A novel method for determination of collagen orientation in cartilage by Fourier transform infrared imaging spectroscopy (FT-IRIS)

Bi, Xiaohong; Li, G.; Doty, Stephen B.; Camacho, Nancy P.

doi:10.1016/j.joca.2005.07.008

Cited by 164 publications

(179 citation statements)

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“…Fourier transform IR (FTIR) is the most commonly applied type of IR spectroscopy, because of its higher speed, accuracy and signal-to-noise ratio compared with conventional (dispersive) IR techniques [97]. Similar to Raman spectroscopy, the orientation and arrangement of mineralized collagen fibres can be investigated through the use of a polarized laser [77,98]. However, IR spectroscopy detects asymmetric rather than symmetric vibrational modes (stretches) [99].…”

Section: Polarized Fourier Transform Infrared Spectroscopymentioning

confidence: 99%

“…Although FTIR has been routinely used to examine the composition of bone [100], relatively few studies have investigated the ultrastructural organization of bone [101,102] and neighbouring tissues such as the ligament-to-bone insertion [103] or cartilage [77,104]. This is due to the relatively recent idea of using polarized light for different sample or polarization rotation angles, which allows collagen fibril orientation to be examined in FTIR [77,98]. It should be noted that, as for PLM and Raman spectroscopy, FTIR is an inherently 2D technique, and cannot provide quantitative 3D orientation information.…”

Section: Polarized Fourier Transform Infrared Spectroscopymentioning

confidence: 99%

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Techniques to assess bone ultrastructure organization: orientation and arrangement of mineralized collagen fibrils

Georgiadis

Müller

Schneider

2016

J. R. Soc. Interface.

112

100

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Bone's remarkable mechanical properties are a result of its hierarchical structure. The mineralized collagen fibrils, made up of collagen fibrils and crystal platelets, are bone's building blocks at an ultrastructural level. The organization of bone's ultrastructure with respect to the orientation and arrangement of mineralized collagen fibrils has been the matter of numerous studies based on a variety of imaging techniques in the past decades. These techniques either exploit physical principles, such as polarization, diffraction or scattering to examine bone ultrastructure orientation and arrangement, or directly image the fibrils at the sub-micrometre scale. They make use of diverse probes such as visible light, X-rays and electrons at different scales, from centimetres down to nanometres. They allow imaging of bone sections or surfaces in two dimensions or investigating bone tissue truly in three dimensions, in vivo or ex vivo, and sometimes in combination with in situ mechanical experiments. The purpose of this review is to summarize and discuss this broad range of imaging techniques and the different modalities of their use, in order to discuss their advantages and limitations for the assessment of bone ultrastructure organization with respect to the orientation and arrangement of mineralized collagen fibrils.

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Section: Polarized Fourier Transform Infrared Spectroscopymentioning

confidence: 99%

Section: Polarized Fourier Transform Infrared Spectroscopymentioning

confidence: 99%

Techniques to assess bone ultrastructure organization: orientation and arrangement of mineralized collagen fibrils

Georgiadis

Müller

Schneider

2016

J. R. Soc. Interface.

112

100

View full text Add to dashboard Cite

show abstract

“…In AC, the polarized FTIR studies have revealed that the intensities of the amide I, the amide II, and the amide III regions vary strongly when polarization plane of infrared light is altered (19,(57)(58)(59)(60), whereas the carbohydrate region shows only weak anisotropy in the radial zone of AC (58,61). It is known that the transition moments of the amide I and II bonds are qualitatively perpendicular to each other (60). This has been utilized to assess the orientation of the collagen fibrils by calculating the ratio of the amide I to the amide II peaks under polarized infrared light.…”

Section: 448 CMmentioning

confidence: 99%

Vibrational spectroscopy of articular cartilage

Rieppo

Töyräs

Saarakkala

2016

Applied Spectroscopy Reviews

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Articular cartilage is a connective tissue that is located at the ends of long bones. Type II collagen, proteoglycans, water, and chondrocytes are the main constituents of articular cartilage. Osteoarthritis, the most common joint disease in the world, causes degenerative changes in articular cartilage tissue. Fourier transform infrared, Raman, and near infrared spectroscopic techniques offer versatile tools to assess biochemical composition and quality of articular cartilage. These vibrational spectroscopic techniques can be used to broaden our understanding about the compositional changes during osteoarthritis, and they also hold promise in disease diagnostics. In this article, the current literature of articular cartilage spectroscopic studies is reviewed.

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“…Images were calculated from data acquired with the polarizer by dividing the areas of the amide I and amide II collagen peaks for each pixel (amide I/amide II). We have previously demonstrated that this ratio provides an index of collagen fibril orientation as follows:≥2.7: fibrils parallel to the articular surface;≤1.7: fibrils perpendicular to the articular surface; 2.7-1.7: random or mixed fibril orientation [41]. For quantitative analysis, all the pixels in the polarized FT-IRIS image were divided into three orientation categories as above, and the percentage of pixels falling into each category was calculated.…”

Section: Ft-iris Image Processingmentioning

confidence: 99%

Fourier transform infrared imaging and MR microscopy studies detect compositional and structural changes in cartilage in a rabbit model of osteoarthritis

Yang

Bostrom

et al. 2006

Anal Bioanal Chem

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Assessment of subtle changes in the primary macromolecular components of cartilage, proteoglycan (PG) and collagen, is critical for the diagnosis of early stages of osteoarthritis (OA), but to date has remained a challenge. In the current study, we induced osteoarthritic cartilage changes in a rabbit model via ligament transection and medial meniscectomy and monitored disease progression with the techniques of infrared fiber optic probe (IFOP) spectroscopy, Fourier transform infrared imaging spectroscopy (FT-IRIS), and magnetic resonance imaging (MRI) microscopy. IFOP studies combined with chemometric partial least squares analysis enabled us to monitor progressive cartilage surface changes from two to twelve weeks post-surgery. FT-IRIS studies of histological sections of femoral condyle cartilage demonstrated that compared to control cartilage, the OA cartilage had significantly reduced PG content 2 and 4 weeks post-surgery, collagen fibril orientation changes 2 and 4 weeks post-surgery, and changes in collagen integrity 2 and 10 weeks post-surgery, but no significant changes in collagen content at any time point. MR microscopy studies found reduced fixed charge density (FCD), reflective of reduced PG content, in the OA cartilage compared to controls 4 weeks post-surgery. In addition, a non-significant trend towards higher apparent MT exchange rate k m was found in the OA cartilage at this time point, suggesting changes in collagen structural features. These two MR findings, for FCD and k m , parallel the FT-IRIS findings of reduced PG content, and altered collagen integrity, respectively. Further, MR microscopy studies at the 12 week time point cartilage found a trend towards longer T 2 values and decreased anisotropy in the deep zone of the OA cartilage, consistent with increased hydration and less ordered collagen. These studies demonstrate that together, FT-IRIS and MR microscopy provide complementary data on compositional changes in articular cartilage at early stages of osteoarthritic degradation.

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A novel method for determination of collagen orientation in cartilage by Fourier transform infrared imaging spectroscopy (FT-IRIS)

Cited by 164 publications

References 45 publications

Techniques to assess bone ultrastructure organization: orientation and arrangement of mineralized collagen fibrils

Techniques to assess bone ultrastructure organization: orientation and arrangement of mineralized collagen fibrils

Vibrational spectroscopy of articular cartilage

Fourier transform infrared imaging and MR microscopy studies detect compositional and structural changes in cartilage in a rabbit model of osteoarthritis

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