Distribution of advanced glycation end products in the cerebellar neurons of dogs.
Nonenzymatically glycated proteins and their advanced stage, the 'advanced glycation end products' (AGEs), have been detected in long-lived proteins and protein deposits in human and animal tissues. They are thought to be associated with normal aging and particularly with the pathogenesis of diabetic complications and Alzheimer's disease. AGEs accumulate in human neurons in an age-dependent manner and, in Alzheimer's disease patients, particularly in amyloid plaques and neurofibrillary tangles. In this study, we demonstrate AGE immunoreactivity in the canine brain, particularly in cerebellar Purkinje cells and brainstem neurons. In addition, distinct AGE-positive granules can be detected in the Purkinje cells which accumulate in an age-dependent manner. Staining with PAS and oil-red suggests that these AGE-positive granules contain the protein, but not the lipid constituents associated with lipofuscin. Our results show that the pattern of AGE distribution in the canine cerebellum resembles the situation in the human brain, but that the time course of AGE formation is much faster in dogs reflecting their much shorter life span.
Weber
K
K
Institut für Pathologie, GSF München, Neuherberg, D85758 Oberschleissheim, Germany.
Schmahl
W
W
Münch
G
G
D000818:Animals; D001933:Brain Stem / Q000166:cytology / Q000378:metabolism*; D002531:Cerebellum / Q000166:cytology / Q000378:metabolism*; D004285:Dogs; D004827:Epilepsy / Q000378:metabolism / Q000473:pathology; D017127:Glycation End Products, Advanced / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D009474:Neurons / Q000378:metabolism*; D012016:Reference Values; D013194:Staining and Labeling
D017127:Glycation End Products, Advanced; D009419:Nerve Tissue Proteins