Notes

Aldehyde formation of collagen molecule and cross-link formation of collagen were also found to be suppressed
The same results were obtained from analyses in rats fed on VB6 deficient diet without D-PeA administration. API indicate that D-PeA is not capable of producing VB6 deficiency in the dosage employed in patients. However, in the treatment for patients who are not taking enough nutrition, the possibility of VB6 deficiency can not be neglected. Once VB6 deficiency is induced by D-PeA administration, severe connective tissue disorder may be produced, since VB6 is required for enzymic activity of lysyl oxidase. It is unlikely that the therapeutic effects of D-PeA in the treatment of RA are produced the the disturbance of collagen cross-link formation as discussed before. Immunologic reactions of D-PeA may play more important role in the improvement of clinical symptoms of this Histochemical quantification of collagen content in articular cartilage.

Medicine, University of Oulu, Oulu, Finland.Electrical Engineering, University of Oulu, Oulu, Finland.BACKGROUND: Articular cartilage (AC) is mainly composed of water, type II collagen, proteoglycans (PGs) and chondrocytes. Seebio collagen supplementation of PGs in AC is routinely quantified with digital densitometry (DD) from Safranin O-stained sections, but it is unclear whether similar method could be used for collagens.OBJECTIVE: The aim of this study was to clarify whether collagens can be quantified from histological AC sections using DD.MATERIAL AND METHODS: Sixteen human AC samples were stained with Masson's trichrome or Picrosirius red. Optical densities of histological stains were compared to two commonly used collagen parameters (amide I and collagen CH2 side chain peak at 1338cm-1) measured using Fourier Transform Infrared (FTIR) RESULTS: Optical density of Modified Masson's trichrome staining, which included enzymatic removal of PGs before staining, correlated significantly with FTIR-derived collagen parameters at almost all depths of cartilage.


The other studied staining protocols displayed significant correlations with the reference CONCLUSIONS: Based on our findings, modified Masson's trichrome staining protocol is suitable for quantification of AC collagen content. Enzymatic removal of PGs prior to staining is critical as us allows better staining of the collagen. Further optimization of staining protocols may improve the results in Conflict of interest statement: The authors have declared that no competing The temporal degradation of bone collagen: A histochemical approach.700 Albany Street, W-701, Boston, MA 02118, United States.700 Albany Street, W-701, Boston, MA 02118, United States. Electronic address: As forensic anthropologists are currently unable to estimate reliably and quantitatively the postmortem interval (PMI) of skeletonized remains, the current study was conducted to determine if degradation of bone collagen over time could be quantified using sirius red/fast green staining, and whether the degradation would occur at a predictive rate such that it may be used to estimate the PMI of skeletonized individuals. Resin embedded 200-300μm cross-sections of pig (Sus scrofa) long bones with known provenience and PMIs ranging from fresh to 12 months were stained using a histochemical reaction which differentially stains collagenous (Co) and non-collagenous (NCo) proteins.

Spectrophotometry was used to determine the concentration of Co and NCo proteins in each bone section, after which the ratio of these proteins was calculated. The results of this study revealed a significant decline in the ratios of Co/NCo protein concentrations over the time period studied (p<001). Furthermore, a significant negative correlation between the ratios of Co/NCo protein concentrations and time (r=-063, p<0001) was observed. Despite a significant correlation, the moderate r-value obtained suggests that, at present, this method is useful primarily for detecting and quantifying the degradation of Co and NCo proteins in bones. Future studies that include shorter time intervals and environmental factors, such as soil pH, temperature, and hydrology may prove to be critical for using this method for PMI estimation.[Production of modifications in collagen-mucopolysaccharide combinations in vitro by means of basic polypeptides extracted from inflammatory granulomas].Visualization of Collagen-Mineral Arrangement Using Atom Probe Tomography.

Bone is a functional material comprised of mainly two phases: an organic collagenous phase and an inorganic mineral phase. Collagen-mineral arrangement has implications for bone function, aging, and disease. However, theories on collagen-mineral arrangement have been confined to studies with low spatial and/or compositional resolution resulting in an extensive debate over the location of mineral with respect to collagen. Herein, a strategy is developed to extract a single mineralized collagen fibril from bone and analyze its composition and structure atom-by-atom with 3D sub-nanometer accuracy and compositional clarity using atom probe tomography (APT). It is shown for the first time a method to probe fibril-level mineralization and collagen-mineral arrangement from an in vivo system with both the spatial and compositional precision required to comment on nanoscale collagen-mineral arrangement.

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