TY - JOUR
T1 - Collagen crosslinking does not dictate stiffness in a transgenic mouse model of skeletal muscle fibrosis
AU - Chapman, Mark A.
AU - Pichika, Rajeswari
AU - Lieber, Richard L.
N1 - Funding Information:
Research reported in this publication was supported by the National Institute of Arthritis and Musculoskeletal and Skin Diseases of the National Institutes of Health under Award Numbers AR061303 & T32AR0607 and by the National Institute of Child Health and Human Development under Award Number HD050837 . The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health . We also acknowledge the National Science Foundation for an NSF-Graduate Research Fellowship to MAC.
Publisher Copyright:
© 2014.
PY - 2015/1/21
Y1 - 2015/1/21
N2 - 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.
AB - 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.
KW - Collagen crosslinking
KW - Extracellular matrix
KW - Fibrosis
KW - Mechanical properties
KW - Muscle
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U2 - 10.1016/j.jbiomech.2014.12.005
DO - 10.1016/j.jbiomech.2014.12.005
M3 - Article
C2 - 25529136
AN - SCOPUS:84920282525
SN - 0021-9290
VL - 48
SP - 375
EP - 378
JO - Journal of Biomechanics
JF - Journal of Biomechanics
IS - 2
ER -