Skeletal muscle acetylcholinesterase molecular forms in amyotrophic lateral sclerosis.
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.
D000110:Acetylcholinesterase / Q000378:metabolism*; D000328:Adult; D000368:Aged; D000690:Amyotrophic Lateral Sclerosis / Q000201:enzymology*; D005260:Female; D006651:Histocytochemistry; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism*; D008297:Male; D008875:Middle Aged; D009045:Motor Endplate / Q000201:enzymology; D009132:Muscles / Q000201:enzymology*; D009469:Neuromuscular Junction / Q000201:enzymology; D011487:Protein Conformation; D012519:Sarcoplasmic Reticulum / Q000201:enzymology
D007527:Isoenzymes; D000110:Acetylcholinesterase