Ft-ir Microspectroscopy Of Rat Ear Cartilage

dc.creatorVidal
dc.creatorBD; Mello
dc.creatorMLS
dc.date2016
dc.date2016-12-06T18:32:14Z
dc.date2016-12-06T18:32:14Z
dc.date.accessioned2018-03-29T02:04:49Z
dc.date.available2018-03-29T02:04:49Z
dc.identifier
dc.identifierPlos One. PUBLIC LIBRARY SCIENCE, n. 11, n. 3, p. .
dc.identifier1932-6203
dc.identifierWOS:000372708900036
dc.identifier10.1371/journal.pone.0151989
dc.identifierhttp://journals.plos.org/plosone/article?id=10.1371/journal.pone.0151989
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/320487
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1311253
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionRat ear cartilage was studied using Fourier transform-infrared (FT-IR) microspectroscopy to expand the current knowledge which has been established for relatively more complex cartilage types. Comparison of the FT-IR spectra of the ear cartilage extracellular matrix (ECM) with published data on articular cartilage, collagen II and 4-chondroitin-sulfate standards, as well as of collagen type I-containing dermal collagen bundles (CBs) with collagen type II, was performed. Ear cartilage ECM glycosaminoglycans (GAGs) were revealed histochemically and as a reduction in ECM FT-IR spectral band heights (1140-820 cm(-1)) after testicular hyaluronidase digestion. Although ear cartilage is less complex than articular cartilage, it contains ECM components with a macromolecular orientation as revealed using polarization microscopy. Collagen type II and GAGs, which play a structural role in the stereo-arrangement of the ear cartilage, contribute to its FT-IR spectrum. Similar to articular cartilage, ear cartilage showed that proteoglycans add a contribution to the collagen amide I spectral region, a finding that does not recommend this region for collagen type II quantification purposes. In contrast to articular cartilage, the symmetric stretching vibration of -SO3- groups at 1064 cm-1 appeared under-represented in the FT-IR spectral profile of ear cartilage. Because the band corresponding to the asymmetric stretching vibration of -SO3- groups (1236-1225 cm(-1)) overlapped with that of amide III bands, it is not recommended for evaluation of the -SO3--contribution to the FT-IR spectrum of the ear cartilage ECM. Instead, a peak (or shoulder) at 1027-1016 cm(-1) could be better considered for this intent. Amide I/amide II ratios as calculated here and data from the literature suggest that protein complexes of the ear cartilage ECM are arranged with a lower helical conformation compared to pure collagen II. The present results could motivate further studies on this tissue under pathological or experimental states involving ear cartilage.
dc.description11
dc.description
dc.description
dc.description
dc.descriptionFundacao de Amparo a Pesquisa do Estado de Sao Paulo [2003/04597-0, 2007/058251-8, 2013/1078-0]
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description
dc.description
dc.description
dc.languageEnglish
dc.publisherPUBLIC LIBRARY SCIENCE
dc.publisherSAN FRANCISCO
dc.relationPlos One
dc.rightsaberto
dc.sourceWOS
dc.subjectArticular-cartilage
dc.subjectMacromolecular Orientation
dc.subjectInfrared-spectroscopy
dc.subjectCollagen Bundles
dc.subjectTendon
dc.subjectProteoglycans
dc.subjectSpecificity
dc.subjectProteins
dc.subjectSulfate
dc.subjectFibers
dc.titleFt-ir Microspectroscopy Of Rat Ear Cartilage
dc.typeArtículos de revistas


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