title: Skeletal muscle ultrastructure and function in statin-tolerant individuals.
abstract: BACKGROUND
  Statins have well-known benefits on cardiovascular mortality, though up to 15% of patients experience side effects. With guidelines from the American Heart Association, American College of Cardiology, and American Diabetes Association expected to double the number of statin users, the overall incidence of myalgia and myopathy will increase.
  
  
  METHODS
  We evaluated skeletal muscle structure and contractile function at the molecular, cellular, and whole tissue levels in 12 statin tolerant and 12 control subjects.
  
  
  RESULTS
  Myosin isoform expression, fiber type distributions, single fiber maximal Ca(2+) -activated tension, and whole muscle contractile force were similar between groups. No differences were observed in myosin-actin cross-bridge kinetics in myosin heavy chain I or IIA fibers.
  
  
  CONCLUSIONS
  We found no evidence for statin-induced changes in muscle morphology at the molecular, cellular, or whole tissue levels. Collectively, our data show that chronic statin therapy in healthy asymptomatic individuals does not promote deleterious myofilament structural or functional adaptations.
authors.affiliation: Department of Cardiology, University of Vermont Medical Center, Burlington, Vermont, USA.
authors.forename: Jason L
authors.initials: JL
authors.lastname: Rengo
authors.affiliation: Department of Medicine, University of Vermont, College of Medicine, Burlington, Vermont, USA.|Department of Molecular Physiology and Biophysics, University of Vermont, College of Medicine, Burlington, Vermont, USA.
authors.forename: Damien M
authors.initials: DM
authors.lastname: Callahan
authors.affiliation: Department of Cardiology, University of Vermont Medical Center, Burlington, Vermont, USA.
authors.forename: Patrick D
authors.initials: PD
authors.lastname: Savage
authors.affiliation: Department of Cardiology, University of Vermont Medical Center, Burlington, Vermont, USA.|Department of Medicine, University of Vermont, College of Medicine, Burlington, Vermont, USA.
authors.forename: Philip A
authors.initials: PA
authors.lastname: Ades
authors.affiliation: Department of Medicine, University of Vermont, College of Medicine, Burlington, Vermont, USA.|Department of Molecular Physiology and Biophysics, University of Vermont, College of Medicine, Burlington, Vermont, USA.
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Toth
mesh_terms: D000199:Actins / Q000378:metabolism; D000368:Aged; D000369:Aged, 80 and over; D001823:Body Composition / Q000187:drug effects; D015331:Cohort Studies; D003430:Cross-Sectional Studies; D004305:Dose-Response Relationship, Drug; D005260:Female; D006801:Humans; D019161:Hydroxymethylglutaryl-CoA Reductase Inhibitors / Q000378:metabolism / Q000494:pharmacology*; D007717:Knee / Q000294:innervation; D008297:Male; D009119:Muscle Contraction / Q000187:drug effects; D018485:Muscle Fibers, Skeletal / Q000187:drug effects / Q000648:ultrastructure; D018482:Muscle, Skeletal / Q000187:drug effects* / Q000378:metabolism / Q000648:ultrastructure*; D018995:Myosin Heavy Chains / Q000378:metabolism
chemical_list: D000199:Actins; D019161:Hydroxymethylglutaryl-CoA Reductase Inhibitors; D018995:Myosin Heavy Chains
keywords: myalgia; myopathy; skeletal muscle; statin; ultrastructure