Modifications of Glyceraldehyde-3-PhosphateDehydrogenase Induced by IncreasingConcentrations of Peroxynitrite:Early Recognition by 20S Proteasome
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| 024 | 7 | 0 | |a 10.1515/BC.2003.026 |2 doi |
| 035 | |a (NATIONALLICENCE)gruyter-10.1515/BC.2003.026 | ||
| 245 | 0 | 0 | |a Modifications of Glyceraldehyde-3-PhosphateDehydrogenase Induced by IncreasingConcentrations of Peroxynitrite:Early Recognition by 20S Proteasome |h [Elektronische Daten] |c [D.P. Buchczyk, T. Grune, H. Sies, L.-O. Klotz] |
| 520 | 3 | |a Peroxynitrite, a potent oxidizing and nitrating species, induces covalent modifications of biomolecules in a number of pathological conditions. In previous studies with S. cerevisiae, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was identified as being especially susceptible to nitration by peroxynitrite. The activity of this enzyme was strongly inhibited by low doses of peroxynitrite in yeast and in cultured rat astrocytes. Here, the sequence of modifications of isolated mammalian GAPDH induced by increasing concentrations of peroxynitrite is demonstrated to be as follows: (i) oxidation, leading to inactivation and to enhanced susceptibility of GAPDH for proteasomal degradation, (ii) oligomer formation, and (iii) nitration. In our study the susceptibility for degradation by isolated 20S proteasome was by far the most sensitive parameter for peroxynitrite-induced damage to GAPDH, implying that this might also occur under pathological conditions where peroxynitrite is generated at low concentrations in vivo. | |
| 540 | |a Copyright © 2003 by Walter de Gruyter GmbH & Co. KG | ||
| 690 | 7 | |a Biochemistry |2 nationallicence | |
| 690 | 7 | |a Molecular biology |2 nationallicence | |
| 690 | 7 | |a Cellular biology |2 nationallicence | |
| 700 | 1 | |a Buchczyk |D D.P. |4 aut | |
| 700 | 1 | |a Grune |D T. |4 aut | |
| 700 | 1 | |a Sies |D H. |4 aut | |
| 700 | 1 | |a Klotz |D L.-O |4 aut | |
| 773 | 0 | |t Biological Chemistry |d Walter de Gruyter |g 384/2(2003-02-20), 237-241 |x 1431-6730 |q 384:2<237 |1 2003 |2 384 |o bchm | |
| 856 | 4 | 0 | |u https://doi.org/10.1515/BC.2003.026 |q text/html |z Onlinezugriff via DOI |
| 908 | |D 1 |a research article |2 jats | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1515/BC.2003.026 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Buchczyk |D D.P. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Grune |D T. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Sies |D H. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Klotz |D L.-O |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Biological Chemistry |d Walter de Gruyter |g 384/2(2003-02-20), 237-241 |x 1431-6730 |q 384:2<237 |1 2003 |2 384 |o bchm | ||
| 900 | 7 | |b CC0 |u http://creativecommons.org/publicdomain/zero/1.0 |2 nationallicence | |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-gruyter | ||