Regional variations in the distribution and colocalization of extracellular matrix proteins in the juvenile bovine meniscus

Authors

  • Eric J. Vanderploeg,

    1. George W. Woodruff School of Mechanical Engineering, Georgia Institute of Technology, Atlanta, GA, USA
    2. Parker H. Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GA, USA
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    • These authors contributed equally to this work.

  • Christopher G. Wilson,

    1. Wallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology, Atlanta, GA, USA
    2. Parker H. Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GA, USA
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    • These authors contributed equally to this work.

  • Stacy M. Imler,

    1. George W. Woodruff School of Mechanical Engineering, Georgia Institute of Technology, Atlanta, GA, USA
    2. Parker H. Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GA, USA
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  • Carrie Hang-Yin Ling,

    1. Department of Mechanical Engineering, Stanford University, Stanford, CA, USA
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  • Marc E. Levenston

    1. Department of Mechanical Engineering, Stanford University, Stanford, CA, USA
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Marc E. Levenston, Department of Mechanical Engineering, Biomechanical Engineering, 233 Durand Building, Stanford, CA 94305-4038, USA. T: + 1 650 7239464; F: + 650 725 1587; E:levenston@stanford.edu

Abstract

A deeper understanding of the composition and organization of extracellular matrix molecules in native, healthy meniscus tissue is required to fully appreciate the degeneration that occurs in joint disease and the intricate environment in which an engineered meniscal graft would need to function. In this study, regional variations in the tissue-level and pericellular distributions of collagen types I, II and VI and the proteoglycans aggrecan, biglycan and decorin were examined in the juvenile bovine meniscus. The collagen networks were extensively, but not completely, colocalized, with tissue-level organization that varied with radial position across the meniscus. Type VI collagen exhibited close association with large bundles composed of type I and II collagen and, in contrast to type I and II collagen, was further concentrated in the pericellular matrix. Aggrecan was detected throughout the inner region of the meniscus but was restricted to the pericellular matrix and sheaths of collagen bundles in the middle and outer regions. The small proteoglycans biglycan and decorin exhibited regional variations in staining intensity but were consistently localized in the intra- and/or peri-cellular compartments. These results provide insight into the complex hierarchy of extracellular matrix organization in the meniscus and provide a framework for better understanding meniscal degeneration and disease progression and evaluating potential repair and regeneration strategies.

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