Some studies on the composition of bovine cortical-bone sialoprotein.
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ABSTRACT:
SUBMITTER: Andrews AT
PROVIDER: S-EPMC1271209 | biostudies-other | 1967 Sep
REPOSITORIES: biostudies-other
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Project description:A fraction containing chondroitin sulphate, isolated from bovine cortical bone under mild conditions, was separated by ion-exchange chromatography into three fractions with apparent homogeneity on electrophoresis and ultracentrifugation. Two of these appeared to consist of chondroitin sulphate bound to a glycoprotein ;core' that had similarities to the bone sialoprotein described previously. The differences in composition of the two fractions were considered to be due to variation in the number or lengths of the polysaccharide chains. The presence of xylose and the alkali-lability of the bond between protein and polysaccharide suggested the presence of a xylosylserine linkage. The third fraction had the properties of a relatively pure chondroitin sulphate which contained a small amount of peptide. These fractions differed considerably from the protein-polysaccharide complexes of epiphysial and other cartilages, and their relevance to the possible role of glycosaminoglycans is discussed.
| S-EPMC1198608 | biostudies-other
Project description:1. Bovine bone sialoprotein (mol.wt. 23000) contains N-acetylneuraminic acid and N-glycollylneuraminic acid, fucose, galactose, mannose, N-acetylgalactosamine and N-acetylglucosamine residues in the form of a very small number, perhaps one, of highly branched oligosaccharide structures linked covalently to peptide. 2. Periodate oxidation of the sialoprotein results in quantitative destruction only of the sialic acid and fucose residue consistent with the earlier findings of their positions as terminal groups. 3. Terminal sialic acid residues are attached to galactopyranose residues by 2,3-linkages, and to some N-acetylgalactosamine residues (at C-6). 4. Sequential Smith degradation indicates that N-acetylgalactosamine residues may be present as points of branching (linked in C-1, C-3 and C-6) and N-acetylglucosamine residues are located in the inner part of the structure, adjacent to the carbohydrate-peptide bond(s). 5. Mannose residues appear to be linked in the 1,3-positions.
| S-EPMC1187590 | biostudies-other
Project description:Tendons/ligaments insert into bone via a transitional structure, the enthesis, which is susceptible to injury and difficult to repair. Fibrocartilaginous entheses contain fibrocartilage in their transitional zone, part of which is mineralized. Mineral-associated proteins within this zone have not been adequately characterized. Members of the Small Integrin Binding Ligand N-linked Glycoprotein (SIBLING) family are acidic phosphoproteins expressed in mineralized tissues. Here we show that two SIBLING proteins, bone sialoprotein (BSP) and osteopontin (OPN), are present in the mouse enthesis. Histological analyses indicate that the calcified zone of the quadriceps tendon enthesis is longer in Bsp(-/-) mice, however no difference is apparent in the supraspinatus tendon enthesis. In an analysis of mineral content within the calcified zone, micro-CT and Raman spectroscopy reveal that the mineral content in the calcified fibrocartilage of the quadriceps tendon enthesis are similar between wild type and Bsp(-/-) mice. Mechanical testing of the patellar tendon shows that while the tendons fail under similar loads, the Bsp(-/-) patellar tendon is 7.5% larger in cross sectional area than wild type tendons, resulting in a 16.5% reduction in failure stress. However, Picrosirius Red staining shows no difference in collagen organization. Data collected here indicate that BSP is present in the calcified fibrocartilage of murine entheses and suggest that BSP plays a regulatory role in this structure, influencing the growth of the calcified fibrocartilage in addition to the weakening of the tendon mechanical properties. Based on the phenotype of the Bsp(-/-) mouse enthesis, and the known in vitro functional properties of the protein, BSP may be a useful therapeutic molecule in the reattachment of tendons and ligaments to bone.
| S-EPMC4875796 | biostudies-literature
Project description:Bone sialoprotein (BSP) is a multifunctional extracellular matrix protein found in mineralized tissues, including bone, cartilage, tooth root cementum (both acellular and cellular types), and dentin. In order to define the role BSP plays in the process of biomineralization of these tissues, we analyzed cementogenesis, dentinogenesis, and osteogenesis (intramembranous and endochondral) in craniofacial bone in Bsp null mice and wild-type (WT) controls over a developmental period (1-60 days post natal; dpn) by histology, immunohistochemistry, undecalcified histochemistry, microcomputed tomography (microCT), scanning electron microscopy (SEM), transmission electron microscopy (TEM), and quantitative PCR (qPCR). Regions of intramembranous ossification in the alveolus, mandible, and calvaria presented delayed mineralization and osteoid accumulation, assessed by von Kossa and Goldner's trichrome stains at 1 and 14 dpn. Moreover, Bsp(-/-) mice featured increased cranial suture size at the early time point, 1 dpn. Immunostaining and PCR demonstrated that osteoblast markers, osterix, alkaline phosphatase, and osteopontin were unchanged in Bsp null mandibles compared to WT. Bsp(-/-) mouse molars featured a lack of functional acellular cementum formation by histology, SEM, and TEM, and subsequent loss of Sharpey's collagen fiber insertion into the tooth root structure. Bsp(-/-) mouse alveolar and mandibular bone featured equivalent or fewer osteoclasts at early ages (1 and 14 dpn), however, increased RANKL immunostaining and mRNA, and significantly increased number of osteoclast-like cells (2-5 fold) were found at later ages (26 and 60 dpn), corresponding to periodontal breakdown and severe alveolar bone resorption observed following molar teeth entering occlusion. Dentin formation was unperturbed in Bsp(-/-) mouse molars, with no delay in mineralization, no alteration in dentin dimensions, and no differences in odontoblast markers analyzed. No defects were identified in endochondral ossification in the cranial base, and craniofacial morphology was unaffected in Bsp(-/-) mice. These analyses confirm a critical role for BSP in processes of cementogenesis and intramembranous ossification of craniofacial bone, whereas endochondral ossification in the cranial base was minimally affected and dentinogenesis was normal in Bsp(-/-) molar teeth. Dissimilar effects of loss of BSP on mineralization of dental and craniofacial tissues suggest local differences in the role of BSP and/or yet to be defined interactions with site-specific factors.
