Histological characterization and biochemical analysis of paraspinal muscles in neuromuscularly healthy subjects

Muscle Nerve. 2015 Jul;52(1):45-54. doi: 10.1002/mus.24490. Epub 2015 May 28.

Abstract

Introduction: There are no generally accepted histopathological reference values in paraspinal skeletal muscle biopsies.

Methods: We examined multifidii muscle biopsies from 20 neuromuscularly healthy subjects using routine histological stains and biochemical analyses of respiratory chain enzymes.

Results: Staining showed incomplete myopathic features, such as increased variability in fiber size, type 1 hypertrophy, rounded fiber shape, endomysial fibrosis, and replacement by adipose tissue. Acid phosphatase reaction was positive in up to 35% of the selected muscle fibers. Mitochondrial changes were obvious but revealed no selective age dependence. Reduced complex I, cytochrome c oxidase (COX), and citrate synthase (CS) could be observed.

Conclusions: Because the increased variability in morphological details can easily be misinterpreted as myopathic changes, analysis of paraspinal muscles should take into consideration that incomplete myopathic features and reduced oxidative enzyme activities for complex I, COX, and CS are normal variations at this location.

Keywords: camptocormia; immunohistochemistry; limb muscles; mitochondrial disease; myopathy; paravertebral muscles.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Aged
  • Electron Transport Complex I / metabolism
  • Electron Transport Complex IV / metabolism
  • Female
  • Humans
  • Male
  • Middle Aged
  • Muscle Fibers, Skeletal* / classification
  • Muscle Fibers, Skeletal* / cytology
  • Muscle Fibers, Skeletal* / metabolism
  • NAD / metabolism
  • Paraspinal Muscles / enzymology*
  • Paraspinal Muscles / pathology
  • Succinate Dehydrogenase / metabolism

Substances

  • NAD
  • Succinate Dehydrogenase
  • Electron Transport Complex IV
  • Adenosine Triphosphatases
  • Electron Transport Complex I