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

JOURNAL OF BIOMECHANICS

卷:48

Article

Chapman, Mark A.¹  Pichika, Rajeswari²  Lieber, Richard L.^1,2,3 

[1] Univ Calif San Diego, Dept Bioengn, La Jolla, CA 92093 USA

[2] Univ Calif San Diego, Dept Orthopaed Surg, La Jolla, CA 92093 USA

[3] Dept Vet Affairs, La Jolla, CA 92093 USA

关键词: Muscle;    Fibrosis;    Collagen crosslinking;    Extracellular matrix;    Mechanical properties;   

DOI  :  10.1016/j.jbiomech.2014.12.005

来源: Elsevier

【 摘 要 】

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. Published by Elsevier Ltd.

【 授权许可】

Free