K. Ando et al., Membrane proteins of human erythrocytes are modified by advanced glycationend products during aging in the circulation, BIOC BIOP R, 258(1), 1999, pp. 123-127
Citations number
46
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Recent immunological studies demonstrated that proteins in vivo in several
diseases are subjected to post-translational modification by advanced glyca
tion end products (AGrEs), suggesting a potential role of AGEs in aging and
age-enhanced disease processes such as diabetic complications, atheroscler
osis and Alzheimer's disease. N-epsilon-(Carboxymethyl)lysine (CML) is one
of the major AGE-structures demonstrated in vivo so far. In the present stu
dy, membrane proteins from young erythrocyte population mere compared with
those from senescent erythrocytes separated from the same individual in the
ir CML-contents using a monoclonal antibody for CML (6D12). SDS-polyacrylam
ide gel electrophoresis and subsequent Western blot showed that 6D12 bound
to the band 1, 2, 3, 4.2, 5, 6 and 7 proteins from senescent erythrocytes,
but not to those from young erythrocyte. Furthermore, quantitative estimati
on of the reactivity of 6D12 to these erythrocyte membranes by ELISA showed
that the reactivity of 6D12 to senescent erythrocyte membranes was 3- to 6
-fold higher than that of young erythrocyte membranes. These results indica
te that membrane proteins of circulating erythrocytes undergo CML-modificat
ion, and the modified proteins accumulated in an age-dependent manner durin
g the life span of erythrocytes. (C) 1999 Academic Press.