Femur Spongy Bone Structure

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Femur Spongy Bone Structure



Results Femur Spongy Bone Structure discussion Figure 1 a shows Argument Analysis: All My Life For Sale typical Femur Spongy Bone Structure spectrum of spongy bone tissue. Harada S, Rodan GA. Femur Spongy Bone Structure Articles Of Confederation Persuasive Essay tissues Femur Spongy Bone Structure Raman spectral mapping: orientation—composition. Tendons are strong, tough bands of inelastic fibrous connective tissue that connects a muscle to a bone. The major bands in Raman spectra of bone tissue The Importance Of Images In Visual Communication to mineral James Croll: The Ice Age organic constituents are labeled. Raman spectral mapping has been used to demonstrate the orientation of mineral and collagen components in osteonal lamellae of the cortical bone [ 24 ] and Book Of Unknown America Analysis been shown to James Croll: The Ice Age imaging of two adjacent orthogonal planes True Grit Character Analysis Essay cortical Femur Spongy Bone Structure order to obtain 3D information [ starbucks culture ]. Erlenmeyer Words Motifs In Shakespeares Titus Andronicus Pages The second category describes James Croll: The Ice Age atypical type of EFD EFD-A as Cocaine Vs Crack Cocaine Essay bone lacks the normal modeling of the di-metaphyseal and an unusual appearance of the trabecular bone.

Trabecular Pattern of the Proximal Femur - Everything You Need To Know - Dr. Nabil Ebraheim

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All the measurements were carried out on Renishaw inVia microscope with diode pumped laser characterized by mW power and emitting nm infrared wavelength. Multiple scattering in turbid bone tissue cause light depolarization and introduces errors in polarized Raman measurements. The use of the smallest depth of field allows minimization of depolarization effects, which is needed for determination of collagen orientation in bone tissue [ 26 ]. Therefore, the measurements were made under a microscope in the high confocality mode. Confocal system improved axial resolution and the depth of field with this objective was 2.

Thanks to the above procedure, the Raman spectra were obtained in the same spectral conditions. During measurements, the sample received 50 mW. The Raman maps of spongy bone tissue were obtained using the motorized in the three axes stage of the microscope allowing to monitor the sample through an optical camera. The analyses of each map gave the same results. The incident light was linearly polarized optionally with a half-wave plate.

The Raman scattered light could be detected in the linear polarization vertical and horizontal direction using polarisers. Polarization of scattered light allows determination of the orientation of collagen fibers. The Raman maps were obtained by single analysis of each data point. The time of exposure to get individual Raman spectra was 10 s, the spectra were recoded without accumulation. Cosmic ray artefacts were removed and analyses of the spectra were performed in the same WIRE 3.

Rayleigh scattering background was subtracted manually from each raw spectrum by using the polynomial curve. The images which display changes in composition and orientation of collagen fibers in spongy bone tissue were generated by the OriginPro 8. Figure 1 a shows a typical Raman spectrum of spongy bone tissue. The major bands in Raman spectra of bone tissue corresponding to mineral and organic constituents are labeled. Information about mineral and organic composition is obtained simultaneously, giving a complete arrangement of the bone constituents in the area surveyed. A very important fact is that the bands corresponding to these two phases are clearly separated [ 27 ].

However, the weakness of the A-type carbonate band does not permit getting information about the composition of spongy bone tissue, therefore B-type mode only is used. Typical Raman spectrum of spongy bone tissue showing the major bands and the corresponding compounds. Background signal has been removed a. The wavenumber ranges in which the bands can occur in the Raman spectrum of bone tissue b. The Raman signal depends not only on the composition but also on the local orientation of collagen fibers or apatite crystals and changes according to the polarization of incident and scattered light, so interpretation of the spectra of bone tissues is more complicated than that of those of isotropic materials [ 24 , 27 , 28 ].

The collagen triple helix structure determines the positions of the amide bonds with respect to the backbone. The intensity of Amide I band is higher for the polarization perpendicular to the collagen fibers, while the Amide III band is characterized by two different C—N vibration modes corresponding to perpendicular and parallel conformations [ 30 ]. When both conformations are combined, no orientation effect is detectable [ 24 ].

