期刊
JOURNAL OF CELL SCIENCE
卷 120, 期 11, 页码 1915-1926出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.03459
关键词
dorsal root ganglia; extracellular matrix; cellular prion protein; vitronectin; axon growth; integrins
类别
资金
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [99/07124-8] Funding Source: FAPESP
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, PrPC-null 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.
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