Literature DB >> 3095415

Age-related acceleration of glycation of tissue proteins in rats.

M Oimomi, Y Kitamura, S Nishimoto, S Matsumoto, H Hatanaka, S Baba.   

Abstract

The Maillard reaction on proteins is a nonenzymatic glycosylation that is now termed glycation and produces a ketoamine linkage on the protein. The extent of this glycation was estimated by determining furosine (epsilon-N-(2-furoylmethyl)-L-lysine), which is derived from glycated lysine residues. Glycation of rat sciatic nerve and aorta increased with advancing age for up to 50 weeks and the high degree of glycation was maintained thereafter. The level of hemoglobin did not change significantly after 14 weeks. These results suggest that tissue glycation may increase with aging and may be involved in the mechanism of aging.

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Year:  1986        PMID: 3095415     DOI: 10.1093/geronj/41.6.695

Source DB:  PubMed          Journal:  J Gerontol        ISSN: 0022-1422


  2 in total

Review 1.  Glycation and insulin resistance: novel mechanisms and unique targets?

Authors:  Fei Song; Ann Marie Schmidt
Journal:  Arterioscler Thromb Vasc Biol       Date:  2012-08       Impact factor: 8.311

2.  Immunohistochemical detection of advanced glycosylation end products in diabetic tissues using monoclonal antibody to pyrraline.

Authors:  S Miyata; V Monnier
Journal:  J Clin Invest       Date:  1992-04       Impact factor: 14.808

  2 in total

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