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Current Gerontology and Geriatrics ResearchVolume 2010 2010, Article ID 230697, 9 pages

Research Article

Department of Medical Chemistry and Cell Biology, Institute of Biomedicine, The Sahlgren's Academy, The University of Gothenburg, Box 440, 405 30 Göteborg, Sweden

Institute of Neuroscience and Physiology-Ophthalmology, The Sahlgren's Academy, The University of Gothenburg, Sahlgren's University Hospital-Mölndal, 431 80 Mölndal, Sweden

Received 8 September 2009; Revised 19 November 2009; Accepted 27 January 2010

Academic Editor: Bertrand Friguet

Copyright © 2010 A. Petersen et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

The proteasome is considered the most important proteolytic system for removal of damaged proteins with aging. Using fluorogenic peptide substrates, the chymotrypsin-like, the trypsin-like, and the peptidylglutamyl peptidase activities of the proteasome were measured in the soluble fractions of liver, brain, and lens rat homogenates. Specific activity was significantly decreased in liver and brain homogenates with maturation of the animal, that is, from newborn 7 days old to fertile rats 2–4 months old. Rat lens homogenate exhibited an increase in activity with maturation and also with aging. Chymotrypsin-like activity was stimulated by calcium and this proteolytic activity was significantly decreased with maturation of the rat brain. The Michaelis-Menten constant increased with age in rat liver and lens, indicating a loss of affinity for its substrates by the proteasome in the animal with maturation and aging. The present data suggest that the loss of function of the proteasome with maturation may be due to structural changes of the proteasome or a decreased content of regulatory components.





Autor: A. Petersen, A. Honarvar, and M. Zetterberg

Fuente: https://www.hindawi.com/



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