Spectroscopic Characterization of Collagen Cross-Links in Bone

Paschalis, Eleftherios P.; Verdelis, Kostas; Doty, Stephen B.; Boskey, Adele L.; Mendelsohn, Richard; Yamauchi, Mitsuo

doi:10.1359/jbmr.2001.16.10.1821

Cited by 465 publications

(450 citation statements)

References 32 publications

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“…Indeed, most of the bands in the spectrum are really superpositions of many of the closely spaced bands. Some of the band envelopes are resolvable into several components, most notably the amide I and amide III envelopes, for which several maxima or shoulders have been identified with particular secondary structure domains [30] or state of interfibril cross-links [31]. Because of the complexity of this problem, our discussion is empirical and our conclusions are only preliminary.…”

Section: Discussionmentioning

confidence: 95%

Bone Chemical Structure Response to Mechanical Stress Studied by High Pressure Raman Spectroscopy

et al. 2005

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Abstract. While the biomechanical properties of bone are reasonably well understood at many levels of structural hierarchy, surprisingly little is known about the response of bone to loading at the ultrastructural and crystal lattice levels. In this study, our aim was to examine the response (i.e., rate of change of the vibrational frequency of mineral and matrix bands as a function of applied pressure) of murine cortical bone subjected to hydrostatic compression. We determined the relative response during loading and unloading of mineral vs. matrix, and within the mineral, phosphate vs. carbonate, as well as proteinated vs. deproteinated bone. For all mineral species, shifts to higher wave numbers were observed as pressure increased. However, the change in vibrational frequency with pressure for the more rigid carbonate was less than for phosphate, and caused primarily by movement of ions within the unit cell. Deformation of phosphate on the other hand, results from both ionic movement as well as distortion. Changes in vibrational frequencies of organic species with pressure are greater than for mineral species, and are consistent with changes in protein secondary structures such as alterations in interfibril cross-links and helix pitch. Changes in vibrational frequency with pressure are similar between loading and unloading, implying reversibility, as a result of the inability to permanently move water out of the lattice. The use of high pressure Raman microspectroscopy enables a deeper understanding of the response of tissue to mechanical stress and demonstrates that individual mineral and matrix constituents respond differently to pressure.Key words: Raman spectroscopy -Bone -Biomechanics -Diamond anvil cell -High pressureThe chemical composition and crystal structure of bone play an essential role in its biological and structural functions [1,2]. Bone tissue can be described as a composite of an organic matrix reinforced with an inorganic mineral phase. The organic matrix is about 90% type I collagen fibrils locally oriented predominantly parallel to each other (in long bone) that provide a supporting matrix upon which the mineral crystals grow. The mineral fraction of bone is a highly impure carbonated apatite situated between collagen fibril cross-links and fibril ends. Both the organic and mineral components and the interactions between the two contribute to boneÕs mechanical properties, including strength, toughness and elasticity. It is not clear though how mineral crystallites deform in response to mechanical loading nor how the matrix deforms. This is particularly true at the atomic level. To better understand deformation it is useful to extract atomic-level compositional information about the changes in inorganic and organic phases that occur when bone undergoes mechanical loading.Raman spectroscopy is a powerful technique for relating bone mechanical properties with bone ultrastructural and crystal lattice changes [3]. Raman spectroscopy provides bone vibrational spectra and, like infrared spectros...

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Section: Discussionmentioning

confidence: 95%

Bone Chemical Structure Response to Mechanical Stress Studied by High Pressure Raman Spectroscopy

et al. 2005

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“…Sequential raw spectra for each trabecula were averaged and the contribution of the embedding pMMA and water vapor were corrected prior to baseline correction. The evaluated IR spectral parameters were (1) mineral crystallinity, which reflects the apatite size and perfection, calculated as the ratio of the relative intensity of subbands at 1020 and 1030 cm − 1 of the phosphate band [27]; (2) collagen maturity, determined as the relative ratio of pyridinium trivalent (Pyr, mature collagen) to dehydrodihydroxylysinonorleucine divalent (deH-DHLNL, new collagen) collagen cross-links using their respective subbands located at 1660 cm − 1 and 1690 cm − 1 of the amide I peak [28] and (3) carbonates to phosphates ratio, which reflects the carbonate content in bone and determined by the ratio of integrated areas of the υ2 CO 3 2− region (850-890 cm −1 ) to the υ1, υ3 phosphate band (900-1200 cm −1 ) [29].…”

Section: Fourier Transformed Infrared Microspectroscopy (Ftirm)mentioning

confidence: 99%

Glucose-dependent insulinotropic polypeptide receptor deficiency leads to modifications of trabecular bone volume and quality in mice

