| Full text | |
| Author(s): Show less - |
Hajj, Glaucia N. M.
;
Lopes, Marilene H.
;
Mercadante, Adriana F.
;
Veiga, Silvio S.
;
Silveira, Rafael B. da
;
Santos, Tiago G.
;
Ribeiro, Karina C. B.
;
Juliano, Maria A.
;
Jacchieri, Saul G.
;
Zanata, Silvio M.
;
Martins, Vilma R.
[11]
Total Authors: 11
|
| Document type: | Journal article |
| Source: | Journal of Cell Science; v. 120, n. 11, p. 1915-1926, May 2007. |
| Field of knowledge: | Biological Sciences - Biochemistry |
| Abstract | |
The physiological functions of the cellular prion protein, PrPC, as a cell surface pleiotropic receptor are under debate. We report that PrPC interacts with vitronectin but not with fibronectin or collagen. The binding sites mediating this PrPC-vitronectin interaction were mapped to residues 105-119 of PrPC and the residues 307-320 of vitronectin. The two proteins were co-localized in embryonic dorsal root ganglia from wild-type mice. Vitronectin addition to cultured dorsal root ganglia induced axonal growth, which could be mimicked by vitronectin peptide 307-320 and abrogated by anti-PrPC antibodies. Full-length vitronectin, but not the vitronectin peptide 307-320, induced axonal growth of dorsal root neurons from two strains of PrPC-null mice. Functional assays demonstrated that relative to wild-type cells, PrPCnull dorsal root neurons were more responsive to the Arg- Gly-Asp peptide (an integrin-binding site), and exhibited greater ALPHA-v-BETA-3 activity. Our findings indicate that PrPC plays an important role in axonal growth, and this function may be rescued in PrPC-knockout animals by integrin compensatory mechanisms. (AU) | |
| FAPESP's process: | 99/07124-8 - The role of celular prion protein in physiological and pathological processes |
| Grantee: | Vilma Regina Martins |
| Support Opportunities: | Research Projects - Thematic Grants |