HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 282, Issue 35, 25597-25603, August 31, 2007

This Article Full Text Full Text (PDF) All Versions of this Article: 282/35/25597    most recent M700569200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Santos, S. C. R. Articles by Saldanha, C. Search for Related Content PubMed PubMed Citation Articles by Santos, S. C. R. Articles by Saldanha, C. Social Bookmarking                      What's this?

Expression and Subcellular Localization of a Novel Nuclear Acetylcholinesterase Protein^*

Susana Constantino Rosa Santos¹, Inês Vala, Cláudia Miguel, João T. Barata, Pedro Garção^¶, Paula Agostinho^¶, Marta Mendes^||, Ana V. Coelho^||**, Angelo Calado, Catarina R. Oliveira^¶, João Martins e Silva, and Carlota Saldanha

From the Instituto de Biopatologia Química, Faculdade de Medicina de Lisboa, 1649-028 Lisboa, Portugal, Instituto de Medicina Molecular, 1649-028 Lisboa, Portugal, ^¶Center for Neuroscience and Cell Biology, Faculty of Medicine, University of Coimbra, 3004-504 Coimbra, Portugal, ^||Instituto Tecnologia Química e Biológica, Universidade Nova Lisboa, 2781-901 Oeiras, Portugal, and ^**Departamento de Química, Universidade deÉvora, 7004-516Évora, Portugal

Acetylcholine is found in the nervous system and also in other cell types (endothelium, lymphocytes, and epithelial and blood cells), which are globally termed the non-neuronal cholinergic system. In this study we investigated the expression and subcellular localization of acetylcholinesterase (AChE) in endothelial cells. Our results show the expression of the 70-kDa AChE in both cytoplasmic and nuclear compartments. We also describe, for the first time, a nuclear and cytoskeleton-bound AChE isoform with 55 kDa detected in endothelial cells. This novel isoform is decreased in response to vascular endothelial growth factor via the proteosomes pathway, and it is down-regulated in human leukemic T-cells as compared with normal T-cells, suggesting that the decreased expression of the 55-kDa AChE protein may contribute to an angiogenic response and associate with tumorigenesis. Importantly, we show that its nuclear expression is not endothelial cell-specific but also evidenced in non-neuronal and neuronal cells. Concerning neuronal cells, we can distinguish an exclusively nuclear expression in postnatal neurons in contrast to a cytoplasmic and nuclear expression in embryonic neurons, suggesting that the cell compartmentalization of this new AChE isoform is changed during the development of nervous system. Overall, our studies suggest that the 55-kDa AChE may be involved in different biological processes such as neural development, tumor progression, and angiogenesis.

Received for publication, January 19, 2007 , and in revised form, June 29, 2007.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Instituto de Biopatologia Química, Faculdade de Medicina de Lisboa/Unidade de Biopatologia Vascular, Instituto de Medicina Molecular, Avenida Professor Egas Moniz, 1649-028 Lisboa, Portugal. Tel.: 351-21-799-94-81; Fax: 351-21-799-94-77; E-mail: sconstantino{at}fm.ul.pt.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				M.-X. Silveyra, G. Evin, M.-F. Montenegro, C. J. Vidal, S. Martinez, J. G. Culvenor, and J. Saez-Valero Presenilin 1 Interacts with Acetylcholinesterase and Alters Its Enzymatic Activity and Glycosylation Mol. Cell. Biol., May 1, 2008; 28(9): 2908 - 2919. [Abstract] [Full Text] [PDF]