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Cholinesterases in development: AChE as a firewall to inhibit cell proliferation and support differentiation.

Layer, Paul G. and Klaczinski, Janine and Salfelder, Anika and Sperling, Laura E. and Thangaraj, Gopenath and Tuschl, Corina and Vogel-Höpker, A. (2013):
Cholinesterases in development: AChE as a firewall to inhibit cell proliferation and support differentiation.
In: Chemico-biological interactions, 203 (1), pp. 269-276. ISSN 1872-7786,
[Article]

Abstract

Acetylcholinesterase (AChE) is a most remarkable protein, not only because it is one of the fastest enzymes in nature, but also since it appears in many molecular forms and is regulated by elaborate genetic networks. AChE is expressed in many tissues during development and in mature organisms, as well as in healthy and diseased states. In search for alternative, "non-classical" functions of cholinesterases (ChEs), AChE could either work within the frame of classic cholinergic systems, but in non-neural tissues ("non-synaptic function"), or act non-enzymatically. Here, we review briefly some of the major ideas and advances of this field, and report on some recent progress from our own experimental work, e.g. that i) non-neural ChEs have pronounced, predominantly enzymatic effects on early embryonic (limb) development in chick and mouse, that ii) retinal R28 cells of the rat overexpressing synaptic AChE present a significantly decreased cell proliferation, and that iii) in developing chick retina ACh-synthesizing and ACh-degrading cells originate from the same postmitotic precursor cells, which later form two locally opposing cell populations. We suggest that such distinct distributions of ChAT(+) vs. AChE(+) cells in the inner half retina provide graded distributions of ACh, which can direct cell differentiation and network formation. Thus, as corroborated by works from many labs, AChE can be considered a highly co-opting protein, which can combine enzymatic and non-enzymatic functions within one molecule.

Item Type: Article
Erschienen: 2013
Creators: Layer, Paul G. and Klaczinski, Janine and Salfelder, Anika and Sperling, Laura E. and Thangaraj, Gopenath and Tuschl, Corina and Vogel-Höpker, A.
Title: Cholinesterases in development: AChE as a firewall to inhibit cell proliferation and support differentiation.
Language: English
Abstract:

Acetylcholinesterase (AChE) is a most remarkable protein, not only because it is one of the fastest enzymes in nature, but also since it appears in many molecular forms and is regulated by elaborate genetic networks. AChE is expressed in many tissues during development and in mature organisms, as well as in healthy and diseased states. In search for alternative, "non-classical" functions of cholinesterases (ChEs), AChE could either work within the frame of classic cholinergic systems, but in non-neural tissues ("non-synaptic function"), or act non-enzymatically. Here, we review briefly some of the major ideas and advances of this field, and report on some recent progress from our own experimental work, e.g. that i) non-neural ChEs have pronounced, predominantly enzymatic effects on early embryonic (limb) development in chick and mouse, that ii) retinal R28 cells of the rat overexpressing synaptic AChE present a significantly decreased cell proliferation, and that iii) in developing chick retina ACh-synthesizing and ACh-degrading cells originate from the same postmitotic precursor cells, which later form two locally opposing cell populations. We suggest that such distinct distributions of ChAT(+) vs. AChE(+) cells in the inner half retina provide graded distributions of ACh, which can direct cell differentiation and network formation. Thus, as corroborated by works from many labs, AChE can be considered a highly co-opting protein, which can combine enzymatic and non-enzymatic functions within one molecule.

Journal or Publication Title: Chemico-biological interactions
Journal volume: 203
Number: 1
Divisions: 10 Department of Biology
10 Department of Biology > Developmental Biology and Neurogenetics
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Date Deposited: 16 Oct 2012 08:32
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