Analysis of muscle proteins in acute quadriplegic myopathy

• Published in: Muscle & nerve Vol. 23; no. 8; pp. 1270 - 1276
• Main Authors: Matsumoto, Nobuko, Nakamura, Takeshi, Yasui, Yoshie, Torii, Junzo
• Format: Journal Article
• Language: English
• Published: New York John Wiley & Sons, Inc 01.08.2000; Wiley
• Subjects: actin; Actins - analysis; acute quadriplegic myopathy; Adult; Biological and medical sciences; Biopsy; Diseases of striated muscles. Neuromuscular diseases; Female; Humans; Male; Medical sciences; Microscopy, Electron; Middle Aged; Muscle Proteins - analysis; Muscle, Skeletal - chemistry; Muscle, Skeletal - pathology; Muscular Diseases - etiology; Muscular Diseases - pathology; Myofibrils - chemistry; Myofibrils - pathology; Myofibrils - ultrastructure; myosin; Myosin Heavy Chains - analysis; Neurology; Neuromuscular Diseases - pathology; Quadriplegia - etiology; Quadriplegia - pathology; skeletal muscle; Status Asthmaticus - complications; Tropomyosin - analysis; troponin; Human; Immunohistochemistry; Stoichiometry; Nervous system diseases; Neuromuscular diseases; Purine nucleoside; Motor system disorder; Fast striated muscle; Muscular fiber; Protein; Striated muscle disease; Paraplegia; Troponin; Actin; Myosin; Neurological disorder; Myopathy
• ISSN: 0148-639X; 1097-4598
• DOI: 10.1002/1097-4598(200008)23:8<1270::AID-MUS18>3.0.CO;2-E

We investigated the changes of muscle proteins in acute quadriplegic myopathy (AQM) using immunohistochemistry and stoichiometry. Cases of AQM were observed in which it was difficult to type muscle fibers with adenosine triphosphatase staining in biopsied muscle. Well‐defined typing of these cases was possible by performing immunofluorescent staining using slow and fast skeletal troponin I (TnI) antibodies. By this means, small angular fibers were shown to be fast skeletal muscle, and myosin was absent from these muscle fibers. Actin and tropomyosin were maintained. Muscle protein ratios were determined by stoichiometry following sodium dodecyl sulfate–polyacrylamide gel electrophoresis of AQM myofibril specimens from four subjects. The myosin heavy chain/actin ratio was significantly decreased compared with a normal control group and other neuromuscular diseases. These pathologic findings returned to normal during recovery from AQM. Thus, myosin selectively decreases, whereas actin and regulatory proteins located above it are maintained during AQM. © 2000 John Wiley & Sons, Inc. Muscle Nerve 23: 1270–1276, 2000