title: Immune detection of acetylcholinesterase in subcellular compartments of Trypanosoma evansi.
abstract: Trypanosoma evansi is a worldwide distributed hemoparasite with a strong economic impact in veterinary activities. Despite widespread knowledge about the etiology of the disease caused by T. evansi, there are few detailed studies about the metabolism of this parasite. The aim of this study was to determine the presence of Acetylcholinesterase (AChE) in T. evansi through a strategy of subcellular localization and confocal microscopy. The localization of the AChE by differential and isopycnic centrifugation strategy showed that this enzyme has a predominant localization in the glycosome, similar to hexokinase, and it is not present in either the cytosol or the plasma membrane. This study shows novel data that help to understand the non-neuronal role of AChE in the Trypanosomatidae family.
authors.affiliation: Centro de Biofísica y Bioquímica, Laboratorio de Fisiología de Parásitos, Instituto Venezolano de Investigaciones Científicas, A.P. 20632, Caracas 1020A, Venezuela.
authors.forename: Alfredo
authors.initials: A
authors.lastname: Mijares
authors.forename: Juan L
authors.initials: JL
authors.lastname: Concepción
authors.forename: Jose R
authors.initials: JR
authors.lastname: Vielma
authors.forename: Ramon
authors.initials: R
authors.lastname: Portillo
mesh_terms: D000110:Acetylcholinesterase / Q000032:analysis*; D002498:Centrifugation; D006801:Humans; D008830:Microbodies / Q000737:chemistry* / Q000201:enzymology*; D018613:Microscopy, Confocal; D014345:Trypanosoma / Q000737:chemistry* / Q000201:enzymology*
chemical_list: D000110:Acetylcholinesterase
references.citation: Annu Rev Entomol. 1998;43:1-16
references.pmid: 9444749
references.citation: Arch Biochem Biophys. 1998 Apr 1;352(1):114-20
references.pmid: 9521823
references.citation: Biochem Biophys Res Commun. 2001 Feb 23;281(2):300-4
references.pmid: 11181045
references.citation: Comp Biochem Physiol B Biochem Mol Biol. 1999 Feb;122(2):211-22
references.pmid: 10327611
references.citation: Protein Sci. 1999 Dec;8(12):2553-61
references.pmid: 10631970
references.citation: Exp Parasitol. 1987 Feb;63(1):84-97
references.pmid: 3026835
references.citation: Exp Parasitol. 2010 Jun;125(2):100-5
references.pmid: 20093112
references.citation: FEMS Microbiol Lett. 1992 Aug 15;74(2-3):267-70
references.pmid: 1326469
references.citation: FASEB J. 1992 Feb 1;6(3):845-52
references.pmid: 1740234
references.citation: J Biol Chem. 1951 Nov;193(1):265-75
references.pmid: 14907713
references.citation: Exp Parasitol. 2001 Dec;99(4):213-9
references.pmid: 11888248
references.citation: Parasitol Today. 1996 Feb;12(2):61-5
references.pmid: 15275256
references.citation: Vet J. 1997 Jul;154(1):11-34
references.pmid: 9265850
references.citation: Exp Parasitol. 1970 Dec;28(3):521-34
references.pmid: 4993889
references.citation: J Biol Chem. 1992 Mar 25;267(9):6020-6
references.pmid: 1556113
references.citation: Eur J Biochem. 1999 Sep;264(3):672-86
references.pmid: 10491113
references.citation: Cell Mol Biol (Noisy-le-grand). 1996 Mar;42(2):221-5
references.pmid: 8696258
references.citation: Acta Cient Venez. 1993;44(2):57-66
references.pmid: 8085408
references.citation: Parasitol Today. 1994 Mar;10(3):107-10
references.pmid: 15275492
references.citation: Mol Biochem Parasitol. 2001 Nov;118(1):111-21
references.pmid: 11704279
references.citation: Biochemistry. 1999 Jun 1;38(22):7032-9
references.pmid: 10353814
references.citation: Mol Biochem Parasitol. 2002 Mar;120(1):83-91
references.pmid: 11849708
references.citation: Pharmacol Ther. 1998 Jan;77(1):59-79
references.pmid: 9500159
references.citation: Mol Biol Evol. 1998 May;15(5):518-27
references.pmid: 9580980
references.citation: Trends Biochem Sci. 1990 Jun;15(6):213-6
references.pmid: 2200163