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

Ramakrishnan N, Xia Y, Bidthanapally A - J Orthop Surg Res (2008)

Bottom Line: With the change in the polarization state of the incident infrared light, the resulting anisotropic behavior of the tissue structure is described here.The parallel sections in the radial zone, however, have a nearly isotropic amide II absorption and a distinct amide I anisotropy.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.

View Article: PubMed Central - HTML - PubMed

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

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 mum thick) were obtained from three different surfaces of the canine tissue blocks and imaged at 6.25 microm pixel resolution. For each section, infrared imaging experiments were repeated thirteen times with the identical parameters except a 15 degrees increment of the analyzer's angle in the 0 degrees-180 degrees 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.

No MeSH data available.


Related in: MedlinePlus

Absorption anisotropy of amide I (a) and amide II (b) of tendon's cross section at three different sample orientations.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC2570663&req=5

Figure 4: Absorption anisotropy of amide I (a) and amide II (b) of tendon's cross section at three different sample orientations.

Mentions: To further investigate the anisotropy of the cross sections from tendon, the same cross section was placed at three different orientations (θ = 0°, ~65° and 90°) with respect to the polarization axis and the anisotropy experiments were repeated at these three orientations. Figure 4 shows the anisotropy profiles of amide I and amide II for these three orientations. It is clear that both amide vibrations have distinct anisotropy with the perpendicularity between them, even though the cross sections of the tendon do not have a visible fibril arrangement (cf Figure 2a). This result has two implications. First, the schematic assumption for the amide II orientation as illustrated in Figure 1b2 needs further investigation (see later in Discussion). Second, these amide bonds have a fixed orientation in the tissue's cross section with respect to the local fibril structure. (These experiments were conducted on various cross sections and the results are found to be consistent.)


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

Ramakrishnan N, Xia Y, Bidthanapally A - J Orthop Surg Res (2008)

Absorption anisotropy of amide I (a) and amide II (b) of tendon's cross section at three different sample orientations.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2570663&req=5

Figure 4: Absorption anisotropy of amide I (a) and amide II (b) of tendon's cross section at three different sample orientations.
Mentions: To further investigate the anisotropy of the cross sections from tendon, the same cross section was placed at three different orientations (θ = 0°, ~65° and 90°) with respect to the polarization axis and the anisotropy experiments were repeated at these three orientations. Figure 4 shows the anisotropy profiles of amide I and amide II for these three orientations. It is clear that both amide vibrations have distinct anisotropy with the perpendicularity between them, even though the cross sections of the tendon do not have a visible fibril arrangement (cf Figure 2a). This result has two implications. First, the schematic assumption for the amide II orientation as illustrated in Figure 1b2 needs further investigation (see later in Discussion). Second, these amide bonds have a fixed orientation in the tissue's cross section with respect to the local fibril structure. (These experiments were conducted on various cross sections and the results are found to be consistent.)

Bottom Line: With the change in the polarization state of the incident infrared light, the resulting anisotropic behavior of the tissue structure is described here.The parallel sections in the radial zone, however, have a nearly isotropic amide II absorption and a distinct amide I anisotropy.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.

View Article: PubMed Central - HTML - PubMed

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

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 mum thick) were obtained from three different surfaces of the canine tissue blocks and imaged at 6.25 microm pixel resolution. For each section, infrared imaging experiments were repeated thirteen times with the identical parameters except a 15 degrees increment of the analyzer's angle in the 0 degrees-180 degrees 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.

No MeSH data available.


Related in: MedlinePlus