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Cellular prion protein interaction with vitronectin supports axonal growth and is compensated by integrins.

Authors
  • Hajj, Glaucia N M
  • Lopes, Marilene H
  • Mercadante, Adriana F
  • Veiga, Silvio S
  • da Silveira, Rafael B
  • Santos, Tiago G
  • Ribeiro, Karina C B
  • Juliano, Maria A
  • Jacchieri, Saul G
  • Zanata, Silvio M
  • Martins, Vilma R
Type
Published Article
Journal
Journal of cell science
Publication Date
Jun 01, 2007
Volume
120
Issue
Pt 11
Pages
1915–1926
Identifiers
PMID: 17504807
Source
Medline
License
Unknown

Abstract

The physiological functions of the cellular prion protein, PrP(C), as a cell surface pleiotropic receptor are under debate. We report that PrP(C) interacts with vitronectin but not with fibronectin or collagen. The binding sites mediating this PrP(C)-vitronectin interaction were mapped to residues 105-119 of PrP(C) 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-PrP(C) antibodies. Full-length vitronectin, but not the vitronectin peptide 307-320, induced axonal growth of dorsal root neurons from two strains of PrP(C)-null mice. Functional assays demonstrated that relative to wild-type cells, PrP(C)-null dorsal root neurons were more responsive to the Arg-Gly-Asp peptide (an integrin-binding site), and exhibited greater alphavbeta3 activity. Our findings indicate that PrP(C) plays an important role in axonal growth, and this function may be rescued in PrP(C)-knockout animals by integrin compensatory mechanisms.

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