Localization of identified advanced glycation end-product structures, Nε-(carboxymethyl)lysine and pentosidine, in age-related inclusions in human brains

Takemi Kimura, Junichi Takamatsu, Toshio Miyata, Taihei Miyakawa, Seikoh Horiuchi

Research output: Contribution to journalArticlepeer-review

48 Citations (Scopus)

Abstract

The recent identification of age-related accumulation of advanced glycation end-products (AGE) of the Maillard reaction in neurons and vessels of the human brain suggests the involvement of AGE in the aging process. A variety of inclusions such as lipofuscin granules, corpora amylacea, Hirano bodies, granulovacuolar degenerations and ubiquitin-positive granular structures are found in the aged human brain. These age-related inclusions contain insoluble and non-degradable proteins. Advanced glycation end- product-modified proteins are also known to be insoluble and protease resistant. The similarity between proteins in such inclusions and AGE- modified proteins suggests the presence of AGE in inclusions. To investigate this possibility, the presence of two known AGE structures, Nε- (carboxymethyl)lysine (CML) and pentosidine, was examined in age-related inclusions. Immunohistochemical examination of the medial temporal area of brain tissues obtained at autopsy from seven non-demented elderly individuals demonstrated positive reactions in lipofuscin granules and corpora amylacea but not in other inclusions for anti-CML and anti-pentosidine antibodies. As CML and pentosidine are glycoxidation products among AGE, the results suggest that glycation and/or oxidation may be involved in the formation of lipofuscin granules and corpora amylacea.

Original languageEnglish
Pages (from-to)575-579
Number of pages5
JournalPathology international
Volume48
Issue number8
DOIs
Publication statusPublished - 1998 Jan 1
Externally publishedYes

Keywords

  • Advanced glycation end-products
  • Aging
  • Corpora amylacea
  • Glycation
  • Lipofuscin granules
  • Nε-(carboxymethyl) lysine
  • Oxidation
  • Pentosidine

ASJC Scopus subject areas

  • Pathology and Forensic Medicine

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