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Exp Gerontol. 2014 Sep;57:122-31. doi: 10.1016/j.exger.2014.05.016. Epub 2014 May 28.

Accumulation of modified proteins and aggregate formation in aging.

Author information

1
Department of Nutritional Toxicology, Institute of Nutrition, Friedrich-Schiller-University Jena, 07743 Jena, Germany.
2
Department of Nutritional Toxicology, Institute of Nutrition, Friedrich-Schiller-University Jena, 07743 Jena, Germany. Electronic address: annika.hoehn@uni-jena.de.

Abstract

Increasing cellular damage during the aging process is considered to be one factor limiting the lifespan of organisms. Besides the DNA and lipids, proteins are frequent targets of non-enzymatic modifications by reactive substances including oxidants and glycating agents. Non-enzymatic protein modifications may alter the protein structure often leading to impaired functionality. Although proteolytic systems ensure the removal of modified proteins, the activity of these proteases was shown to decline during the aging process. The additional age-related increase of reactive compounds as a result of impaired antioxidant systems leads to the accumulation of damaged proteins and the formation of protein aggregates. Both, non-enzymatic modified proteins and protein aggregates impair cellular functions and tissue properties by a variety of mechanisms. This is increasingly important in aging and age-related diseases. In this review, we will give an overview on oxidation and glycation of proteins and the function of modified proteins in aggregate formation. Furthermore, their effects as well as their role in aging and age-related diseases will be highlighted.

KEYWORDS:

Advanced glycation end products; Aging; Lipofuscin; Protein aggregates; Protein oxidation

PMID:
24877899
DOI:
10.1016/j.exger.2014.05.016
[Indexed for MEDLINE]

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