T. Oya et al., A NOVEL BIOMARKER FOR HYPERGLYCEMIA, MRX ISOLATED FROM HYDROLYSATE OFGLYCATED PROTEINS, Biochemical and biophysical research communications, 246(1), 1998, pp. 267-271
Long-lived proteins can undergo non-enzymatic glycation to form highly
crosslinked structures with characteristic fluorescence during aging
and diabetes processes. In this paper, a typical fluorophore, named Ma
illard reaction product X (MRX), was isolated from the hydrolysate of
glycated proteins. MRX could be formed by incubation of bovine serum a
lbumin with glucose, followed by acid hydrolysis. The structure of MRX
was determined to be ihydrothiazolo[3,2-alpha]pyridinium-3-carboxylat
e. MRX was also found to be formed by the incubation of cysteine and a
rginine with glucose, followed by hydrolysis. We found the formation o
f MRX in the recently developed genetically diabetic Otsuka Long-Evans
Tokushima Fatty (OLETF) rats and compared them with that in the contr
ol Long-Evans Tokushima Otsuka (LETO) rats. Significantly higher level
s of MRX were observed from the serum (p < 0.005) and urinary protein
(p < 0.001) of OLETF rats in comparison with those of LETO rats. MRX m
ust be a potential candidate as a biomarker for hyperglycemia. (C) 199
8 Academic Press.