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Matrix Biol Plus. 2021 Dec 28;13:100099. doi: 10.1016/j.mbplus.2021.100099. eCollection 2022 Feb.

Coordinate roles for collagen VI and biglycan in regulating tendon collagen fibril structure and function.

Matrix biology plus

Ryan J Leiphart, Hai Pham, Tyler Harvey, Taishi Komori, Tina M Kilts, Snehal S Shetye, Stephanie N Weiss, Sheila M Adams, David E Birk, Louis J Soslowsky, Marian F Young

Affiliations

  1. McKay Orthopedic Research Laboratory, University of Pennsylvania, Philadelphia, PA, USA.
  2. National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892, USA.
  3. Carnegie Institution for Science, Department of Embryology, The Johns Hopkins University, USA.
  4. University of South Florida, Morsani College of Medicine, Tampa, FL 33612, USA.

PMID: 35036900 PMCID: PMC8749075 DOI: 10.1016/j.mbplus.2021.100099

Abstract

Tendon is a vital musculoskeletal tissue that is prone to degeneration. Proper tendon maintenance requires complex interactions between extracellular matrix components that remain poorly understood. Collagen VI and biglycan are two matrix molecules that localize pericellularly within tendon and are critical regulators of tissue properties. While evidence suggests that collagen VI and biglycan interact within the tendon matrix, the relationship between the two molecules and its impact on tendon function remains unknown. We sought to elucidate potential coordinate roles of collagen VI and biglycan within tendon by defining tendon properties in knockout models of collagen VI, biglycan, or both molecules. We first demonstrated co-expression and co-localization of collagen VI and biglycan within the healing tendon, providing further evidence of cooperation between the two molecules during nascent tendon matrix formation. Deficiency in collagen VI and/or biglycan led to significant reductions in collagen fibril size and tendon mechanical properties. However, collagen VI-null tendons displayed larger reductions in fibril size and mechanics than seen in biglycan-null tendons. Interestingly, knockout of both molecules resulted in similar properties to collagen VI knockout alone. These results indicate distinct and non-additive roles for collagen VI and biglycan within tendon. This work provides better understanding of regulatory interactions between two critical tendon matrix molecules.

© 2021 Published by Elsevier B.V.

Keywords: Biglycan; Biomechanics; Collagen VI; Collagen fibrils; Extracellular matrix; Tendon

Conflict of interest statement

The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

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