Selective degradation of oxidatively modified protein substrates by the proteasome
Section snippets
Oxidative protein modification
The degree of protein oxidation caused by a given oxidant depends on many factors, including the nature, relative location, and flux rate of the oxidant, and the presence (or absence) of antioxidants. Both the oxidation of free amino acids and the oxidation of peptides and proteins have been studied by many laboratories, and numerous amino acids are known to be susceptible to oxidation [4], [5], [6], [11], [16], [18], [39], [40]. Although chemical reactions occur during amino acid side chain
Accumulation of cross-linked proteins
Several diseases, and aging processes, are accompanied by the accumulation of cross-linked proteins. This accumulation of oxidized protein aggregates can occur both extracellularly, and within various cellular compartments. Differences in the effects of protein aggregates on various cellular or organismal functions may be expected, depending on the rate of formation and the exact location of such aggregates. In several cases aggregated/cross-linked material will be autophagocytosed, resulting
Degradation of oxidized proteins
Following exposure to oxidants one can detect changes in the proteolytic susceptibility of a number of protein substrates (Fig. 2). This change in proteolytic susceptibility has a biphasic response. At moderate oxidant concentrations proteolytic susceptibility increases, whereas at higher oxidant concentrations a decrease (sometimes even below the ‘basal degradation’ level) in proteolytic susceptibility occurs (see Fig. 2). Between these extremes, the oxidant reaches an ‘optimal concentration’
Recognition of the oxidized protein substrates by the proteasome
It has been shown that erythrocytes and reticulocytes from rabbits, cows, and human beings, as well as rat muscles in vitro, rat hepatocytes, fibroblasts, macrophages, tumor cells, and Escherichia coli cells [1], [2], [9], [14], [15], [16], [21], [22], [24], [30], [31], [54], [55], [56], [57] are able to selectively degrade oxidatively modified proteins. What forms the recognition motif of oxidized proteins for the proteasome is one of the key research questions surrounding the fate of oxidized
Role of further components of the proteasomal system in the recognition of oxidized proteins
Numerous studies have been performed using the isolated 20S ‘core’ proteasome to degrade oxidized proteins. However, since our knowledge about the proteasomal system, its components, and its coordinated action with various ubiquitination systems is quite extensive, the question arises as to which form of the proteasome is involved in the degradation of oxidized proteins. Today it is accepted that the proteasome is just the core proteolytic particle of a whole system of regulatory factors, many
Recognition of oxidized proteins in cells
Although it is generally accepted that oxidized, unfolded proteins can be degraded by the isolated 20S ‘core’ proteasome in vitro, it has been rather less clear if this same form of the proteasome actually has physiological relevance in living cells. Rivett [1], [2] demonstrated the selective degradation of oxidatively modified glutamine synthetase in a non-lysosomal pathway by a cytosolic protease. Subsequently, numerous studies have demonstrated that this key enzyme is the proteasome,
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