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.
|出版ステータス||Published - 1998|
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