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PRIMARY STRUCTURE OF A COLLAGENIC TAIL PEPTIDE OF TORPEDO ACETYLCHOLINESTERASE - COEXPRESSION WITH CATALYTIC SUBUNIT INDUCES THE PRODUCTION OF COLLAGEN-TAILED FORMS IN TRANSFECTED CELLS
KREJCI, E; COUSSEN, F; DUVAL, N; CHATEL, M; LEGAY, C; PUYPE, M; Vandekerckhove, J; CARTAUD, J; BON, S; MASSOULIE, J (1991). PRIMARY STRUCTURE OF A COLLAGENIC TAIL PEPTIDE OF TORPEDO ACETYLCHOLINESTERASE - COEXPRESSION WITH CATALYTIC SUBUNIT INDUCES THE PRODUCTION OF COLLAGEN-TAILED FORMS IN TRANSFECTED CELLS. EMBO J. 10(5): 1285-1293
In: The EMBO Journal. Nature Publishing Group: Eynsham (P.O. Box 1, Eynsham, Oxford OX8 1JJ). ISSN 0261-4189, more
Peer reviewed article  

Available in Authors 

Author keywords
    ACETYLCHOLINESTERASE; ASYMMETRIC FORMS; COLLAGEN; CDNA SEQUENCE;TORPEDO-MARMORATA

Authors  Top 
  • KREJCI, E
  • COUSSEN, F
  • DUVAL, N
  • CHATEL, M
  • LEGAY, C
  • PUYPE, M
  • Vandekerckhove, J
  • CARTAUD, J
  • BON, S
  • MASSOULIE, J

Abstract
    The asymmetric forms of cholinesterases are synthesized only in differentiated muscular and neural cells of vertebrates. These complex oligomers are characterized by the presence of a collagen-like tail, associated with one, two or three tetramers of catalytic subunits. The collagenic tail is responsible for ionic interactions, explaining the insertion of these molecules in extracellular basal lamina, e.g. at neuromuscular endplates. We report the cloning of a collagenic subunit from Torpedo marmorata acetylcholinesterase (AChE). The predicted primary structure contains a putative signal peptide, a proline-rich domain, a collagenic domain, and a C-terminal domain composed of proline-rich and cysteine-rich regions. Several variants are generated by alternative splicing. Apart from the collagenic domain, the AChE tail subunit does not present any homology with previously known proteins. We show that coexpression of catalytic AChE subunits and collagenic subunits results in the production of asymmetric, collagen-tailed AChE forms in transfected COS cells. Thus, the assembly of these complex forms does not depend on a specific cellular processing, but rather on the expression of the collagenic subunits.

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