Advertisement

Applied Physics B

, 125:232 | Cite as

Anisotropy of bovine nasal cartilage measured by Fourier transform infrared imaging

  • Yuan Zhao
  • Yong-kang Zhu
  • Yan-fei Lu
  • Lin-wei Shang
  • Ming-yang Zhai
  • Xiao Wang
  • Jian-hua YinEmail author
Article
  • 30 Downloads

Abstract

Fourier transform infrared imaging (FTIRI) can be used to obtain the composition and structure information of sample. Here, FTIRI combined with spectral polarization analysis method was applied to investigate the fine anisotropy of bovine nasal cartilage (BNC). The upper BNC tissue was sliced into a three-dimensional (3D) block with three planes (XY, YZ, and XZ) parallel to horizontal section, forward section, and lateral section, respectively. The anisotropy of collagen fiber in BNC was represented by the absorbance of amide II (1590–1500 cm−1) at different polarization directions. It was found that collagen fiber showed little anisotropy in plane XY, XZ, and along the direction Z in plane YZ. It was more important that collagen fiber showed strong anisotropy along direction Y in plane YZ (transverse axis) of BNC, possibly including arched or wavy fiber orientation even a mixture of both in nasal septum top end. Two anisotropic deflections ranging from 600 to 930 μm and from 2680 to 2980 μm were quantitatively calculated. This study is of important significance for further understanding the physiological structure of nasal septum and provides remarkable experimental support for being a good transplant material in cartilage reshaping studies.

Notes

Acknowledgements

The authors acknowledge (1) the National Natural Science Foundation of China (NSFC) (61378087) and (2) Six Talent Peaks Project in Jiangsu Province (SWYY-034) for funding this work.

Compliance with ethical standards

Conflict of interest

The authors declare no conflict of interest.

