Age-dependent accumulation of advanced glycosylation end products in human neurons.
Glucose can react nonenzymatically with free amino groups on proteins and form advanced glycosylation end-products (AGEPs), that have been previously isolated and characterised in aging human connective tissues. In this study, we used immunocytochemistry to examine the distribution of AGEPs in the aging human brain. Our findings show that the pyramidal neurons selectively accumulate AGEP-containing vesicles in an age-dependent manner. In addition, our results demonstrate that AGEPs accumulate in the same type of neuron that degenerates in Alzheimer's disease.
Li
J J
JJ
Glaxo Institute for Molecular Biology, Geneva, Switzerland.
Surini
M
M
Catsicas
S
S
Kawashima
E
E
Bouras
C
C
D000293:Adolescent; D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D000375:Aging / Q000378:metabolism*; D000544:Alzheimer Disease / Q000378:metabolism / Q000473:pathology; D015153:Blotting, Western; D001921:Brain / Q000378:metabolism / Q000473:pathology; D002648:Child; D002675:Child, Preschool; D004797:Enzyme-Linked Immunosorbent Assay; D006031:Glycosylation; D006801:Humans; D007124:Immunoenzyme Techniques; D008875:Middle Aged; D009410:Nerve Degeneration / Q000502:physiology; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D016874:Neurofibrillary Tangles / Q000378:metabolism / Q000473:pathology; D017966:Pyramidal Cells / Q000378:metabolism*
D009419:Nerve Tissue Proteins