Advanced glycosylation end-products and heat shock proteins accumulate in the basophilic degeneration of the myocardium and the corpora amylacea of the glia
Article first published online: 12 DEC 2008
© 1996 Cambridge Philosophical Society
Volume 46, Issue 10, pages 757–763, October 1996
How to Cite
Iwaki, T., Harnada, Y. and Tateishi, J. (1996), Advanced glycosylation end-products and heat shock proteins accumulate in the basophilic degeneration of the myocardium and the corpora amylacea of the glia. Pathology International, 46: 757–763. doi: 10.1111/j.1440-1827.1996.tb03545.x
- Issue published online: 12 DEC 2008
- Article first published online: 12 DEC 2008
- Received 4 March 1996. Accepted for publication 4 June 1996.
- advanced glycosylation end-products;
- corpora amylacea;
- heat shock protein;
- heme oxygenase-1;
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.