| S-EPMC4466207 | biostudies-literature
Project description:Orthopedic implant failure due to aseptic loosening and mechanical instability remains a major problem in total joint replacement. Improving osseointegration at the bone-implant interface may reduce micromotion and loosening. Bone sialoprotein (BSP) has been shown to enhance bone formation when coated onto titanium femoral implants and in rat calvarial defect models. However, the most appropriate method of BSP coating, the necessary level of BSP coating, and the effect of BSP coating on cell behavior remain largely unknown. In this study, BSP was covalently coupled to titanium surfaces via an aminosilane linker (APTES), and its properties were compared to BSP applied to titanium via physisorption and untreated titanium. Cell functions were examined using primary human osteoblasts (hOBs) and L929 mouse fibroblasts. Gene expression of specific bone turnover markers at the RNA level was detected at different intervals. Cell adhesion to titanium surfaces treated with BSP via physisorption was not significantly different from that of untreated titanium at any time point, whereas BSP application via covalent coupling caused reduced cell adhesion during the first few hours in culture. Cell migration was increased on titanium disks that were treated with higher concentrations of BSP solution, independent of the coating method. During the early phases of hOB proliferation, a suppressive effect of BSP was observed independent of its concentration, particularly when BSP was applied to the titanium surface via physisorption. Although alkaline phosphatase activity was reduced in the BSP-coated titanium groups after 4 days in culture, increased calcium deposition was observed after 21 days. In particular, the gene expression level of RUNX2 was upregulated by BSP. The increase in calcium deposition and the stimulation of cell differentiation induced by BSP highlight its potential as a surface modifier that could enhance the osseointegration of orthopedic implants. Both physisorption and covalent coupling of BSP are similarly effective, feasible methods, although a higher BSP concentration is recommended.
| S-EPMC4844107 | biostudies-literature
Project description:The underlying mechanisms of breast cancer cells metastasizing to distant sites are complex and multifactorial. Bone sialoprotein (BSP) and ?v?3 integrin were reported to promote the metastatic progress of breast cancer cells, particularly metastasis to bone. Most theories presume that BSP promotes breast cancer metastasis by binding to ?v?3 integrin. Interestingly, we found the ?v?3 integrin decreased in BSP silenced cells (BSPi), which have weak ability to form bone metastases. However, the relevance of their expression in primary tumor and the way they participate in metastasis are not clear. In this study, we evaluated the relationship between BSP, ?v?3 integrin levels, and the bone metastatic ability of breast cancer cells in patient tissues, and the data indicated that the ?v?3 integrin level is closely correlated to BSP level and metastatic potential. Overexpression of ?v?3 integrin in cancer cells could reverse the effect of BSPi in vitro and promote bone metastasis in a mouse model, whereas knockdown of ?v?3 integrin have effects just like BSPi. Moreover, The Cancer Genome Atlas data and RT-PCR analysis have also shown that SPP1, KCNK2, and PTK2B might be involved in this process. Thus, we propose that ?v?3 integrin is one of the downstream factors regulated by BSP in the breast cancer-bone metastatic cascade.
| S-EPMC6778634 | biostudies-literature
Project description:BACKGROUND:Until today, a reliable diagnostic discrimination between periprosthetic joint infections (PJI) and aseptic failure (AF) after total joint arthroplasty (TJA) remains challenging. Nearly all recent research focused on synovial markers to be elevated in PJI rather than in AF patients. In this study, synovial bone sialoprotein (sBSP) was investigated in PJI and AF arthroplasty patients before revision surgery. METHODS:sBSP and C-reactive protein (CRP) were determined in synovial fluid samples of PJI (n = 13) patients fulfilling the MSIS criteria and AF (n = 25) patients. Beside descriptive analysis and comparison, computed statistics determined the area under the receiver operating characteristics curve (AUC) to evaluate the discrimination ability of the tested synovial markers. RESULTS:In patients with PJI according to the MSIS criteria, mean sBSP was significantly lower: 14.8?ng/ml (95% CI 5.5-24.1) vs. 38.2?ng/ml in the AF group (95% CI 31.1-45.3), p ? 0.001. Conversely, mean sCRP was significantly higher in PJI patients: 8.4??g/ml (95% CI 0-17.2) vs. 1.8??g/ml in the AF group (95% CI 0.9-2.8), p = 0.032. The AUC of sCRP in PJI patients was 0.71. The AUC of sBSP in AF revision arthroplasty patients was 0.83. The detection of osteolyses was not associated with higher sBSP concentrations. CONCLUSIONS:Considering the MSIS criteria, significantly higher sBSP concentrations were found in synovial fluid samples of AF compared to PJI patients. sCRP showed only fair, sBSP good discrimination potential. If it is not clear whether PJI is present or not, sBSP may be considered as an add-on synovial marker.
