Immunochemical detection of advanced glycosylation end products in vivo
Reducing sugars react with protein amino groups to form a diverse group of protein-bound moieties with fluorescent and cross-linking properties. These compounds, called advanced glycosylation end products (AGEs), have been implicated in the structural and functional alterations of proteins that occu...
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Published in | The Journal of biological chemistry Vol. 267; no. 8; pp. 5133 - 5138 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Bethesda, MD
American Society for Biochemistry and Molecular Biology
15.03.1992
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Subjects | |
Online Access | Get full text |
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Summary: | Reducing sugars react with protein amino groups to form a diverse group of protein-bound moieties with fluorescent and cross-linking
properties. These compounds, called advanced glycosylation end products (AGEs), have been implicated in the structural and
functional alterations of proteins that occur during aging and long-term diabetes. Although several AGEs have been identified
on the basis of de novo synthesis and tissue isolation procedures, the measurement of AGE compounds in vivo has remained difficult.
As an approach to the study of AGE formation in vivo, we prepared polyclonal antiserum to an AGE epitope(s) which forms in
vitro after incubation of glucose with ribonuclease (RNase). This antiserum proved suitable for the detection of AGEs which
form in vivo. Both diabetic tissue and serum known to contain elevated levels of AGEs readily competed for antibody binding.
Cross-reactivity studies revealed the presence of a common AGE epitope(s) which forms after the incubation of diverse proteins
with glucose. Cross-reactive epitopes also formed with glucose 6-phosphate or fructose. These data suggest that tissue AGEs
which form in vivo appear to contain a common immunological epitope which cross-reacts with AGEs prepared in vitro, supporting
the concept that immunologically similar AGE structures form from the incubation of sugars with different proteins (Horiuchi,
S., Araki, N., and Morino, Y. (1991) J. Biol. Chem. 266, 7329-7332). None of the known AGEs, such as 4-furanyl-2-furoyl-1H-imidazole,
1-alkyl-2-formyl-3,4-diglycosylpyrrole, pyrraline, carboxymethyllysine, or pentosidine, were found to compete for binding
to anti-AGE antibody. These data further suggest that the dominant AGE epitope which forms from the reaction of glucose with
proteins under native conditions is immunologically distinct from the structurally defined AGEs described to date. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(18)42741-X |