Artículo
Differential inhibition of human erythrocyte acetylcholinesterase by polyphenols epigallocatechin-3-gallate and resveratrol. Relevance of the membrane-bound form
Salazar, Paula Belén
; de Athayde Moncovo Collado, Alejandro
; Canal Martinez, Veronica de Los Angeles
; Minahk, Carlos Javier
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Fecha de publicación:
01/2017
Editorial:
IOS Press
Revista:
Biofactors
ISSN:
0951-6433
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
The activity of acetylcholinesterase (AChE) from human erythrocytes was tested in the presence of the phenolic compounds resveratrol and epigallocatechin-3-gallate (EGCG). Even though the stilbene barely changed this enzymatic activity, EGCG did inhibit AChE. Importantly, it preferentially acted on the membrane-bound enzyme rather than on its soluble form. Actually, it was shown that this flavonoid may bind to the red blood cell membrane surface, which may improve the interaction between EGCG and AChE. Therefore, caution should be taken when screening AChE inhibitors. In fact, testing compounds with the soluble form of the enzyme may underestimate the activity of some of these potential inhibitors, hence it would be advisable not to use them as a sole model system for screening. Moreover, erythrocyte AChE is proposed as a good model for these enzymatic assays. � 2016 BioFactors, 43(1):73–81, 2017.
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Articulos(INSIBIO)
Articulos de INST.SUP.DE INVEST.BIOLOGICAS
Articulos de INST.SUP.DE INVEST.BIOLOGICAS
Citación
Salazar, Paula Belén; de Athayde Moncovo Collado, Alejandro; Canal Martinez, Veronica de Los Angeles; Minahk, Carlos Javier; Differential inhibition of human erythrocyte acetylcholinesterase by polyphenols epigallocatechin-3-gallate and resveratrol. Relevance of the membrane-bound form; IOS Press; Biofactors; 43; 1; 1-2017; 73-81
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