PMID: 8605227Feb 9, 1996Paper

Acetylcholinesterase-induced respiratory burst in macrophages: evidence for the involvement of the macrophage mannose-fucose receptor

Biochimica Et Biophysica Acta
A KlegerisS A Greenfield

Abstract

It has long been suggested that acetylcholinesterase is capable of functioning in a non-cholinergic manner. However, very little is known about the molecular structures which mediate the interaction between this protein and the cellular membrane. Previously it was demonstrated that acetylcholinesterase interacted in a carbohydrate-specific manner with peritoneal macrophages and induced the 'respiratory burst' [1]. This study aimed to establish whether a carbohydrate-binding site exists on the acetylcholinesterase molecule itself, or alternatively, whether the macrophage carbohydrate-binding receptor is involved. No carbohydrate binding properties intrinsic to acetylcholinesterase were detected using affinity chromatography with immobilised monosaccharides, erythrocyte agglutination and gel-diffusion techniques. The interaction between acetylcholinesterase and several monosaccharide columns observed in this study appeared to be due to ionic interactions. Moreover, it was shown that a specific inhibitor of the enzymatic activity of AChE, BW284C51, could inhibit the peritoneal cell response not only to acetylcholinesterase, but also to several other stimuli, thus exhibiting a non-specific effect on macrophages. However, the inhibi...Continue Reading

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Citations

Oct 13, 1999·Journal of Neuroscience Research·M P MarzoloN C Inestrosa
Mar 11, 2005·Pediatric Surgery International·S W Moore, G Johnson
Sep 7, 2006·Journal of Pediatric Gastroenterology and Nutrition·Maria MusumeciSalvatore Musumeci
Feb 13, 2002·American Journal of Physiology. Lung Cellular and Molecular Physiology·Carlos A Rivera-MarreroJesse Roman

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