Glycated Albumin: The Next HgA1c?

April 15, 2015

Albumin -- the most abundant protein in the human body -- has many roles. It transports hormones, fatty acids, and other compounds. It buffers serum pH, and maintains osmotic pressure. Now, it appears that albumin may be a tool that could be used in diabetes management.

Albumin—the most abundant protein in the human body—has many roles. It transports hormones, fatty acids, and other compounds. It buffers serum pH, and maintains osmotic pressure. Now, it appears that albumin may be a tool that could be used in diabetes management.

Researchers have published a description of glycated serum albumin’s potential role as a disease marker in the online version of Diabetes & Metabolic Syndrome.

Glycation—or non-enzymatic glycosylation—binds proteins or lipids with sugar or carbohydrate.

Human serum albumin, by virtue of its ubiquitous presence and ample supply, is the protein most susceptible to non-enzymatic glycation. Albumin’s structural and biological properties change when a carbohydrate is attached to its free amino terminal residues. These changes are irreversible and stable, making the altered molecule an ideal diagnostic marker in diabetes associated complications.

These researchers indicate that glycated albumin levels can determine glycemic control much like the erythrocyte-based HbA1c does. HbA1c, currently the clinical gold standard for assessment of glycemic control, is based on erythrocyte half-life of 28 days and tends to measure mean plasma glucose level. Serum albumin’s half life is 2 weeks, and it reflects short-term control better. It also reflects plasma glucose excursions or postprandial glucose levels better than HbA1c.

In healthy normal individuals, glycated albumin levels range between 1% and 10%. In diabetic patients, they are 2 to 3 fold higher. Ethnic differences in HgA1c have been reported, and the researcher note that the genetic issues that cause these differences do not affect glycated albumin levels.

Although this paper is quite technical in its presentation, it is a comprehensive review of the biochemistry that causes and contributes to diabetes and microvascular complications. The researchers note that accurate measurements of glycated albumin with highly sensitive techniques are in the development stage and have serious implications for management of diabetes.

Finally, glycated albumin’s special qualities offer hope that it can be used not only as a diagnostic tool, but also as an assessment tool for diabetes-associated complications. Tacking a carbohydrate residue to human serum albumin has been associated with some of diabetes’ most troublesome pathological events. These include diabetic nephropathy, neuropathy, retinopathy and cardiovascular complications.


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