Coexpression of myosin isoforms in muscle of patients with neurogenic disease.

Abstract

Three well-characterized antimyosin heavy chain monoclonal antibodies (McAbs) were used as immunocytochemical reagents to study myosin isoform expression in relationship to adenosine triphosphatase (ATPase) defined fiber types in human muscle. The biopsy specimens were from patients with neurogenic muscle disease whose muscle exhibited fiber type grouping and group atrophy. The use of McAbs revealed heretofore unrecognized coexpression of multiple myosin isoforms in selected fibers in the pathologic samples which was not apparent with ATPase reactions and not present in normal muscle. The fibers containing multiple myosin isoforms were probably undergoing neurally directed fiber type transformation. Furthermore, a small population of fibers in neurogenic specimens expressed a "prenatal" myosin signifying the presence of regenerating fibers. We also demonstrated immunocytochemical evidence of the persistence of adult slow myosin in denervated mature human skeletal muscle despite the reputed necessity of innervation for maintenance of expression of this myosin isoform proffered by others.