Butterfield, D.A., Reed, T., Newman, S.F. and Sultana, R. (2007) Roles of Amyloid β-Peptide-Associated Oxidative Stress and Brain Protein Modifications in the Pathogenesis of Alzheimer’s Disease and Mild Cognitive Impairment. Free Radical Biology and Medicine, 43, 658-677.
http://dx.doi.org/10.1016/j.freeradbiomed.2007.05.037

has been cited by the following article:

• TITLE: Role of Cathepsin G in the Degradation of Glyceraldehyde-3-Phosphate Dehydrogenase Triggered by 4-Hydroxy-2-Nonenal in U937 Cells

  AUTHORS: Satoshi Ohta, Noriko Suzuki, Shigeki Kobayashi, Toshiyuki Chikuma

  KEYWORDS: 4-Hydroxy-2-Nonenal, Glyceraldehyde-3-Phosphate Dehydrogenase, Cathepsin G, U937, Oxidative Stress, Proteasome

  JOURNAL NAME: CellBio, Vol.3 No.2, May 16, 2014

  ABSTRACT: Degradation of oxidized or oxidatively modified proteins is an essential part of the cellular antioxidant defense system. 4-Hydroxy-2-nonenal (HNE), a major reactive aldehyde formed by lipid peroxidation, causes many types of cellular damage. HNE-modified proteins are degraded by the ubiquitin-proteasome pathway or the lysosomal pathway. However, our previous studies using U937 cells showed that HNE-modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is degraded by cathepsin G. In the present study, we examined whether GAPDH in U937 cells treated with HNE in culture is degraded similarly to that incubated with HNE and U937 cell extract. Treatment with HNE for 10 min in culture decreased GAPDH activity in a concentration dependent manner, but did not affect GAPDH degradation. The proteasome activities were not affected by HNE, but culturing with HNE decreased cathepsin G activity and protein level in a concentration dependent manner. These results suggest that HNE-induced oxidative stress leads to decreased cathepsin G activity and results in the loss of GAPDH degradation. Taken together, our findings indicate that cathepsin G has an important role in the degradation of oxidatively modified GAPDH in U937 cells.