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Conference Paper: Individual collagen fibrils of osteoarthritic cartilage are mechanically inferior outside in

TitleIndividual collagen fibrils of osteoarthritic cartilage are mechanically inferior outside in
Authors
KeywordsMedical sciences
Orthopedics and traumatology medical sciences
Endocrinology
Issue Date2010
PublisherElsevier Inc.
Citation
The 2010 International Conference on Osteoporosis and Bone Research, Shenzhen, China, 28-31 October 2010. In Bone, 2010, v. 47, suppl. 3, p. S443, abstract no. 349 How to Cite?
AbstractOBJECTIVE: It was reported in Nature Nanotechnology in 2009 that the disruption of collagen fibrils meshwork of articular cartilage could be detected by atomic force microscopy ahead of proteoglycan loss and cartilage erosion in osteoarthritis. Yet few studies have been done on individual collagen fiber although a very recent study suggested that individual collagen fibril disruption triggered the breakdown of the meshwork in osteoarthritis initiation. METHODS: The fresh specimens of articular cartilage were collected with informed consent from postmenopausal women, who underwent arthroplasty due to the end-stage of osteoarthritis (OA) or hip fracture. The articular cartilage from the patients of hip fracture served as age-match control. The fresh specimens were cryo-sectioned by the layers with 500 μm outside in and put for indentation-type atomic force microscope (AFM). AFM was used to image and locate the collagen fibrils for nanoindentation. The tip of the nanoindentator was 10 nm in diameter and the indentation depth was 20 nm. Twenty indentations were performed for each layer of the specimens under ambient condition. RESULTS: In the control group, the Young's modulus of individual collagen fibril in deep layer was significantly higher (2.6± 0.6 GPa) than that in superficial layer (2.2±0.4 GPa, p<0.05). It was echoed by the larger collagen fibril diameter in deep layer. Yet in OA group, the Young's modulus of individual collagen fibril in deep layer was significantly lower (2.4±0.4 GPa) than that in superficial layer (3.1±0.9 GPa, p<0.01). There was no significant difference between the superficial and deep layer of the remaining OA cartilage in the diameter of individual collagen fibril, which spread in a wide range from 80 nm to 240 nm. CONCLUSIONS: The Young's modulus of individual collagen fibrils of cartilage is compatible with the data previously reported. Our findings firstly addressed that individual collagen fibrils of osteoarthritic cartilage are mechanically inferior outside in. The weakened deep layer of OA cartilage might contribute to the progression of articular cartilage erosion.
Persistent Identifierhttp://hdl.handle.net/10722/135310
ISSN
2023 Impact Factor: 3.5
2023 SCImago Journal Rankings: 1.179
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorWu, CBen_US
dc.contributor.authorTang, Ben_US
dc.contributor.authorWen, Cen_US
dc.contributor.authorLu, WWen_US
dc.contributor.authorYan, CHen_US
dc.contributor.authorChiu, Ken_US
dc.date.accessioned2011-07-27T01:33:10Z-
dc.date.available2011-07-27T01:33:10Z-
dc.date.issued2010en_US
dc.identifier.citationThe 2010 International Conference on Osteoporosis and Bone Research, Shenzhen, China, 28-31 October 2010. In Bone, 2010, v. 47, suppl. 3, p. S443, abstract no. 349en_US
dc.identifier.issn8756-3282-
dc.identifier.urihttp://hdl.handle.net/10722/135310-
dc.description.abstractOBJECTIVE: It was reported in Nature Nanotechnology in 2009 that the disruption of collagen fibrils meshwork of articular cartilage could be detected by atomic force microscopy ahead of proteoglycan loss and cartilage erosion in osteoarthritis. Yet few studies have been done on individual collagen fiber although a very recent study suggested that individual collagen fibril disruption triggered the breakdown of the meshwork in osteoarthritis initiation. METHODS: The fresh specimens of articular cartilage were collected with informed consent from postmenopausal women, who underwent arthroplasty due to the end-stage of osteoarthritis (OA) or hip fracture. The articular cartilage from the patients of hip fracture served as age-match control. The fresh specimens were cryo-sectioned by the layers with 500 μm outside in and put for indentation-type atomic force microscope (AFM). AFM was used to image and locate the collagen fibrils for nanoindentation. The tip of the nanoindentator was 10 nm in diameter and the indentation depth was 20 nm. Twenty indentations were performed for each layer of the specimens under ambient condition. RESULTS: In the control group, the Young's modulus of individual collagen fibril in deep layer was significantly higher (2.6± 0.6 GPa) than that in superficial layer (2.2±0.4 GPa, p<0.05). It was echoed by the larger collagen fibril diameter in deep layer. Yet in OA group, the Young's modulus of individual collagen fibril in deep layer was significantly lower (2.4±0.4 GPa) than that in superficial layer (3.1±0.9 GPa, p<0.01). There was no significant difference between the superficial and deep layer of the remaining OA cartilage in the diameter of individual collagen fibril, which spread in a wide range from 80 nm to 240 nm. CONCLUSIONS: The Young's modulus of individual collagen fibrils of cartilage is compatible with the data previously reported. Our findings firstly addressed that individual collagen fibrils of osteoarthritic cartilage are mechanically inferior outside in. The weakened deep layer of OA cartilage might contribute to the progression of articular cartilage erosion.-
dc.languageengen_US
dc.publisherElsevier Inc.-
dc.relation.ispartofBone-
dc.subjectMedical sciences-
dc.subjectOrthopedics and traumatology medical sciences-
dc.subjectEndocrinology-
dc.titleIndividual collagen fibrils of osteoarthritic cartilage are mechanically inferior outside inen_US
dc.typeConference_Paperen_US
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=8756-3282&volume=47, suppl. 3&spage=S443&epage=&date=2010&atitle=Individual+collagen+fibrils+of+osteoarthritic+cartilage+are+mechanically+inferior+outside+in-
dc.identifier.emailTang, B: tangbin@hkucc.hku.hken_US
dc.identifier.emailWen, C: paulwen@hku.hken_US
dc.identifier.emailLu, WW: wwlu@hku.hken_US
dc.identifier.emailYan, CH: yanchoi@hku.hken_US
dc.identifier.emailChiu, K: pkychiu@hkucc.hku.hken_US
dc.identifier.authorityTang, B=rp00081en_US
dc.identifier.authorityLu, WW=rp00411en_US
dc.identifier.authorityYan, CH=rp00303en_US
dc.identifier.authorityChiu, K=rp00379en_US
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.bone.2010.09.297-
dc.identifier.hkuros188848en_US
dc.identifier.volume47en_US
dc.identifier.issuesuppl. 3-
dc.identifier.spageS443, abstract no. 349en_US
dc.identifier.epageS443, abstract no. 349en_US
dc.identifier.isiWOS:000285278200242-
dc.description.otherInternational Conference on Osteoporosis and Bone Research, Shenzhen, China, 28-31 October 2010. In Bone, 2010, v. 47, suppl. 3, p. S443, abstract no. 349-
dc.identifier.issnl1873-2763-

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