The role of collagen crosslinking in the increased stiffness of avian dystrophic muscle

Muscle Nerve. 1989 Jun;12(6):486-92. doi: 10.1002/mus.880120609.

Abstract

The resting tension and stiffness in the range of sarcomere lengths 2.4-3.6 microns were studied in highly inbred normal and dystrophic chicken pectoral muscle bundles, and the results were compared with the collagen content and the extent of crosslinkage of the collagen. All parameters increased in the order normal homozygote (003/003) less than heterozygote (003/433) less than dystrophic homozygote (433/433) chickens, with the data from the heterozygotes being halfway between the two homozygotes, thus exhibiting a semi-dominant inheritance pattern. In separate experiments, lathyrism was induced by treating normal (412/412) and dystrophic (413/413) chickens with alpha-acetoaminonitrile, an inhibitor of lysyl oxydase, the enzyme responsible for the initiation of collagen crosslinkage formation. These experiments showed that the tension and stiffness in response to passive stretch did not change with lathyrism in normal muscles, whereas the tension and stiffness decreased significantly with lathyrism in dystrophic muscles. The collagen content did not change with lathryrism in both normal and dystrophic muscles. These results indicate that the increased content of collagen crosslinkages is the basis for the increased resting tension and stiffness in the dystrophic muscles of the chicken, and that the effects can be reversed by treatment with an inhibitor of collagen crosslinkage formation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biomechanical Phenomena
  • Chickens
  • Collagen / metabolism*
  • Lathyrism / metabolism
  • Muscles / metabolism
  • Muscles / physiopathology*
  • Muscular Dystrophy, Animal / metabolism
  • Muscular Dystrophy, Animal / physiopathology*

Substances

  • Collagen