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Glycosylation of Acetylcholinesterase Forms in Microsomal Membranes from Normal and Dystrophic Lama2 dy Mouse Muscle
Author(s) -
CabezasHerrera Juan,
MoralNaranjo María Teresa,
Campoy F. Javier,
Vidal Cecilio J.
Publication year - 1997
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.1471-4159.1997.69051964.x
Subject(s) - acetylcholinesterase , sarcolemma , biology , aché , biochemistry , glycosylation , vesicle , anatomy , membrane , chemistry , enzyme
The distribution and glycosylation of acetylcholinesterase (AChE) forms in vesicles derived from sarcoplasmic reticulum of normal muscle (NMV) were investigated and compared with those from dystrophic muscle vesicles (DMV). AChE activity was similar in NMV and DMV. Most of the AChE in NMV and half in DMV were released with Triton X‐100. Asymmetric (A 12 ) and globular hydrophilic and amphiphilic (G H 4 , G A 4 , G A 2 , and G A 1 ) AChE species occurred in NMV and DMV, the lighter forms being predominant. The percentage of G H 4 and G A 4 decreased in DMV. A fraction of the AChE that could not be extracted with detergent was detached with collagenase. Most of the detergent‐released A 12 AChE from NMV and nearly half in DMV failed to bind to Ricinus communis agglutinin (RCA‐I). Conversely, the collagenase‐detached isoforms bound to RCA, revealing that asymmetric AChE associated with internal membranes or basal lamina differed in glycosylation. Moreover, nearly half of G A 4 AChE in DMV and a few in NMV bound to RCA. Most of the RCA‐unreactive G A 4 forms in NMV come from sarcolemma. The results indicate that dystrophy induces minor changes in the distribution and glycosylation of AChE forms in internal membranes of muscle.