Mouse AChE binds in vivo to domain IV of laminin-1beta
Functions of acetylcholinesterase (AChE) other than hydrolysis of acetylcholine, e.g. related to cell differentiation, synaptogenesis, neuronal signaling and diseases are well documented, but mechanisms supporting them are not understood. Therefore, we searched for AChE ligands in the central nervou...
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| Veröffentlicht in: | Chemico-biological interactions 2005-12, Vol.157-158, p.411-413 |
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| creator | Paraoanu, Laura E Layer, Paul G |
| description | Functions of acetylcholinesterase (AChE) other than hydrolysis of acetylcholine, e.g. related to cell differentiation, synaptogenesis, neuronal signaling and diseases are well documented, but mechanisms supporting them are not understood. Therefore, we searched for AChE ligands in the central nervous system using a yeast two-hybrid screen (Y2H). 18 independent candidates were identified. One of the membrane or extracellular proteins was laminin-1, an extracellular matrix protein involved in neuronal differentiation and adhesion. The laminin-1 fragment found to interact with AChE contains 898 bp from the 1beta-chain. Moreover, we identified the region containing amino acid residues 240-503 of AChE as essential for interaction with laminin-1beta. Co-immunoprecipitation experiments confirmed the yeast two-hybrid results. |
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Therefore, we searched for AChE ligands in the central nervous system using a yeast two-hybrid screen (Y2H). 18 independent candidates were identified. One of the membrane or extracellular proteins was laminin-1, an extracellular matrix protein involved in neuronal differentiation and adhesion. The laminin-1 fragment found to interact with AChE contains 898 bp from the 1beta-chain. Moreover, we identified the region containing amino acid residues 240-503 of AChE as essential for interaction with laminin-1beta. 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Therefore, we searched for AChE ligands in the central nervous system using a yeast two-hybrid screen (Y2H). 18 independent candidates were identified. One of the membrane or extracellular proteins was laminin-1, an extracellular matrix protein involved in neuronal differentiation and adhesion. The laminin-1 fragment found to interact with AChE contains 898 bp from the 1beta-chain. Moreover, we identified the region containing amino acid residues 240-503 of AChE as essential for interaction with laminin-1beta. 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| subjects | Acetylcholinesterase - metabolism Animals Brain - metabolism Immunohistochemistry Laminin - chemistry Laminin - metabolism Mice Protein Binding Protein Structure, Tertiary Signal Transduction Two-Hybrid System Techniques |
| title | Mouse AChE binds in vivo to domain IV of laminin-1beta |
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