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Skeletal muscle acetylcholinesterase molecular forms in amyotrophic lateral sclerosis
Author(s) -
Fernandez Hugo L.,
Stiles Joel R.,
Donoso J. Alejandro
Publication year - 1986
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.880090504
Subject(s) - acetylcholinesterase , amyotrophic lateral sclerosis , aché , motor endplate , anatomy , endoplasmic reticulum , intracellular , chemistry , extracellular , biology , medicine , neuromuscular junction , biochemistry , neuroscience , enzyme , disease
Acetylcholinesterase (AChE) molecular forms in muscle biopsies from control and amyotrophic lateral sclerosis (ALS) patients were extracted under low (G: globular forms) and high (A: asymmetric forms) ionic strength conditions and were evaluated by velocity sedimentation analysis. Total AChE activity in endplate‐containing ALS muscle sections was reduced by an average of 65% of control muscle levels. This decrement resulted from an almost complete disappearance of 9.5S (G4) and 8.0S (A4) AChE and significant decreases in the 3.8S (G1), 12.1S (A8), and 15.8S (A12) forms (66%, 9%, and 25% of control, respectively). In most of the ALS biopsies examined, ultrastructural‐cytochemical analysis revealed large reductions in AChE reaction product of both synaptic infoldings (extracellular) and sarcoplasmic reticulum (intracellular) of the muscles' motor endplate regions. These data are compatible with the view that alterations observed in AChE forms from ALS muscles are related to disturbances in the normal “trophic” interactions between nerve and muscle.