| Autor: |
Alain Anselmet, Jean Massoulié, Françoise Coussen, Eric Krejci, Claire Legay, Suzanne Bon |
| Rok vydání: |
1996 |
| Předmět: |
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| Popis: |
Publisher Summary This chapter focuses on the biosynthesis and integration of acetylcholinesterase in the cholinergic synapse. Acetylcholine is rapidly hydrolyzed by acetylcholinesterase after its release in cholinergic synapses. This enzyme possesses an extremely high catalytic efficiency and also presents a variety of molecular forms that may be anchored in various ways in the synaptic architecture. The implication of cholinesterases in non-synaptic functions may imply their catalytic activity on acetylcholine or possibly on other substrates. In this respect, it should be emphasized that the possibility of a peptidasic activity has now been conclusively ruled out. The significance of the different forms of Acetylcholinesterase (AChE) in vivo is assessed by inactivating the genes encoding each type of anchoring protein in transgenic mice. An implication in cellular interactions would be consistent with the fact that some acetylcholinesterase molecules carry the HNK-1 epitope, which is considered a hallmark of adhesion proteins, and more convincingly that they are homologous with non enzymatic adhesion molecules. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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