TAILIEUCHUNG - Báo cáo khoa học: Biochemical characterization of human umbilical vein endothelial cell membrane bound acetylcholinesterase

Acetylcholinesterase is an enzyme whose best-known function is to hydro-lyze the neurotransmitter acetylcholine. Acetylcholinesterase is expressed in several noncholinergic tissues. Accordingly, we report for the first time the identification of acetylcholinesterase in human umbilical cord vein endo-thelial cells. Here we further performed an electrophoretic and biochemical characterization of this enzyme, using protein extracts obtained by solubili-zation of human endothelial cell membranes with Triton X-100. . | iFEBS Journal Biochemical characterization of human umbilical vein endothelial cell membrane bound acetylcholinesterase Filomena A. Carvalho1 Luis M. Graọa2 Joao Martins-Silva1 and Carlota Saldanha1 1 Institute de Biopatologia Quimica Faculdade de Medicina de Lisboa Unidade de Biopatologia Vascular Institute de Medicina Molecular Lisbon Portugal 2 Departamento de Ginecologia Obstetricia Hospitalde Santa Maria de Lisboa Lisbon Portugal Keywords acetylcholinesterase biochemical characterization cellular membrane human endothelial cells Correspondence F. Almeida Carvalho Instituto de Biopatologia Quimica Faculdade de Medicina de Lisboa Unidade de Biopatologia Vascular Instituto de Medicina Molecular Edificio Egas Moniz Avenue Prof Egas Moniz 1649-028 Lisbon Portugal Tel 351 21 7985136 Fax 351 21 7999477 E-mail filomenacarvalho@ Received 15 July 2005 revised 25 August 2005 accepted 2 September 2005 doi Acetylcholinesterase is an enzyme whose best-known function is to hydrolyze the neurotransmitter acetylcholine. Acetylcholinesterase is expressed in several noncholinergic tissues. Accordingly we report for the first time the identification of acetylcholinesterase in human umbilical cord vein endothelial cells. Here we further performed an electrophoretic and biochemical characterization of this enzyme using protein extracts obtained by solubilization of human endothelial cell membranes with Triton X-100. These extracts were analyzed under polyacrylamide gel electrophoresis in the presence of Triton X-100 and under nondenaturing conditions followed by specific staining for cholinesterase or acetylcholinesterase activity. The gels revealed one enzymatically active acetylcholinesterase band in the extracts that disappeared when staining was performed in the presence of eserine an acetylcholinesterase inhibitor . Performing western blotting with the C-terminal anti-acetylcholinesterase IgG we identified a single protein band of .

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