Alzheimer's disease and amyloid β-peptide deposition in the brain: a matter of 'aging'?
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Alzheimer's disease and amyloid β-peptide deposition in the brain : a matter of 'aging'? / Moro, Maria Luisa; Collins, Matthew J.; Cappellini, Enrico.
In: Biochemical Society Transactions, Vol. 38, No. 2, 2010, p. 539-544.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Alzheimer's disease and amyloid β-peptide deposition in the brain
T2 - a matter of 'aging'?
AU - Moro, Maria Luisa
AU - Collins, Matthew J.
AU - Cappellini, Enrico
PY - 2010
Y1 - 2010
N2 - Biomolecules can experience aging processes that limit their long-term functionality in organisms. Typical markers of protein aging are spontaneous chemical modifications, such as AAR (amino acid racemization) and AAI (amino acid isomerization), mainly involving aspartate and asparagine residues. Since these modifications may affect folding and turnover, they reduce protein functionality over time and may be linked to pathological conditions. The present mini-review describes evidence of AAR and AAI involvement in the misfolding and brain accumulation of Abeta (amyloid beta-peptide), a central event in AD (Alzheimer's disease) synaptic dysfunctions. Structural alterations introduced by site-specific modifications linked to protein aging may affect Abeta production, polymerization and clearance, and therefore play a pivotal role in the pathogenesis of sporadic and genetic forms of AD. Early changes associated with molecular aging also have significant long-term consequences for Abeta folding and turnover. New fast, reproducible and accurate methods for the screening of protein aging markers in biological samples may contribute to improve diagnostic and therapeutic approaches in AD.
AB - Biomolecules can experience aging processes that limit their long-term functionality in organisms. Typical markers of protein aging are spontaneous chemical modifications, such as AAR (amino acid racemization) and AAI (amino acid isomerization), mainly involving aspartate and asparagine residues. Since these modifications may affect folding and turnover, they reduce protein functionality over time and may be linked to pathological conditions. The present mini-review describes evidence of AAR and AAI involvement in the misfolding and brain accumulation of Abeta (amyloid beta-peptide), a central event in AD (Alzheimer's disease) synaptic dysfunctions. Structural alterations introduced by site-specific modifications linked to protein aging may affect Abeta production, polymerization and clearance, and therefore play a pivotal role in the pathogenesis of sporadic and genetic forms of AD. Early changes associated with molecular aging also have significant long-term consequences for Abeta folding and turnover. New fast, reproducible and accurate methods for the screening of protein aging markers in biological samples may contribute to improve diagnostic and therapeutic approaches in AD.
KW - Aging
KW - Alzheimer Disease
KW - Amino Acid Isomerases
KW - Amyloid beta-Peptides
KW - Animals
KW - Biological Clocks
KW - Brain
KW - Humans
KW - Models, Biological
KW - Protein Processing, Post-Translational
KW - Time Factors
U2 - 10.1042/BST0380539
DO - 10.1042/BST0380539
M3 - Journal article
C2 - 20298218
VL - 38
SP - 539
EP - 544
JO - Biochemical Society Transactions
JF - Biochemical Society Transactions
SN - 0300-5127
IS - 2
ER -
ID: 36094150