Studies from University of Naples further understanding of Down syndrome in children

A new study, 'Accumulation of altered aspartyl residues in erythrocyte proteins from patients with Down's syndrome,' is now available. "Spontaneous protein deamidation of labile Asn residues, generating L-isoaspartates and D-aspartates, is associated with cell aging and is enhanced by an oxidative microenvironment; to minimize the damage, the isoaspartate residues can be 'repaired' by a specific L-isoaspartate (D-aspartate) protein O-methyltransferase (PIMT). As both premature aging and chronic oxidative stress are typical features of Down's syndrome (DS), we tested the hypothesis that deamidated proteins may build up in trisomic patients," scientists in Italy report.

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