Advanced glycosylation end-products and heat shock proteins accumulate in the basophilic degeneration of the myocardium and the corpora amylacea of the glia.
Using monospecific antibody for the advanced glycosylation end-products (AGEP), it was revealed that the AGEP localized in the basophilic degeneration of the myocardium and the corpora amylacea of the glia. The stability of the proteins that constitute those degenerative deposits suggests that they would be ideal substrates for non-enzymatic glycation, a process that occurs over a long time under a high glucose content, and ultimately results in the formation of the AGEP. Such deposits also exhibited evidence of stress reactions: the accumulation of HSP72, heme oxygenase-1 and ubiquitin. As recent studies have shown that AGEP-modified proteins aggregate and that they generate reactive oxygen intermediates, the accumulation of such heat shock proteins may reflect the oxidative stress concomitant with AGEP accumulation, and thereby promote their cellular dysfunction. Hereby, it is proposed that the age-related increase in the AGEP, that is, a fundamental aging process, is involved in the formation of the basophilic degeneration in the myocardium and the corpora amylacea of the glia.
Iwaki
T
T
Department of Neuropathology, Faculty of Medicine, Kyushu University, Fukuoka, Japan.
Hamada
Y
Y
Tateishi
J
J
D000368:Aged; D000369:Aged, 80 and over; D005260:Female; D017127:Glycation End Products, Advanced / Q000032:analysis*; D006360:Heat-Shock Proteins / Q000032:analysis*; D006801:Humans; D007150:Immunohistochemistry; D002479:Inclusion Bodies / Q000737:chemistry*; D008297:Male; D008875:Middle Aged; D009206:Myocardium / Q000737:chemistry* / Q000473:pathology*; D009336:Necrosis; D009457:Neuroglia / Q000737:chemistry* / Q000473:pathology*
D017127:Glycation End Products, Advanced; D006360:Heat-Shock Proteins