References

  1. 1.
    Y. Xia, S. Zheng, M. Shark et al., Anisotropic properties of bovine nasal cartilage. Microsc. Res. Tech. 75(3), 300–306 (2012).  https://doi.org/10.1002/jemt.21058 CrossRefGoogle Scholar
  2. 2.
    Z.H. Mao, Y.C. Wu, X.X. Zhang et al., Comparative study on identification of healthy and osteoarthritic articular cartilages by fourier transform infrared imaging and chemometrics methods. J. Innov. Opt. Health Sci. (2017).  https://doi.org/10.1142/S1793545816500541 CrossRefGoogle Scholar
  3. 3.
    D.W. Ebert, C. Roberts, S.K. Farrar et al., Articular cartilage optical properties in the spectral range 300-850 nm. J. Biomed Opt. 3(3), 326–333 (1998).  https://doi.org/10.1117/1.429893 CrossRefADSGoogle Scholar
  4. 4.
    J.I. Youn, S.A. Telenkov, E. Kim et al., Optical and thermal properties of nasal septal cartilage. Lasers Surg. Med. 27(2), 119–128 (2000).  https://doi.org/10.1002/1096-9101(2000)27:2%3c119:AID-LSM3%3e3.0.CO;2-V CrossRefGoogle Scholar
  5. 5.
    E. Salomatina, A.N. Yaroslavsky, Evaluation of the in vivo and ex vivo optical properties in a mouse ear model. Phys. Med. Biol. 53(11), 2797–2807 (2008).  https://doi.org/10.1088/0031-9155/53/11/003 CrossRefGoogle Scholar
  6. 6.
    D.A. Reiter, P.C. Lin, K.W. Fishbein et al., Multicomponent T2 Relaxation analysis in cartilage. Magn. Reson. Med. 61(4), 803–809 (2009).  https://doi.org/10.1002/mrm.21926 CrossRefGoogle Scholar
  7. 7.
    C.F. Brewer, H. Keiser, Carbon-13 nuclear magnetic resonance study of chondroitin 4-sulfate in the proteoglycan of bovine nasal cartilage. Proc. Natl. Acad. Sci. U.S.A. 72(9), 3421–3423 (1975).  https://doi.org/10.1073/pnas.72.9.3421 CrossRefADSGoogle Scholar
  8. 8.
    J.G. Hofstaetter, L. Wunderlich, R.E. Samuel et al., Systemic hypoxia alters gene expression levels of structural proteins and growth factors in knee joint cartilage. Biochem. Biophys. Res. Commun. 330(2), 386–394 (2005).  https://doi.org/10.1016/j.bbrc.2005.02.168 CrossRefGoogle Scholar
  9. 9.
    T. Fukui, E. Tenborg, J.H.N. Yik et al., In-vitro and in vivo imaging of MMP activity in cartilage and joint injury. Biochem. Biophys. Res. Commun. 460(3), 741–746 (2015).  https://doi.org/10.1016/j.bbrc.2015.03.100 CrossRefGoogle Scholar
  10. 10.
    J.H. Yin, Y. Xia, Macromolecular concentrations in bovine nasal cartilage by Fourier transform infrared imaging and principal component regression. Appl. Spectrosc. 64(11), 1199–1208 (2010).  https://doi.org/10.1366/000370210793335124 CrossRefADSGoogle Scholar
  11. 11.
    J.H. Yin, F.L. Huang, Z.Y. Qian, Applications and progress of fourier transform infrared spectroscopic microimaging in bone disease research. Spectrosc. Spectr Anal. 4(34), 340–343 (2014).  https://doi.org/10.3964/j.issn.1000-0593(2014)02-0340-04 CrossRefGoogle Scholar
  12. 12.
    A. Yasuda, T. Sasaki, K. Suto et al., Mid-infrared transmission imaging and spectroscopy with PbSnTe laser diodes grown with stoichiometry-controlled liquid-phase epitaxy. Infrared Phys. Technol. 72, 249–253 (2015).  https://doi.org/10.1016/j.infrared.2015.08.009 CrossRefADSGoogle Scholar
  13. 13.
    J.H. Yin, Y. Xia, N. Ramakrishnan, Depth-dependent anisotropy of proteoglycan in articular cartilage by Fourier transform infrared imaging. Vib. Spectrosc. 57(2), 338–341 (2011).  https://doi.org/10.1016/j.vibspec.2011.08.005 CrossRefGoogle Scholar
  14. 14.
    J.H. Yin, Y. Xia, Proteoglycan concentrations in healthy and diseased articular cartilage by Fourier transform infrared imaging and principal component regression. Spectrochim. Acta Part A Mol. Biomol. Spectrosc. 133(133C), 825–830 (2014).  https://doi.org/10.1016/j.saa.2014.05.092 CrossRefADSGoogle Scholar
  15. 15.
    N. Jing, X. Jiang, Q. Wang et al., Attenuated total reflectance/Fourier transform infrared (ATR/FTIR) mapping coupled with principal component analysis for the study of in vitro degradation of porous polylactide/hydroxyapatite composite material. Anal. Methods 6(15), 5590–5595 (2014).  https://doi.org/10.1039/C4AY01289E CrossRefGoogle Scholar
  16. 16.
    Y. Xia, H. Alhadlaq, N. Ramakrishnan et al., Molecular and morphological adaptations in compressed articular cartilage by polarized light microscopy and Fourier-transform infrared imaging. J. Struct. Biol. 164, 88–95 (2008).  https://doi.org/10.1016/j.jsb.2008.06.009 CrossRefGoogle Scholar
  17. 17.
    Z.Y. Xiao, J.H. Yin, Fourier transform infrared spectroscopic analysis and characterization of principal components of articular cartilage. Chin. J. Light Scatt. 26(2), 213–218 (2014).  https://doi.org/10.13883/j.issn1004-5929.201402020 CrossRefGoogle Scholar
  18. 18.
    X. Yang, N. Ramakrishnan, A. Bidthanapally, The depth-dependent anisotropy of articular cartilage by fourier-transform infrared imaging (FTIRI). Osteoarthr. Cartil. 15(7), 780–788 (2007).  https://doi.org/10.1016/j.joca.2007.01.007 CrossRefGoogle Scholar
  19. 19.
    X. Bi, G. Li, S.B. Doty et al., A novel method for determination of collagen orientation in cartilage by Fourier transform infrared imaging spectroscopy (FT-IRIS). Osteoarthr. Cartil. 13(12), 1050–1058 (2005).  https://doi.org/10.1016/j.joca.2005.07.008 CrossRefGoogle Scholar
  20. 20.
    D.A. Boas, C. Pitris, N. Ramanujam, Handbook of biomedical optics (CRC Press, Boca Raton, 2011), pp. 94–100Google Scholar
  21. 21.
    J.F. Beek, P. Blokland, P. Posthumus et al., In vitro double-integrating-sphere optical properties of tissues between 630 and 1064 nm. Phys. Med. Biol. 42(11), 2255–2261 (1997).  https://doi.org/10.1088/0031-9155/42/11/017 CrossRefGoogle Scholar
  22. 22.
    I. Bushra, M. Nawshad, R. Abdur et al., Development of collagen/PVA composites patches for osteochondral defects using a green processing of ionic liquid. Int. J. Polym. Mat. Polym. Biomater. (2018).  https://doi.org/10.1080/00914037.2018.1474358 CrossRefGoogle Scholar
  23. 23.
    S.F. Weng, Fourier transform infrared spectroscopy (Chemical industry press, Beijing, 2010), pp. 188–192Google Scholar

Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2019

Authors and Affiliations

  • Yuan Zhao
    • 1
  • Yong-kang Zhu
    • 1
  • Yan-fei Lu
    • 1
  • Lin-wei Shang
    • 1
  • Ming-yang Zhai
    • 1
  • Xiao Wang
    • 1
  • Jian-hua Yin
    • 1
    Email author
  1. 1.Department of Biomedical EngineeringNanjing University of Aeronautics and AstronauticsNanjingChina

Personalised recommendations