Format

Send to

Choose Destination
J Biomech. 2015 Jan 21;48(2):375-8. doi: 10.1016/j.jbiomech.2014.12.005. Epub 2014 Dec 10.

Collagen crosslinking does not dictate stiffness in a transgenic mouse model of skeletal muscle fibrosis.

Author information

1
Department of Bioengineering, University of California San Diego, 9500 Gilman Drive, La Jolla, CA, 92093-0863, USA.
2
Department of Orthopaedic Surgery, University of California San Diego, 9500 Gilman Drive, La Jolla, CA, 92093-0863, USA.
3
Department of Bioengineering, University of California San Diego, 9500 Gilman Drive, La Jolla, CA, 92093-0863, USA; Department of Orthopaedic Surgery, University of California San Diego, 9500 Gilman Drive, La Jolla, CA, 92093-0863, USA; Department of Veteran׳s Affairs, 9500 Gilman Drive, La Jolla, CA, 92093-0863, USA. Electronic address: rlieber@ric.org.

Abstract

Skeletal muscle fibrosis is characterized by increases in tissue stiffness and collagen content. However, a very weak correlation exists between collagen content and stiffness in skeletal muscle. Recently, it has been hypothesized that collagen crosslinking explains tissue stiffness in fibrotic skeletal muscle. Therefore, we addressed this hypothesis by correlating tissue stiffness with lysyl-pyridinoline, hydroxylysyl-pyridinoline, and pentosidine collagen crosslinks. Stepwise regression revealed that, separate or together, collagen crosslinks did not correlate with tissue stiffness. Our result demonstrates that increased tissue stiffness in skeletal muscle fibrosis is not simply explained by increased collagen crosslinks and/or collagen crosslink density. We suggest that collagen organization may affect tissue stiffness.

KEYWORDS:

Collagen crosslinking; Extracellular matrix; Fibrosis; Mechanical properties; Muscle

PMID:
25529136
PMCID:
PMC4286487
DOI:
10.1016/j.jbiomech.2014.12.005
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center