ISSLS prize winner: Adaptations to the multifidus muscle in response to experimentally induced intervertebral disc degeneration
Brown SH, Gregory DE, Carr JA, Ward SR, Masuda K, Lieber RL.
Spine, 2011 36(21):1728-36. Epub 2011 Feb 4.
Spine, 2011 36(21):1728-36. Epub 2011 Feb 4.
Abstract:
Study Design: Basic science study of the rabbit multifidus muscle's response to intervertebral disc degeneration.
Objective: To assess changes in passive mechanical properties, associated protein structure, and histology of multifidus in response to disc degeneration produced by experimental needle puncture.
Summary of Background Data: Relationships have been reported between muscle dysfunction and low back injury; however, little is known about the cause and effect of such relationships.
Methods: 12 rabbits were studied; 4 in each of 3 groups: control, 4-weeks post-intervertebral disc injury (4-week disc degeneration), and 12-weeks post-intervertebral disc injury (12-week disc degeneration). Single multifidus fibers and bundles of fibers were isolated and tested for slack sarcomere length and elastic modulus. Titin isoform mass, myosin heavy chain distribution, and muscle histology were also examined.
Results: Compared to control, individual muscle fibers were 34% stiffer and fiber bundles 107% stiffer in the 12-week disc degeneration group. No changes were detected at 4-weeks disc degeneration. No statistically significant change was found for MHC distribution in the 12-week disc degeneration group when compared to control, while titin isoforms were larger (p < 0.05) in the 12-week disc degeneration group. Histology revealed select regions of multifidus, at 12-weeks disc degeneration, with increased space between bundles of fibers which in some instances was partly occupied by adipose tissue.
Conclusions: Multifidus becomes stiffer, both in individual fibers and fiber bundles, in response to experimentally-induced intervertebral disc degeneration. This cannot be explained by change in fiber-type due to reduced muscle use, nor by the increased size of the protein titin (which would reduce stiffness). We hypothesize that fiber bundles become stiffer by proliferation and/or re-organization of collagen content within the muscle but the basis for fiber stiffening is not known.
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Objective: To assess changes in passive mechanical properties, associated protein structure, and histology of multifidus in response to disc degeneration produced by experimental needle puncture.
Summary of Background Data: Relationships have been reported between muscle dysfunction and low back injury; however, little is known about the cause and effect of such relationships.
Methods: 12 rabbits were studied; 4 in each of 3 groups: control, 4-weeks post-intervertebral disc injury (4-week disc degeneration), and 12-weeks post-intervertebral disc injury (12-week disc degeneration). Single multifidus fibers and bundles of fibers were isolated and tested for slack sarcomere length and elastic modulus. Titin isoform mass, myosin heavy chain distribution, and muscle histology were also examined.
Results: Compared to control, individual muscle fibers were 34% stiffer and fiber bundles 107% stiffer in the 12-week disc degeneration group. No changes were detected at 4-weeks disc degeneration. No statistically significant change was found for MHC distribution in the 12-week disc degeneration group when compared to control, while titin isoforms were larger (p < 0.05) in the 12-week disc degeneration group. Histology revealed select regions of multifidus, at 12-weeks disc degeneration, with increased space between bundles of fibers which in some instances was partly occupied by adipose tissue.
Conclusions: Multifidus becomes stiffer, both in individual fibers and fiber bundles, in response to experimentally-induced intervertebral disc degeneration. This cannot be explained by change in fiber-type due to reduced muscle use, nor by the increased size of the protein titin (which would reduce stiffness). We hypothesize that fiber bundles become stiffer by proliferation and/or re-organization of collagen content within the muscle but the basis for fiber stiffening is not known.
Full text (pdf)