X-Message-Number: 11234
Date: Sun, 7 Feb 1999 17:09:09 -0800 (PST)
From: Doug Skrecky <>
Subject: peroxisomes and aging rats

Authors
  Beier K.  Volkl A.  Fahimi HD.
Institution
  Institut fur Anatomie und Zellbiologie II, Heidelberg, Germany.
Title
  The impact of aging on enzyme proteins of rat liver
  peroxisomes: quantitative analysis by immunoblotting and
  immunoelectron microscopy.
Source
  Virchows Archiv. B, Cell Pathology Including Molecular Pathology. 
  63(3):139-46, 1993.
Abstract
  The alterations of hepatic peroxisomes and their enzymes
  during aging were investigated in male rats.
  Peroxisomes in the livers of young (2 months) and old (39
  months) male Wistar rats were analyzed by morphometry and quantitative
  immunocytochemistry, as well as by immunoblotting of highly purified
  peroxisomal fractions. Immunoblots showed that catalase and acyl-CoA oxidase
  were decreased in peroxisomes of old animals but the
  trifunctional enzyme, thiolase, and urate oxidase were increased. The
  morphometrical analysis revealed a heterogeneous distribution of
  peroxisomes in the liver lobule of the old animals, with a
  significant elevation of peroxisomal volume density in pericentral over
  periportal hepatocytes, in contrast to the uniform pattern in the young rats.
  Furthermore, age-related lobular gradients were also observed by quantitative
  immunocytochemistry in the peroxisomal concentrations of trifunctional enzyme
  (central > portal) and, inversely, for catalase (portal > central). Whereas
  acyl-CoA oxidase was diminished across the liver lobule, the enzyme
  3-ketoacyl-CoA thiolase was elevated. These observations show that
  peroxisomes are significantly altered in aged animals and
  suggest that these alterations may contribute to the disturbance of lipid
  metabolism in aged animals. Moreover, the diminution in catalase and the
  elevation of urate oxidase could contribute to the oxidative stress which is
  considered to be of fundamental importance in the aging
  process.

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