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Advanced glycosylation end‐products and heat shock proteins accumulate in the basophilic degeneration of the myocardium and the corpora amylacea of the glia
Author(s) -
Iwaki Tow,
Harnada Yasuhiro,
Tateishi Jun
Publication year - 1996
Publication title -
pathology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.73
H-Index - 74
eISSN - 1440-1827
pISSN - 1320-5463
DOI - 10.1111/j.1440-1827.1996.tb03545.x
Subject(s) - glycation , chemistry , heat shock protein , oxidative stress , microbiology and biotechnology , basophilic , glycosylation , degeneration (medical) , biochemistry , lipofuscin , biology , pathology , receptor , medicine , gene
Uslng monospecific antibody for the advanced glycosylation end‐products (AGEP), It was revealed that the AGEP localized in the basophllic 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 the under a high glucose content, and ultimately results in the formation of the AGEP. Such deposlts also exhibited evidence of stress reactions: the accumulation of HSP72, heme oxygenase‐1 and ublquitin. 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 basophllic degeneration in the myocardium and the corpora amylacea of the glla.