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Cellular prion protein binds laminin and mediates neuritogenesis
E Graner1, A F Mercadante, S M Zanata
1Ludwig Institute for Cancer Research, São Paulo Branch, Rua Prof. Antônio Prudente 109/4A, 01509-010, São Paulo, Brazil.
Brain Research. Molecular Brain Research
|March 17, 2000
Summary
The cellular prion protein (PrPc) acts as a specific receptor for laminin (LN), a key molecule in neuron development. This interaction is crucial for neuronal plasticity and neurite outgrowth.
Area of Science:
- Neuroscience
- Cell Biology
- Biochemistry
Background:
- Laminin (LN) is vital for neuronal differentiation, migration, and survival.
- The cellular prion protein (PrPc) is implicated in various cellular processes.
Purpose of the Study:
- To investigate the interaction between cellular prion protein (PrPc) and laminin (LN).
- To determine the role of PrPc-LN interaction in neuritogenesis and neuronal plasticity.
Main Methods:
- Biochemical assays to confirm PrPc as a specific, high-affinity receptor for LN.
- Cellular studies using PC-12 cells and primary neuronal cultures (rat, wild type, and PrP null mice).
- Identification of the LN binding site within a gamma-1 chain peptide.
Main Results:
- PrPc functions as a saturable, specific, high-affinity receptor for LN.
- The PrPc-LN interaction mediates neuritogenesis induced by nerve growth factor (NGF) plus LN in PC-12 cells.
- A carboxy-terminal decapeptide from the gamma-1 LN chain contains the PrPc binding site.
- PrPc is the primary cellular receptor for this LN domain, influencing neuritogenesis in primary hippocampal neurons.
Conclusions:
- The interaction between PrPc and LN is a significant mechanism in neuronal plasticity.
- PrPc plays a critical role in mediating the effects of specific laminin domains on neuronal development.