Artículos de revistas
Ft-ir Microspectroscopy Of Rat Ear Cartilage
Registro en:
Plos One. PUBLIC LIBRARY SCIENCE, n. 11, n. 3, p. .
1932-6203
WOS:000372708900036
10.1371/journal.pone.0151989
Autor
Vidal
BD; Mello
MLS
Institución
Resumen
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Rat 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. 11
Fundacao de Amparo a Pesquisa do Estado de Sao Paulo [2003/04597-0, 2007/058251-8, 2013/1078-0] Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)