Modification of amino acid residues in carious dentin matrix.
J Dent Res
; 77(3): 488-95, 1998 Mar.
Article
em En
| MEDLINE
| ID: mdl-9496922
ABSTRACT
The Maillard reaction between sugar and protein has been postulated as the cause for the browning and arrestment of caries lesions. This reaction has been implicated as the cause for decreased degradability of collagen in vivo. The aim of the present study was to verify the occurrence of the reaction in vivo. Carious and sound dentin samples were taken from extracted human teeth and analyzed for the fluorescence characteristic of the Maillard reaction and oxidation and, by HPLC, for Maillard products. In addition, physiological cross-links were analyzed by HPLC. Oxidation- and Maillard reaction-related fluorescence increased in collagenase digests from carious dentin. Advanced Maillard products (carboxymethyllysine and pentosidine) increased, whereas furosine, a marker for the initial reaction, was not observed consistently. This implies no direct addition of sugars to protein, but rather the addi-tion of smaller metabolites and glycoxidation products. In addition, the physiological cross-links hydroxylysinonorleucine and dihydroxylysinonorleucine decreased in carious dentin. Also for hydroxylysylpyridinoline, a decrease was observed, but not consistently. In conclusion, the caries process modifies amino acids in dentin collagen, which can lead to increased resistance against proteolysis and ultimately to caries arrestment.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Produtos Finais de Glicação Avançada
/
Cárie Dentária
/
Dentina
Limite:
Humans
Idioma:
En
Revista:
J Dent Res
Ano de publicação:
1998
Tipo de documento:
Article
País de afiliação:
Holanda