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Article: Collagen fibril stiffening in osteoarthritic cartilage of human beings revealed by atomic force microscopy

TitleCollagen fibril stiffening in osteoarthritic cartilage of human beings revealed by atomic force microscopy
Authors
KeywordsArticular cartilage
Atomic force microscopy
Collagen fibril
Nanoindentation
Osteoarthritis
Issue Date2012
PublisherWB Saunders Co Ltd. The Journal's web site is located at http://www.elsevier.com/locate/joca
Citation
Osteoarthritis And Cartilage, 2012, v. 20 n. 8, p. 916-922 How to Cite?
AbstractObjective: This study aimed to characterize the in-situ mechanical property and morphology of individual collagen fibril in osteoarthritic cartilage using indentation-type atomic force microscopy (IT-AFM). Methods: The specimens with intact articular cartilage (AC), mild to severe degenerated cartilage from osteoarthritis (OA) were collected with informed consent from the postmenopausal women who underwent hip or knee arthroplasty. The fresh specimens were cryo-sectioned by layers with 50 μm thick for each from the articular surface to calcified cartilage, and then processed for AFM imaging and nanoindentation test. For each layer, a total of 20 collagen fibrils were randomly selected for testing. AFM tips with the nominal radius less than 10. nm were employed for probing the individual collagen fibril, and the obtained cantilever deflection signal and displacement were recorded for calculating its elastic modulus. Results: An intact AC exhibited a gradation in elastic modulus of collagen fibrils from articular surface (2.65 ± 0.31. GPa) to the cartilage-bone interface (3.70 ± 0.44. GPa). It was noted in mildly degenerated OA cartilage that the coefficient of variation for mechanical properties of collagen fibers, ranging from 25% to 48%, significantly increased as compared with intact one (12%). The stiffened collagen fibrils occurred at either articular surface (3.11 ± 0.91. GPa) or the cartilage-bone interface (5.64 ± 1.10. GPa), accompanied by loosely organized meshwork with advancement of OA cartilage degeneration. It was echoed by histological findings of OA cartilage, including fibrotic changes of surface region and tidemark irregularities. Conclusion: The stiffened collagen fibrils in AC occurred with OA onset and progression, not only at articular surface but also the cartilage-bone interface. © 2012 Osteoarthritis Research Society International.
Persistent Identifierhttp://hdl.handle.net/10722/152715
ISSN
2015 Impact Factor: 4.535
2015 SCImago Journal Rankings: 1.901
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWen, CYen_HK
dc.contributor.authorWu, CBen_HK
dc.contributor.authorTang, Ben_HK
dc.contributor.authorWang, Ten_HK
dc.contributor.authorYan, CHen_HK
dc.contributor.authorLu, WWen_HK
dc.contributor.authorPan, Hen_HK
dc.contributor.authorHu, Yen_HK
dc.contributor.authorChiu, KYen_HK
dc.date.accessioned2012-07-16T09:46:53Z-
dc.date.available2012-07-16T09:46:53Z-
dc.date.issued2012en_HK
dc.identifier.citationOsteoarthritis And Cartilage, 2012, v. 20 n. 8, p. 916-922en_HK
dc.identifier.issn1063-4584en_HK
dc.identifier.urihttp://hdl.handle.net/10722/152715-
dc.description.abstractObjective: This study aimed to characterize the in-situ mechanical property and morphology of individual collagen fibril in osteoarthritic cartilage using indentation-type atomic force microscopy (IT-AFM). Methods: The specimens with intact articular cartilage (AC), mild to severe degenerated cartilage from osteoarthritis (OA) were collected with informed consent from the postmenopausal women who underwent hip or knee arthroplasty. The fresh specimens were cryo-sectioned by layers with 50 μm thick for each from the articular surface to calcified cartilage, and then processed for AFM imaging and nanoindentation test. For each layer, a total of 20 collagen fibrils were randomly selected for testing. AFM tips with the nominal radius less than 10. nm were employed for probing the individual collagen fibril, and the obtained cantilever deflection signal and displacement were recorded for calculating its elastic modulus. Results: An intact AC exhibited a gradation in elastic modulus of collagen fibrils from articular surface (2.65 ± 0.31. GPa) to the cartilage-bone interface (3.70 ± 0.44. GPa). It was noted in mildly degenerated OA cartilage that the coefficient of variation for mechanical properties of collagen fibers, ranging from 25% to 48%, significantly increased as compared with intact one (12%). The stiffened collagen fibrils occurred at either articular surface (3.11 ± 0.91. GPa) or the cartilage-bone interface (5.64 ± 1.10. GPa), accompanied by loosely organized meshwork with advancement of OA cartilage degeneration. It was echoed by histological findings of OA cartilage, including fibrotic changes of surface region and tidemark irregularities. Conclusion: The stiffened collagen fibrils in AC occurred with OA onset and progression, not only at articular surface but also the cartilage-bone interface. © 2012 Osteoarthritis Research Society International.en_HK
dc.languageengen_US
dc.publisherWB Saunders Co Ltd. The Journal's web site is located at http://www.elsevier.com/locate/jocaen_HK
dc.relation.ispartofOsteoarthritis and Cartilageen_HK
dc.subjectArticular cartilageen_HK
dc.subjectAtomic force microscopyen_HK
dc.subjectCollagen fibrilen_HK
dc.subjectNanoindentationen_HK
dc.subjectOsteoarthritisen_HK
dc.subject.meshAdulten_HK
dc.subject.meshAgeden_HK
dc.subject.meshCartilage, Articular - ultrasonographyen_HK
dc.subject.meshFemaleen_HK
dc.subject.meshFibrillar Collagens - ultrastructureen_HK
dc.subject.meshHumansen_HK
dc.subject.meshMicroscopy, Atomic Force - methodsen_HK
dc.subject.meshMiddle Ageden_HK
dc.subject.meshOsteoarthritis, Knee - pathologyen_HK
dc.subject.meshPostmenopauseen_HK
dc.subject.meshStress, Mechanicalen_HK
dc.titleCollagen fibril stiffening in osteoarthritic cartilage of human beings revealed by atomic force microscopyen_HK
dc.typeArticleen_HK
dc.identifier.emailTang, B: tangbin@hkucc.hku.hken_HK
dc.identifier.emailPan, H: haobo@hku.hken_HK
dc.identifier.emailHu, Y: yhud@hku.hken_HK
dc.identifier.authorityTang, B=rp00081en_HK
dc.identifier.authorityPan, H=rp01564en_HK
dc.identifier.authorityHu, Y=rp00432en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1016/j.joca.2012.04.018en_HK
dc.identifier.pmid22548795-
dc.identifier.scopuseid_2-s2.0-84862989410en_HK
dc.identifier.hkuros200616en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-84862989410&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume20en_HK
dc.identifier.issue8en_HK
dc.identifier.spage916en_HK
dc.identifier.epage922en_HK
dc.identifier.isiWOS:000306988000014-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridWen, CY=36731630800en_HK
dc.identifier.scopusauthoridWu, CB=55232883300en_HK
dc.identifier.scopusauthoridTang, B=24554184100en_HK
dc.identifier.scopusauthoridWang, T=11840122500en_HK
dc.identifier.scopusauthoridYan, CH=54934787000en_HK
dc.identifier.scopusauthoridLu, WW=54989091200en_HK
dc.identifier.scopusauthoridPan, H=7403295092en_HK
dc.identifier.scopusauthoridHu, Y=7407116091en_HK
dc.identifier.scopusauthoridChiu, KY=34967948100en_HK

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