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Journal article
Type III collagen is a key regulator of the collagen fibrillar structure and biomechanics of articular cartilage and meniscus
Matrix biology, v 85-86
Jan 2020
PMID: 31655293
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Despite the fact that type III collagen is the second most abundant collagen type in the body, its contribution to the physiologic maintenance and repair of skeletal tissues remains poorly understood. This study queried the role of type III collagen in the structure and biomechanical functions of two structurally distinctive tissues in the knee joint, type II collagen-rich articular cartilage and type I collagen-dominated meniscus. Integrating outcomes from atomic force microscopy-based nanomechanical tests, collagen fibril nanostructural analysis, collagen cross-link analysis and histology, we elucidated the impact of type III collagen haplodeficiency on the morphology, nanostructure and biomechanical properties of articular cartilage and meniscus in Col3a1+/− mice. Reduction of type III collagen leads to increased heterogeneity and mean thickness of collagen fibril diameter, as well as reduced modulus in both tissues, and these effects became more pronounced with skeletal maturation. These data suggest a crucial role of type III collagen in mediating fibril assembly and biomechanical functions of both articular cartilage and meniscus during post-natal growth. In articular cartilage, type III collagen has a marked contribution to the micromechanics of the pericellular matrix, indicating a potential role in mediating the early stage of type II collagen fibrillogenesis and chondrocyte mechanotransduction. In both tissues, reduction of type III collagen leads to decrease in tissue modulus despite the increase in collagen cross-linking. This suggests that the disruption of matrix structure due to type III collagen deficiency outweighs the stiffening of collagen fibrils by increased cross-linking, leading to a net negative impact on tissue modulus. Collectively, this study is the first to highlight the crucial structural role of type III collagen in both articular cartilage and meniscus extracellular matrices. We expect these results to expand our understanding of type III collagen across various tissue types, and to uncover critical molecular components of the microniche for regenerative strategies targeting articular cartilage and meniscus repair.
•Collagen III regulates fibril structure and mechanics in both collagen II-rich cartilage and collagen I-dominated meniscus.•Collagen III affects the aggrecan network compression possibly by mediating the aggrecan and collagen network integration.•Collagen III regulates cartilage pericellular matrix micromechanics, potentially mediating chondrocyte mechanotransduction.•Disruption of structure due to reduced collagen III outweighs increase in collagen cross-linking, causing reduced modulus.
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Details
- Title
- Type III collagen is a key regulator of the collagen fibrillar structure and biomechanics of articular cartilage and meniscus
- Creators
- Chao Wang - Drexel UniversityBecky K. Brisson - University of PennsylvaniaMasahiko Terajima - University of North Carolina at Chapel HillQing Li - Drexel UniversityKevt’her Hoxha - Drexel UniversityBiao Han - School of Biomedical Engineering, Science and Health Systems, Drexel University, Philadelphia, PA 19104, United StatesAbby M. Goldberg - University of PennsylvaniaX. Sherry Liu - McKay Orthopaedic Research Laboratory, Department of Orthopaedic Surgery, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104, United StatesMichele S. Marcolongo - Drexel UniversityMotomi Enomoto-Iwamoto - University of Maryland, BaltimoreMitsuo Yamauchi - University of North Carolina at Chapel HillSusan W. Volk - University of PennsylvaniaLin Han - Drexel University
- Publication Details
- Matrix biology, v 85-86
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- School of Biomedical Engineering, Science, and Health Systems
- Web of Science ID
- WOS:000528055100004
- Scopus ID
- 2-s2.0-85076244439
- Other Identifier
- 991019168932704721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Cell Biology