[Glycoxidative modification of albumin in medical research]

Human albumin is a major, multi-functional serum protein. As the other protein is subjected to many modifications, including glycation and oxidation, which occurs physiologically in low intensity, however, are significantly increased in various pathological conditions. They often co-occur with each other, reinforcing its negative effects, and therefore are referred to common name - glycoxidative processes. Glycation, increased especially in diabetes, causes structural and functional changes of many proteins, both short-and long-lived, and it may result in increased oxidative stress and protein oxidation, which secondarily may increase their susceptibility to glycation. Studies in vivo and in vitro processes of oxidation and glycation of albumin and other proteins allowed us to identify biochemical markers that are routinely used in the diagnosis and monitoring of diseases (ischemia modified albumin, fructosamine) and those commonly used in research (e.g. AGE, CML, SH and CO groups, AOPP), which in perspective could be used in clinical trials (especially AGEs and AOPP). The study presents current state of knowledge on the mechanisms, the importance and the possibility of using glycoxidative modified albumin in medical science.