Correlation between myofibrillar ATPase activity and myosin heavy chain composition in single human muscle fibers.
Single human muscle fibers were analysed using a combination of histochemical and biochemical techniques. Routine myofibrillar adenosine triphosphatase (mATPase) histochemistry revealed a continuum of staining intensities between the fast fiber types IIA and IIB (type IIAB fibers) after preincubation at pH 4.6. Electrophoretic analysis of single, histochemically-identified fibers demonstrated a correlation between the staining intensity and the myosin heavy chain (MHC) composition. All fibers classified as type I contained exclusively MHCI and all type IIA fibers contained only MHCIIa. Type IIAB fibers displayed variable amounts of both MHCIIa and MHCIIb; the greater the staining intensity of these fibers after preincubation at pH 4.6, the greater the percentage of MHCIIb. Those fibers histochemically classified as type IIB contained either entirely MHCIIb or, in addition to MHCIIb, a small amount of MHCIIa. These data establish a correlation between the mATPase activity and MHC content in single human muscle fibers.
Staron
R S
RS
Department of Zoological and Biomedical Sciences, College of Osteopathic Medicine, Ohio University, Athens 45701.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006651:Histocytochemistry; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008297:Male; D009132:Muscles / Q000737:chemistry* / Q000201:enzymology / Q000502:physiology; D009210:Myofibrils / Q000201:enzymology; D009218:Myosins / Q000032:analysis*; D012680:Sensitivity and Specificity
D000251:Adenosine Triphosphatases; D009218:Myosins