Type III collagen is a key regulator of the collagen fibrillar structure and biomechanics of articular cartilage and meniscus

纤维发生 弯月面 Ⅰ型胶原 纤维 胶原蛋白,I型,α1 解剖 II型胶原 胶原纤维 软骨 细胞外基质 软骨细胞 机械转化 化学 基质(化学分析) 生物物理学 细胞生物学 骨关节炎 医学 病理 生物 物理 生物化学 入射(几何) 替代医学 光学 色谱法
作者
Chao Wang,Becky K. Brisson,Masahiko Terajima,Qing Li,Kevt’her Hoxha,Biao Han,Abby Goldberg,X. Sherry Liu,Michele Marcolongo,Motomi Enomoto‐Iwamoto,Mitsuo Yamauchi,Susan W. Volk,Lin Han
出处
期刊:Matrix Biology [Elsevier]
卷期号:85-86: 47-67 被引量:85
标识
DOI:10.1016/j.matbio.2019.10.001
摘要

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.
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