title: Histochemical, biochemical, and ultrastructural analyses of single human muscle fibers, with special reference to the C-fiber population.
abstract: A muscle biopsy from the vastus lateralis muscle of a strength-trained woman was found to contain an unusual fiber type composition and was analyzed by histochemical, biochemical, and ultrastructural techniques. Special attention was given to the C-fibers, which comprised over 15% of the total fiber number in the biopsy. The mATPase activity of the C-fibers remained stable to varying degrees over the pH range normally used for routine mATPase histochemistry. Although a continuum existed, the C-fibers were histochemically subdivided into three main fiber types: IC, IIC, and IIAC. The IC fibers were histochemically more similar to the Type I, the IIAC were more similar to the Type IIA, and the IIC were darkly stained throughout the pH range. Biochemical analysis revealed that all C-fibers coexpressed myosin heavy chains (MHC) I and IIa in variable ratios. The histochemical staining intensity correlated with the myosin heavy chain composition such that the Type IC fibers contained a greater ratio of MHCI/MHCIIa, the IIAC contained a greater ratio of MHCIIa/MHCI, and the Type IIC contained equal amounts of these two heavy chains. Ultrastructural data of the C-fiber population revealed an oxidative capacity between fiber Types I and IIA and suggested a range of mitochondrial volume percent from highest to lowest such that I greater than IC greater than IIC greater than IIA-C greater than IIA. Under physiological conditions, it appears that the IC fibers represent Type I fibers that additionally express some fast characteristics, whereas the Type IIAC are Type IIA fibers that additionally express some slow characteristics. Fibers expressing a 50:50 mixture of MHCI and MHCIIa (IIC fibers) were rarely found. It is not known whether C-fibers represent a distinct population between the fast- and slow-twitch fibers that is specifically adapted to a particular usage or whether they are transforming fibers in the process of going from fast to slow or slow to fast.
authors.affiliation: Department of Zoological & Biomedical Sciences, Ohio University, Athens 45701.
authors.forename: R S
authors.initials: RS
authors.lastname: Staron
authors.forename: R S
authors.initials: RS
authors.lastname: Hikida
mesh_terms: D000328:Adult; D001706:Biopsy; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D009132:Muscles / Q000166:cytology* / Q000648:ultrastructure; D015879:Myosin Subfragments / Q000032:analysis*
chemical_list: D015879:Myosin Subfragments