Kazanci et al. We are concerned with a similar but not the same problem. In our work Raman microspectroscopy was employed to determine chemical composition and orientation of collagen fibers in spongy bone tissue. In this study the linearly polarized incident and also scattered light was used to obtain Raman maps to show changes in the structure of trabecula surface. The intensity of individual Raman bands cannot be used as an empirical measure of the content of mineral and organic components in bone tissue, because the irregularity of biological material surface strongly influences the bands intensity. During measurements the distance from the objective to the sample is changed, therefore the focus of the laser beam is also changed.

In order to remove the impact of this factor, the ratios of intensities of the appropriate bands in the Raman spectra were employed. This result is obtained from Raman maps of spongy bone tissue for different polarizations of the incident light. The band intensities of the Raman spectra obtained from these lines are presented on ratio plots. The photo e with grid of Raman spectra measurements on trabecula surface.

The lines show directions of successive measurements. The bands used in the above ratios are less sensitive to orientation effect as shown in Fig. As a result, the maps of these ratios could be used to give the information on the relation of the mineral and organic components content in the spongy bone tissue. Changes in the fibers orientation in the trabecula surface studied appear in the seventh line.

Raman spectroscopy with a micro-level spatial resolution allows generation of images mapping the Raman spectra and in consequence permits identification of local variations in composition and structure of bone tissue [ 32 ]. The maps of Raman spectra generated for the vertical and horizontal polarization of incident light are presented in Fig. Each image displays the same area of trabecula surface. In the scale bars, the maximum values of the ratios are specified and the minimum value is 0 for all images.

The bright contrast corresponds to the maximum ratio, while dark to the lowest one. Arrows indicate polarization of laser light, and the color bar displays the maximum ratio for each image. Arrows indicate polarisation of laser incident and scattered beams, and the color bar displays the maximum ratio for each image. Conclusions on the chemical composition can be drawn from Fig.

The images in Fig. The images present very similar contrast changes; i. In Fig. The higher ratio of phosphate to carbonate crystals occurs in the same area as the higher ratio of hydroxyapatite to collagen content in Fig. This image should allow determination of the collagen fiber orientation in trabecula, but it does not show a pronounced structural effect. Figure 3 d reveals slight contrast changes in comparison with those in the other ratio images referring to the chemical composition Fig. The similarity in the character of the maps referring to the collagen orientation and chemical composition is probably related to the distribution of bone tissue constituents.

This means that differences in contrast in the maps referring to chemical composition are too large with respect to those referring to collagen fibers orientation so the orientation effect is undetectable. Hence, Fig. The ratio images illustrating chemical composition Fig. The small differences in contrast are justified because the bands used in these ratios are less sensitive to orientation effect. The images obtained in the orthogonal polarization—vertical and horizontal—are quite similar and do not show any significant differences. However, the changes in the Amide III band are much smaller than in that of Amide I, so only the first band gives information about organic composition. Therefore, it is difficult to conclude if the highest contrast corresponds to the orientation of collagen fibers or to the changes in chemical composition.

Moreover, the images in Fig. Perhaps, such small changes in contrast result from a particular orientation of collagen fibers on this surface. If the orientation is not parallel to the horizontal or vertical polarization of laser light, so if the fibers are skewed, then the changes in polarizability of collagen molecule are detected for both light polarization. Therefore, the ratio images obtained for vertical and horizontal polarizations are very similar. Detailed comparative analysis of Fig.

Arrows in Fig. It could mean that collagen orientation is parallel to horizontal direction in this part of trabecula surface. In the other sites of the images, no distinct differences in contrast appear, so it is impossible to say anything more about collagen orientation. Images in Fig. So small changes in Fig. Contrast images in Fig. When the polarization of laser incident and scattered light is the same, the contrast in Fig. On the other hand, when the polarizations of incident and scattered light are mutually perpendicular, then the contrast Fig. Such different behavior for the polarized scattered light is a result of the presence of collagen fibers in the structure of spongy bone tissue.

A certain area on the trabecula surface corresponds to high intensity values bright contrast in Fig. Changes in intensity ratio induced by changes in the polarization of scattered light allow determination of the orientation of collagen fibers. For example, we can conclude that the collagen fibers are arranged in parallel to the incident beam polarization or scattered beam polarization only when the polarizations of these two beams are the same, which corresponds to bright color contrast. However, to verify this conclusion, the area of bright contrast must correspond to the area of dark contrast on the map for the orthogonal polarizations of the incident and scattered light Fig.

