First Author | Yasuda T | Year | 2013 |
Journal | Biochem Biophys Res Commun | Volume | 436 |
Issue | 2 | Pages | 289-94 |
PubMed ID | 23743200 | Mgi Jnum | J:203207 |
Mgi Id | MGI:5525189 | Doi | 10.1016/j.bbrc.2013.05.095 |
Citation | Yasuda T, et al. (2013) DJ-1 cooperates with PYCR1 in cell protection against oxidative stress. Biochem Biophys Res Commun 436(2):289-94 |
abstractText | DJ-1, a product of the DJ-1/PARK7 gene, has been suggested to play various functions involved in transcriptional regulation, protease activity, anti-oxidative stress activity, and regulation of mitochondrial complex I. Such a variety of functions of DJ-1 are supposed to be realized through interactions with different partner proteins. Among the candidates for DJ-1-partner proteins detected in TOF-MAS analyses of the cellular proteins co-immunoprecipitated with DJ-1, we focused here pyrroline-5-carboxylate reductase 1, PYCR1, a final key enzyme for proline biosynthesis. DJ-1 directly bound to PYCR1 in vivo and in vitro. DJ-1 and PYCR1 colocalized in mitochondria, and both were suggested to be involved in regulation of mitochondrial membrane potential, but differently. DJ-1 enhanced the enzymatic activity of PYCR1 in vitro. The cells knocked down for DJ-1 and PYCR1 showed lower viability under oxidative stress conditions. No additive nor synergistic results were obtained for the cells that had been knocked down for both DJ-1 and PYCR1, suggesting that DJ-1 and PYCR1 are on the same pathway of anti-oxidative stress protection of the cells. |