TAILIEUCHUNG - Báo cáo khoa học: Respective roles of the catalytic domains and C-terminal tail peptides in the oligomerization and secretory trafficking of human acetylcholinesterase and butyrylcholinesterase

Butyrylcholinesterase (BChE) and the T splice variant of acetylcholinester-ase that is predominant in mammalian brain and muscles (AChET) possess a characteristic C-terminal tail (t) peptide. This t peptide allows their assembly into tetramers associated with the anchoring proteins ColQ and PRiMA. | Respective roles of the catalytic domains and C-terminal tail peptides in the oligomerization and secretory trafficking of human acetylcholinesterase and butyrylcholinesterase Dong Liang1 2 Jean-Philippe Blouet1 Fernanda Borrega1 Suzanne Bon1 and Jean Massoulie1 1 Laboratoire de Neurobiologie CNRS UMR 8544 Ecole Normale Superieure Paris France 2 Key Laboratory of Brain FunctionalGenomics MOE STCSM Shanghai Institute of Brain FunctionalGenomics East China Normal University China Keywords acetylcholinesterase butyrylcholinesterase cysteines oligomers secretion Correspondence J. Massoulie Laboratoire de Neurobiologie CNRS UMR 8544 Ecole Normale Superieure Paris France Fax 33 1 44 32 38 87 Tel 33 1 44 32 38 91 E-mail Received 13 August 2008 revised 25 September 2008 accepted 24 October 2008 doi Butyrylcholinesterase BChE and the T splice variant of acetylcholinesterase that is predominant in mammalian brain and muscles AChET possess a characteristic C-terminal tail t peptide. This t peptide allows their assembly into tetramers associated with the anchoring proteins ColQ and PRiMA. Although the t peptides of all vertebrate cholinesterases are remarkably similar and in particular contain seven strictly conserved aromatic residues these enzymes differ in some of their oligomerization properties. To explore these differences we studied human AChE Aa and BChE Bb and chimeras in which the t peptides a and b were exchanged Ab and Ba . We found that secretion was increased by deletion of the t peptides and that it was more efficient with a than with b. The patterns of oligomers were similar for Aa and Ab as well as for Ba and Bb indicating a predominant influence of the catalytic domains. However addition of a cysteine within the aromatic-rich segment of the t peptides modified the oligomeric patterns with a cysteine at position 19 the proportion of tetramers was markedly increased for Aa S19C and Ba S19C and to a

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