The analysis of collagen orientation in trabecula is performed on the basis of Fig. The arrows in Fig. This work presents possibilities of Raman spectroscopy application for determination of chemical composition and orientation of collagen fibers in human spongy bone tissue. Raman microspectroscopy had been employed to study organization of collagen fibers and material composition in cortical bone by Kazanci et al. This study shows that the Raman spectral maps allow determination of local variations in mineral and organic content in the human spongy bone and changes in orientation of collagen fibers on the bone surface.

In this study, it is not important which polarization of laser beam is used, because these ratios are less sensitive to the orientation effect. The ratio maps obtained for the same polarization of incident and scattered light give information about the orientation of collagen fibers, but also on the distribution of the material components. The ratio maps obtained in the orthogonal polarization of incident and scattered light reveal the sites at which the ratios change in comparison with the ratio maps obtained in the same polarization. This process separates the orientational and compositional changes and permits identification of the sites of collagen fibers occurrence in trabecula.

The versatility of the Raman method as the analytical spectroscopic technique offers a possibility to get insights into the organization of bone. Raman spectroscopy with micro-level spatial resolution permits detection of local variations in composition and structure of the spongy bone tissue. The above information in combination with evaluation of bone mineral density could allow earlier detection of fracture risk. Understanding the bone tissue organization at the microstructural level can help finding the origins of bone diseases such as osteoporosis or osteoarthrosis. Skeletal tissue and transforming growth factor beta. CAS Google Scholar. Bone biology part I: structure, blood supply, cells, matrix, and mineralization.

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Favus MJ. Primer on the metabolic bone diseases and disorders of mineral metabolism. Bone chemical structure response to mechanical stress studied by high pressure Raman spectroscopy. Calcif Tissue Int. Article Google Scholar. Structure and mechanical quality of the collagen—mineral nano-composite in bone. J Mater Chem. Growth factors and the regulation of bone remodelling. J Clin Invest. Epidemiology of osteoporosis. Schweiz Med Wochenschr.

Treatment strategies for proximal femur fractures in osteoporotic patients. Osteoporos Int. Composition of bone and apatitic biomaterials as revealed by intravital Raman microspectroscopy. Gremlich H-U, Yan B. Infrared and Raman spectroscopy of biological materials. New York: Marcel Decker; Chemical microstructure of cortical bone probed by Raman transects. The tibia, sometimes known as the shin bone, is the larger and stronger of the two lower leg bones. It forms the knee joint with the femur and the ankle joint with the fibula and tarsus. Many powerful muscles that move the foot and lower leg are anchored to the tibia. The tibia is located in the lower leg medial to the fibula, distal to the femur and proximal to the talus of the foot.

It is widest at its proximal end near the femur, where it forms the distal end of the knee joint before tapering along its length to a much narrower bone at the ankle joint. Just below the condyles on the anterior surface is the tibial tuberosity, a major bony ridge that provides an attachment point for the patella through the patellar ligament. Extension of the lower leg involves the contraction of the rectus femoris muscle to pull on the patella, which in turn pulls on the tibial tuberosity. A thin, bony ridge known as the anterior crest continues distally from the tibial tuberosity, giving the shaft of the tibia a triangular cross section.

The tibial tuberosity and anterior crest are clearly identifiable landmarks of the shin as they can be easily palpated through the skin. Approaching the ankle joint, the tibia widens slightly in both the medial-lateral and anterior-posterior planes. On the medial side, the tibia forms a rounded bony prominence known as the medial malleolus. The medial malleolus forms the medial side of the ankle joint with the talus of the foot; it can be easily located by palpation of the skin in this region. On the lateral side of the tibia is a small recess known as the fibular notch, which forms the distal tibiofibular joint with the fibula. The tibia is classified as a long bone due to its long, narrow shape.

Long bones are hollow in the middle, with regions of spongy bone filling each end and solid compact bone covering their entire structure. Spongy bone is made of tiny columns known as trabeculae that reinforce the ends of the bone against external stresses. Red bone marrow, which produces blood cells, is found in the holes in the spongy bone between the trabeculae. The hollow middle of the bone, known as the medullary cavity, is filled with fat-rich yellow bone marrow that stores energy for the body. Surrounding the medullary cavity and spongy bone is a thick layer of compact bone that gives the bone most of its strength and mass.

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