期刊
ACS NANO
卷 13, 期 10, 页码 11320-11333出版社
AMER CHEMICAL SOC
DOI: 10.1021/acsnano.9b04477
关键词
articular cartilage; extracellular matrix; proteoglycan; decorin; molecular assembly; nanomechanics; poroelasticity
类别
资金
- National Institutes of Health (NIH) [AR066824]
- National Science Foundation (NSF) [CMMI-1662544]
- NIH [P30 AR069619]
Joint biomechanical functions rely on the integrity of cartilage extracellular matrix. Understanding the molecular activities that govern cartilage matrix assembly is critical for developing effective cartilage regeneration strategies. This study elucidated the role of decorin, a small leucine-rich proteoglycan, in 20 the structure and biomechanical functions of cartilage. In decorin- null cartilage, we discovered a substantial reduction of aggrecan content, the major proteoglycan of cartilage matrix, and mild changes in collagen fibril nanostructure. This loss of aggrecan resulted in significantly impaired biomechanical properties of cartilage, including decreased modulus, elevated hydraulic permeability, and reduced energy dissipation capabilities. At the cellular level, we found that decorin functions to increase the retention of aggrecan in the neo-matrix of chondrocytes, rather than to directly influence the biosynthesis of aggrecan. At the molecular level, we demonstrated that decorin significantly increases the adhesion between aggrecan and aggrecan molecules and between aggrecan molecules and collagen II fibrils. We hypothesize that decorin plays a crucial structural role in mediating the matrix integrity and biomechanical functions of cartilage by providing physical linkages to increase the adhesion and assembly of aggrecan molecules at the nanoscale.
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