,27). Kisugi and cols.…”

“…Similar to the other proteins, albumin also goes through the physiologic process of glycation (21). By definition, glycation is a non-enzymatic spontaneous reaction in which a reducing sugar is added to a free amino group, typically lysine or arginine present within proteins, also called as Maillard reaction (Figure 1) (18)(19)(20).…”

Is HbA1c the only choice? Alternative biomarkers for glycaemic control assessment

“…The result is calculated based on the GA/albumin ratio. Glycation reduces the albumin antioxidative properties and its bonding abilities, which can have a negative effect on blood concentrations of medicaments in use [30]. A rise in GA concentration and advanced glycation end products alike affects the change of cell signal transduction pathways, activating inflammatory mediators and contributing to development of late diabetic complications.…”