Log on / register
BioMed Central home | Journals A-Z | Feedback | Support | My details
Open AccessResearch article

Fourier-transform infrared anisotropy in cross and parallel sections of tendon and articular cartilage

Nagarajan Ramakrishnan email, Yang Xia email and Aruna Bidthanapally email

Department of Physics and Center for Biomedical Research, Oakland University, Rochester, MI 48309, USA

author email corresponding author email

Journal of Orthopaedic Surgery and Research 2008, 3:48doi:10.1186/1749-799X-3-48

Published: 6 October 2008

Abstract

Background

Fourier Transform Infrared Imaging (FTIRI) is used to investigate the amide anisotropies at different surfaces of a three-dimensional cartilage or tendon block. With the change in the polarization state of the incident infrared light, the resulting anisotropic behavior of the tissue structure is described here.

Methods

Thin sections (6 μm thick) were obtained from three different surfaces of the canine tissue blocks and imaged at 6.25 μm pixel resolution. For each section, infrared imaging experiments were repeated thirteen times with the identical parameters except a 15° increment of the analyzer's angle in the 0° – 180° angular space. The anisotropies of amide I and amide II components were studied in order to probe the orientation of the collagen fibrils at different tissue surfaces.

Results

For tendon, the anisotropy of amide I and amide II components in parallel sections is comparable to that of regular sections; and tendon's cross sections show distinct, but weak anisotropic behavior for both the amide components. For articular cartilage, parallel sections in the superficial zone have the expected infrared anisotropy that is consistent with that of regular sections. The parallel sections in the radial zone, however, have a nearly isotropic amide II absorption and a distinct amide I anisotropy.

Conclusion

From the inconsistency in amide anisotropy between superficial to radial zone in parallel section results, a schematic model is used to explain the origins of these amide anisotropies in cartilage and tendon.


© 1999-2010 BioMed Central Ltd unless otherwise stated. Part of Springer Science+Business Media.