| S-EPMC7254687 | biostudies-literature
Project description:Stress fractures are a common overuse injury among runners associated with the mechanical fatigue of bone. Several in vivo biomechanical studies have investigated specific characteristics of the vertical ground reaction force (vGRF) in heel-toe running and have observed an association between increased loading rate during impact and individuals with a history of stress fracture. The purpose of this study was to examine the fatigue behavior of cortical bone using vGRF-like loading profiles, including those that had been decomposed into their respective impact and active phase components. Thirty-eight cylindrical cortical bone samples were extracted from bovine tibiae and femora. Hydrated samples were fatigue tested at room temperature in zero compression under load control using either a raw (n?=?10), active (n?=?10), low impact (n?=?10), or high impact (n?=?8) vGRF profile. The number of cycles to failure was quantified and the test was terminated if the sample survived 105 cycles. Fatigue life was significantly greater for both impact groups compared to the active (p?<?0.001) and raw (p?<?0.001) groups, with all low impact samples and 6 of 8 high impact samples surviving 105 cycles. The mean (± SD) number of cycles to failure for the active and raw groups was 12,133±11,704 and 16,552±29,612, respectively. The results suggest that loading rates associated with the impact phase of a typical vGRF in running have little influence on the mechanical fatigue behavior of bone relative to loading magnitude, warranting further investigation of the mechanism by which increased loading rates are associated with stress fracture.
| S-EPMC5798456 | biostudies-literature
Project description:Although acellular cementum is essential for tooth attachment, factors directing its development and regeneration remain poorly understood. Inorganic pyrophosphate (PPi), a mineralization inhibitor, is a key regulator of cementum formation: tissue-nonspecific alkaline phosphatase (Alpl/TNAP) null mice (increased PPi) feature deficient cementum, while progressive ankylosis protein (Ank/ANK) null mice (decreased PPi) feature increased cementum. Bone sialoprotein (Bsp/BSP) and osteopontin (Spp1/OPN) are multifunctional extracellular matrix components of cementum proposed to have direct and indirect effects on cell activities and mineralization. Studies on dentoalveolar development of Bsp knockout (Bsp-/-) mice revealed severely reduced acellular cementum, however underlying mechanisms remain unclear. The similarity in defective cementum phenotypes between Bsp-/- mice and Alpl-/- mice (the latter featuring elevated PPi and OPN), prompted us to examine whether BSP is operating by modulating PPi-associated genes. Genetic ablation of Bsp caused a 2-fold increase in circulating PPi, altered mRNA expression of Alpl, Spp1, and Ank, and increased OPN protein in the periodontia. Generation of a Bsp knock-out (KO) cementoblast cell line revealed significantly decreased mineralization capacity, 50% increased PPi in culture media, and increased Spp1 and Ank mRNA expression. While addition of 2?g/ml recombinant BSP altered Spp1, Ank, and Enpp1 expression in cementoblasts, changes resulting from this dose were not dependent on the integrin-binding RGD motif or MAPK/ERK signaling pathway. Decreasing PPi by genetic ablation of Ank on the Bsp-/- mouse background reestablished cementum formation, allowing >3-fold increased acellular cementum volume compared to wild-type (WT). However, deleting Ank did not fully compensate for the absence of BSP. Bsp-/-; Ank-/- double-deficient mice exhibited mean 20-27% reduced cementum thickness and volume compared to Ank-/- mice. From these data, we conclude that the perturbations in PPi metabolism are not solely driving the cementum pathology in Bsp-/- mice, and that PPi is more potent than BSP as a cementum regulator, as shown by the ability to override loss of BSP by lowering PPi. We propose that BSP and PPi work in concert to direct mineralization in cementum and likely other mineralized tissues.
| S-EPMC5730356 | biostudies-literature
Project description:The H(+) ion dissociation of bone sialoprotein in 0.2m-sodium chloride at 25 degrees was studied. The total content of carboxyl groups available for titration was calculated by comparing the titration curve with the titration curves of three model systems and by the use of analytical data. This comparison showed that 7.0 carboxyl groups/mol. do not participate in the titration, and it is proposed that these are aspartic acid or glutamic acid carboxyl groups present as amides; this is also indicated by titration of the sialoprotein after acid hydrolysis. The titration of carboxyl groups was found to agree well with the Linderstrøm-Lang equation for spherical macroions.
| S-EPMC1198438 | biostudies-other