Immunochemical detection of oxalate monoalkylamide, an ascorbate-derived Maillard reaction product in the human lens

Carbohydrates with reactive aldehyde and ketone groups can undergo Maillard reactions with proteins to form advanced glycation end products. Oxalate monoalkylamide was identified as one of the advanced glycation end products formed from the Maillard reaction of ascorbate with proteins. In these expe...

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Bibliographic Details
Published in:FEBS letters 1999-06, Vol.453 (3), p.327-330
Main Authors: Nagaraj, Ramanakoppa H., Shamsi, Farrukh A., Huber, Birgit, Pischetsrieder, Monika
Format: Article
Language:English
Subjects:
Adolescent
Adult
Aged
Aged, 80 and over
Aging - physiology
Alkanes - isolation & purification
Amides - isolation & purification
Animals
Antibody Specificity
ASC, ascorbate
Ascorbate degradation
Ascorbic Acid - metabolism
BLP, bovine lens protein
Cataract - etiology
Cattle
Child
Crystallins - chemistry
Crystallins - metabolism
DKG, 2,3-diketogulonate
ELISA, enzyme-linked immunosorbent assay
Glycation End Products, Advanced - biosynthesis
Glycation End Products, Advanced - chemistry
GSH, glutathione
Human lens
Humans
Lens, Crystalline - chemistry
Lens, Crystalline - metabolism
Maillard Reaction
Middle Aged
OMA, oxalate monoalkylamide
Oxalate monoalkylamide
Oxalates - immunology
Oxalates - isolation & purification
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Summary:Carbohydrates with reactive aldehyde and ketone groups can undergo Maillard reactions with proteins to form advanced glycation end products. Oxalate monoalkylamide was identified as one of the advanced glycation end products formed from the Maillard reaction of ascorbate with proteins. In these experiments, we have analyzed human lens proteins immunochemically for the presence of oxalate monoalkylamide. Oxalate monoalkylamide was absent in most of the very young lenses but was present in old and cataractous lenses. The highest levels were found in senile brunescent lenses. Incubation experiments using bovine lens proteins revealed that oxalate monoalkylamide could form from the ascorbate degradation products, 2,3-diketogulonate and L-threose. These data provide the first evidence for oxalate monoalkylamide in vivo and suggest that ascorbate degradation and its binding to proteins are enhanced during lens aging and cataract formation.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(99)00571-2