[Glycation and protein crosslinking in the diabetes and ageing pathogenesis].

Long exposition to hyperglycemia is associated with development of vascular diseases in diabetic patients. Many of these effects are mediated by non-enzymatic glycosylation (glycation) of proteins and formation of advanced glycation end-products (AGEs). This phenomenon is accelerated in conditions where glucose concentration is chronically high, as it happens in diabetes mellitus.

Glycation does not modify bovine serum albumin (BSA)-induced reduction of rat aortic relaxation: the response to glycated and nonglycated BSA is lost in metabolic syndrome.

The effects of nonglycated bovine serum albumin (BSA) and advanced glycosylation end products of BSA (AGE-BSA) on vascular responses of control and metabolic syndrome (MS) rats characterized by hypertriglyceridemia, hypertension, hyperinsulinemia, and insulin resistance were studied. Albumin and in vitro prepared AGE-BSA have vascular effects; however, recent studies indicate that some effects of in vitro prepared AGEs are due to the conditions in which they were generated. We produced AGEs by incubating glucose with BSA for 60 days under sterile conditions in darkness and at 37 degrees C.