Gaudin-Audrain¹,

Irwin²,

Mansur³

et al. 2013

Bone

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A role for the gastro-intestinal tract in controlling bone remodeling is suspected since serum levels of bone remodeling markers are affected rapidly after a meal. Glucose-dependent insulinotropic polypeptide (GIP) represents a suitable candidate in mediating this effect. The aim of the present study was to investigate the effect of total inhibition of GIP signaling on trabecular bone volume, microarchitecture and quality. We used GIP receptor (GIPR) knockout mice and investigated trabecular bone volume and microarchitecture by microCT and histomorphometry. GIPR-deficient animals at 16 weeks of age presented with a significant (20%) increase in trabecular bone mass accompanied by an increase (17%) in trabecular number. In addition, the number of osteoclasts and bone formation rate was significantly reduced and augmented, respectively in these animals when compared with wild-type littermates. These modifications of trabecular bone microarchitecture are linked to a remodeling in the expression pattern of adipokines in the GIPR-deficient mice. On the other hand, despite significant enhancement in bone volume, intrinsic mechanical properties of the bone matrix was reduced as well as the distribution of bone mineral density and the ratio of mature/immature collagen cross-links. Taken together, these results indicate an increase in trabecular bone volume in GIPR KO animals associated with a reduction in bone quality.

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“…After acquisition, spectra were transferred to an offline computer (Dell Precision 650, Round Rock, TX, USA), and were zero-corrected for the baseline in the spectral area of Amide I and II ($1490-1700 cm À1 ) using Grams/32 (Galactic Software, Philadelphia, PA, USA); water vapor and polymethylmethacrylate (PMMA) spectral interferences were corrected for as described. (23,24) The spectra then underwent curve-fitting based on calculated second-derivative spectra, and the relative area ratio of the underlying bands at 1660 and 1690 cm À1 was calculated. This ratio corresponds to the relative ratio of pyr/divalent collagen cross-links, due to the perturbation that the cross-links exert on the molecular vibrations of the carbonyl groups present in the collagen chains.…”

Section: Raman Analysismentioning

confidence: 99%

“…This ratio corresponds to the relative ratio of pyr/divalent collagen cross-links, due to the perturbation that the cross-links exert on the molecular vibrations of the carbonyl groups present in the collagen chains. (24,25) For each biopsy, three trabeculae with evident fluorescent double labels were analyzed, and in each of these regions three measurements were obtained, for a total of nine measurements. For each patient, these nine values were averaged and the resultant value was treated as a single statistical unit.…”

Section: Raman Analysismentioning

confidence: 99%

Effects of alendronate and risedronate on bone material properties in actively forming trabecular bone surfaces

Hofstetter

Gamsjaeger

Phipps³

et al. 2012

Journal of Bone and Mineral Research

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We used Raman and Fourier transform infrared microspectroscopy (FTIRM) analysis to examine the intrinsic bone material properties at actively bone-forming trabecular surfaces in iliac crest biopsies from women with postmenopausal osteoporosis (PMO) who were treated with either alendronate (ALN) or risedronate (RIS). At eight study sites, women were identified who had postmenopausal osteoporosis (PMO), were at least 5 years postmenopause, and had been on long-term therapy (either 3-5 years or >5 years) with daily or weekly ALN or RIS. Following standard tetracycline labeling, biopsies were collected from 102 women (33 treated with ALN for 3-5 years , 35 with ALN for >5 years , 26 with RIS for 3-5 years , and 8 with RIS for >5 years ) and were analyzed at anatomical areas of similar tissue age in bone-forming areas (within the fluorescent double labels). The following outcomes were monitored and reported: mineral to matrix ratio (corresponding to ash weight), relative proteoglycan content (regulating mineralization commencement), mineral maturity (indicative of the mineral crystallite chemistry and stoichiometry, and having a direct bearing on crystallite shape and size), and the ratio of two of the major enzymatic collagen cross-links (pyridinoline/divalent). In RIS-5 there was a significant decrease in the relative proteoglycan content (À5.83% compared to ALN-5), while in both RIS-3 and RIS-5 there was significantly lower mineral maturity/ crystallinity (À6.78% and À13.68% versus ALN-3 and ALN-5, respectively), and pyridinoline/divalent collagen cross-link ratio (À23.09% and À41.85% versus ALN-3 and ALN-5, respectively). The results of the present study indicate that ALN and RIS exert differential effects on the intrinsic bone material properties at actively bone-forming trabecular surfaces. ß

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Spectroscopic Characterization of Collagen Cross-Links in Bone

Cited by 465 publications

References 32 publications

Bone Chemical Structure Response to Mechanical Stress Studied by High Pressure Raman Spectroscopy

Bone Chemical Structure Response to Mechanical Stress Studied by High Pressure Raman Spectroscopy

Glucose-dependent insulinotropic polypeptide receptor deficiency leads to modifications of trabecular bone volume and quality in mice

Effects of alendronate and risedronate on bone material properties in actively forming trabecular bone surfaces

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