Division of Life Science, Center for Chinese Medicine, The Hong Kong University of Science and Technology Hong Kong, China.
Front Mol Neurosci. 2011 Oct 25;4:36. doi: 10.3389/fnmol.2011.00036. eCollection 2011.
Acetylcholinesterase (AChE) is responsible for the hydrolysis of the neurotransmitter, acetylcholine, in the nervous system. The functional localization and oligomerization of AChE T variant are depending primarily on the association of their anchoring partners, either collagen tail (ColQ) or proline-rich membrane anchor (PRiMA). Complexes with ColQ represent the asymmetric forms (A(12)) in muscle, while complexes with PRiMA represent tetrameric globular forms (G(4)) mainly found in brain and muscle. Apart from these traditional molecular forms, a ColQ-linked asymmetric form and a PRiMA-linked globular form of hybrid cholinesterases (ChEs), having both AChE and BChE catalytic subunits, were revealed in chicken brain and muscle. The similarity of various molecular forms of AChE and BChE raises interesting question regarding to their possible relationship in enzyme assembly and localization. The focus of this review is to provide current findings about the biosynthesis of different forms of ChEs together with their anchoring proteins.
乙酰胆碱酯酶（AChE）负责水解神经系统中的神经递质乙酰胆碱。AChE T 变体的功能定位和寡聚化主要取决于其锚定伙伴胶原尾（ColQ）或富含脯氨酸的膜锚（PRiMA）的关联。与 ColQ 形成的复合物代表肌肉中的不对称形式（A(12)），而与 PRiMA 形成的复合物代表主要在大脑和肌肉中发现的四聚体球状形式（G(4)）。除了这些传统的分子形式外，在鸡的大脑和肌肉中还发现了具有 AChE 和 BChE 催化亚基的混合乙酰胆碱酯酶（ChE）的 ColQ 连接的不对称形式和 PRiMA 连接的球状形式。AChE 和 BChE 的各种分子形式的相似性提出了一个有趣的问题，即它们在酶组装和定位中的可能关系。这篇综述的重点是提供有关不同形式的 ChE 及其锚定蛋白生物合成的最新发现。
