| First Author | Brown DR | Year | 1998 |
| Journal | J Neurosci Res | Volume | 52 |
| Issue | 3 | Pages | 260-7 |
| PubMed ID | 9590434 | Mgi Jnum | J:47452 |
| Mgi Id | MGI:1203455 | Doi | 10.1002/(SICI)1097-4547(19980501)52:3<260::AID-JNR2>3.0.CO;2-B |
| Citation | Brown DR, et al. (1998) Prion protein fragment interacts with PrP-deficient cells. J Neurosci Res 52(3):260-7 |
| abstractText | A fragment of the prion protein (PrP106-126) induces cell death in cultures of wild-type embryonic day (E)16 mouse cortical neurons but not cells derived from mice devoid of cellular PrP(PrPo/o). Two common binding partners for PrP106-126 expressed in both wild-type and PrPo/o mouse brain were isolated and their sequences determined. The two proteins were found to be alpha and beta tubulin. Further evidence that tubulin binds PrP106-126 within cells comes from cell culture experiments. Colchicine toxicity on PrPo/o mouse cortical cells is enhanced by PrP106-126 and taxol enhances toxicity of PrP106-126 on wild-type mouse cortical cells. Our evidence shows that a fragment of PrP can bind a cellular protein and in so doing, alters the metabolism of cells even when they do not express native PrP. This indicates that PrP106-126 is nontoxic to PrPo/o cells, not because of an inability to interact with these cells but because of the loss of some aspect of a PrP expression-dependent phenotype. |
