| First Author | Sakudo A | Year | 2004 |
| Journal | Biochem Biophys Res Commun | Volume | 313 |
| Issue | 4 | Pages | 850-5 |
| PubMed ID | 14706620 | Mgi Jnum | J:87467 |
| Mgi Id | MGI:2687162 | Doi | 10.1016/j.bbrc.2003.12.020 |
| Citation | Sakudo A, et al. (2004) Prion protein suppresses perturbation of cellular copper homeostasis under oxidative conditions. Biochem Biophys Res Commun 313(4):850-5 |
| abstractText | Prion protein (PrP) binds copper and exhibits superoxide dismutase-like activity, while the roles of PrP in copper homeostasis remain controversial. Using Zeeman graphite furnace atomic absorption spectroscopy, we quantified copper levels in immortalized PrP gene (Prnp)-deficient neuronal cells transfected with Prnp and/or Prnd, which encodes PrP-like protein (PrPLP/Dpl), in the presence or absence of oxidative stress induced by serum deprivation. In the presence of serum, copper levels were not significantly affected by the expression of PrP and/or PrPLP/Dpl, whereas serum deprivation induced a decrease in copper levels that was inhibited by PrP but not by PrPLP/Dpl. The inhibitory effect of PrP on the decrease of copper levels was prevented by overexpression of PrPLP/Dpl. These findings indicate that PrP specifically stabilizes copper homeostasis, which is perturbed under oxidative conditions, while PrPLP/Dpl overexpression prevents PrP function in copper homeostasis, suggesting an interaction of PrP and PrPLP/Dpl and distinct functions between PrP and PrPLP/Dpl on metal homeostasis. Taken together, these results strongly suggest that PrP, in addition to its antioxidant properties, plays a role in stabilizing cellular copper homeostasis under oxidative conditions. |
