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dc.creatorHanifi, A
dc.creatorMcCarthy, H
dc.creatorRoberts, S
dc.creatorPleshko, N
dc.date.accessioned2021-01-31T19:08:15Z
dc.date.available2021-01-31T19:08:15Z
dc.date.issued2013-05-22
dc.identifier.issn1932-6203
dc.identifier.issn1932-6203
dc.identifier.doihttp://dx.doi.org/10.34944/dspace/5381
dc.identifier.other23717662 (pubmed)
dc.identifier.urihttp://hdl.handle.net/20.500.12613/5399
dc.description.abstractHyaline cartilage and mechanically inferior fibrocartilage consisting of mixed collagen types are frequently found together in repairing articular cartilage. The present study seeks to develop methodology to identify collagen type and other tissue components using Fourier transform infrared (FTIR) spectral evaluation of matrix composition in combination with multivariate analyses. FTIR spectra of the primary molecular components of repair cartilage, types I and II collagen, and aggrecan, were used to develop multivariate spectral models for discrimination of the matrix components of the tissues of interest. Infrared imaging data were collected from bovine bone, tendon, normal cartilage, meniscus and human repair cartilage tissues, and composition predicted using partial least squares analyses. Histology and immunohistochemistry results were used as standards for validation. Infrared fiber optic probe spectral data were also obtained from meniscus (a tissue with mixed collagen types) to evaluate the potential of this method for identification of collagen type in a minimally-invasive clinical application. Concentration profiles of the tissue components obtained from multivariate analysis were in excellent agreement with histology and immunohistochemistry results. Bone and tendon showed a uniform distribution of predominantly type I collagen through the tissue. Normal cartilage showed a distribution of type II collagen and proteoglycan similar to the known composition, while in repair cartilage, the spectral distribution of both types I and II collagen were similar to that observed via immunohistochemistry. Using the probe, the outer and inner regions of the meniscus were shown to be primarily composed of type I and II collagen, respectively, in accordance with immunohistochemistry data. In summary, multivariate analysis of infrared spectra can indeed be used to differentiate collagen type I and type II, even in the presence of proteoglycan, in connective tissues, using both imaging and fiber optic methodology. This has great potential for clinical in situ applications for monitoring tissue repair. © 2013 Hanifi et al.
dc.format.extente64822-e64822
dc.language.isoen
dc.relation.haspartPLoS ONE
dc.relation.isreferencedbyPublic Library of Science (PLoS)
dc.rightsCC BY
dc.subjectAnimals
dc.subjectBone and Bones
dc.subjectCartilage
dc.subjectCattle
dc.subjectCollagen
dc.subjectFiber Optic Technology
dc.subjectHumans
dc.subjectMenisci, Tibial
dc.subjectMicroscopy
dc.subjectMultivariate Analysis
dc.subjectSpectroscopy, Fourier Transform Infrared
dc.subjectTendons
dc.titleFourier Transform Infrared Imaging and Infrared Fiber Optic Probe Spectroscopy Identify Collagen Type in Connective Tissues
dc.typeArticle
dc.type.genreJournal Article
dc.relation.doi10.1371/journal.pone.0064822
dc.ada.noteFor Americans with Disabilities Act (ADA) accommodation, including help with reading this content, please contact scholarshare@temple.edu
dc.creator.orcidPleshko, Nancy|0000-0001-8656-3936
dc.date.updated2021-01-31T19:08:11Z
refterms.dateFOA2021-01-31T19:08:16Z


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