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Increased Butyrylcholinesterase Levels in Microsomal Membranes of Dystrophic Lama2 dy Mouse Muscle
Author(s) -
MoralNaranjo María Teresa,
Campoy Francisco Javier,
CabezasHerrera Juan,
Vidal Cecilio J.
Publication year - 1999
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1999.0731138.x
Subject(s) - microsome , membrane , butyrylcholinesterase , chemistry , biochemistry , enzyme , acetylcholinesterase , aché
: The proportions and the glycosylation of butyrylcholinesterase (BuChE) forms in vesicles rich in sarcoplasmic reticulum from normal (NMV) and dystrophic (DMV) muscle were analyzed, using merosin‐deficient dystrophic mice. BuChE activity in DMV was two‐ to threefold that in NMV. Globular amphiphilic G A 1 , G A 2 , and G A 4 and hydrophilic G H 4 BuChE forms were identified in NMV and DMV. The amount of G A 2 forms increased sevenfold in DMV, and the other forms increased about twofold. The higher BuChE level in DMV might reflect a maturational defect, with dystrophy preventing the down‐regulation of BuChE with muscle development. About half of G A 1 , G A 2 , and G H 4 BuChE forms in NMV or DMV bound to Lens culinaris agglutinin (LCA), a higher fraction to wheat germ agglutinin (WGA), and little to Ricinus communis agglutinin (RCA). Most of the G A 4 forms in NMV or DMV bound to LCA or WGA ; those from NMV failed to bind to RCA, whereas most of the variants in DMV bound to it, suggesting that the excess of tetramers in DMV is mainly RCA‐reactive. The differential interaction of lectins with BuChE components from muscle microsomes, serum, and nerves confirmed that the microsomal BuChE was muscle‐intrinsic. The results provide clues regarding the alterations that dystrophy produces in the biosynthesis of BuChE forms in muscle.