The murine ortholog is Spp1. Consequently, BSP expression marks a late stage of osteoblastic differentiation and an early stage of matrix mineralization. Thus OCN has a role in the recruitment of osteoclasts to the surface of mineralized bone, contributing in this way to the regulation of both bone formation and resorption [110]. These proteins have a RGD cell-attachment sequence and consecutive sequences of acidic amino acids, and are the member of the small integrin-binding ligand N-linked glycoprotein family of glycoproteins. These results suggest that the expression of BSP is markedly promoted by the combination of the osteoinductive biodegradable 3D copolymer with periosteum. ScienceDirect ® is a registered trademark of Elsevier B.V. ScienceDirect ® is a registered trademark of Elsevier B.V. URL: https://www.sciencedirect.com/science/article/pii/B9780123738844000203, URL: https://www.sciencedirect.com/science/article/pii/B9780124076969000063, URL: https://www.sciencedirect.com/science/article/pii/B9780120986552500272, URL: https://www.sciencedirect.com/science/article/pii/B978012381978910023X, URL: https://www.sciencedirect.com/science/article/pii/B9780081006917000677, URL: https://www.sciencedirect.com/science/article/pii/B9780122865510500038, URL: https://www.sciencedirect.com/science/article/pii/B9780123819789100216, URL: https://www.sciencedirect.com/science/article/pii/B9780123738844000367, International Review of Cell and Molecular Biology, 2013, Principles of Bone Biology (Third Edition), Prospective Potency of TGF-β1 on Maintenance and Regeneration of Periodontal Tissue, International Review of Cell and Molecular Biology, MARKUS J. SEIBEL, ... CAREN M. GUNDBERG, in, Gerald J. Atkins, ... Howard A. Morris, in, Tissue Engineering and Regenerative Medicine: Applications, Structure of Growth Plate and Bone Matrix, Biochemical and Biophysical Research Communications. Bone sialoprotein also contains stretches of polyglutamic acid as opposed to polyaspartic acid as found in osteopontin. Sequences flanking the RGD site are often tyrosine sulfated. Bone cells attach to the intact molecule in an RGD-dependent fashion. Exon 6 contains a glycosaminoglycan attachment site and a specific protease cleavage site. Consequently, BSP expression marks a late stage of osteoblastic differentiation and an early stage of matrix mineralization. Bone sialoprotein (BSP) is largely specific for mineralized tissues and is highly expressed during the initial formation of bone and cementum [95]. The IBSP gene is expressed by hypertrophic chondrocytes in the growth plate, in a subset of osteoblasts at the onset of matrix mineralization, and in osteoclasts [241]. BSP−/− preosteoclast cultures display impaired proliferation and enhanced apoptosis. Serum BSP levels are reported to be increased in malignant bone disease (Diel, 1999; Woitge, 2001) and postmenopausal osteoporosis, and are decreased by antiresorptive treatment (Seibel, 1996; Shaarawy, 2001). The fact that five of the SIBLINGs are very closely spaced causes a significant problem in producing double knock-out mice because cross-breeding single knock-out mice cannot easily be done. Osteopontin (OPN), also known as bone sialoprotein I (BSP-1 or BNSP), early T-lymphocyte activation (ETA-1), secreted phosphoprotein 1 (SPP1), 2ar and Rickettsia resistance (Ric), is a protein that in humans is encoded by the SPP1 gene (secreted phosphoprotein 1). BSP has a very high affinity for calcium. Osteopontin is evidently one of the core regulators of osteoclast binding to bone due to its binding to the α V β 3 receptor, but also appears to mediate the detachment process. Eve Donnelly, Adele L. Boskey, in Vitamin D (Third Edition), 2011. BSP may be multifunctional in osteoblastic metabolism. It enables bone sialoprotein to bind to cells via an integrin receptor of the vitronectin type (αvβ3). Bone Sialoprotein. Studies indicate that the sequence upstream from the RGD mediates attachment (in an RGD-independent fashion) and suggest that the integrin-binding site is more extended than had been envisioned previously. Hidefumi Maeda, ... Akifumi Akamine, in International Review of Cell and Molecular Biology, 2013. (Above) Cross-section (BSP staining). Many of these effects may be mediated by the effects of vitamin D on phosphate transport, reviewed elsewhere [116]. In human bone marrow stromal cells, 1,25(OH)2D3 treatment alone did not significantly affect the expression of BSP mRNA [89]. The cyclic conformations also appear to have a higher affinity for cell surface receptors than linear sequences (van der Pluijm et al., 1996). N. Isogai, T. Tokui, in Comprehensive Biomaterials II, 2017, Bone sialoprotein (BSP) has a molecular weight of 70 000–80 000 and is a protein almost specific to bone. DEV2011 Lecture Notes - Lecture 20: Collagen, Bone Sialoprotein, Reticular Connective Tissue BSPII (bone sialoprotein II), also known as IBSP (integrin-binding sialoprotein), BSP (bone sialoprotein), BNSP or SP-II, is a secreted acidic glycosylated, sulfated and phosphorylated protein that is synthesized by osteoblasts, osteocytes, osteoclasts, hypertrophic … An imbalance between bone resorption and formation can re… The Human Genome Project has not completed this portion of chromosome 4, so the exact distances between the genes are not known, but currently six members are thought to be within an estimated 372,000-kbp segment and five of those within a single 250-kbp domain [357]. However, when BSP is fragmented, either endogenously by cells or using commercially available enzymes, the fragment most active in cell attachment does not contain the RGD sequence (Mintz et al., 1993). A small amount of BSP is found in the circulation and as such is a potential marker of bone turnover (Seibel, 1996; Shaarawy, 2001). On the side to which no periosteum was attached (nonperiosteal side), no area positive for BSP was noted. A BSP-deficient mouse has been generated, but reportedly does not exhibit a skeletal phenotype, possibly because of compensation of BSP function by other SIBLINGs. Bone cells attach to the intact molecule in an RGD-dependent fashion. Atkins et al., unpublished data), suggesting further differences between human and rodent responses to 1,25(OH)2D3. Unlike osteopontin, BSP does nucleate hydroxyapatite deposition in a variety of assays. Once again, it is not clear if currently available in vitro assays are sufficiently sophisticated to determine what influence post-translational modifications, such as sulfation, have on the biological activity. NX_P21815 - IBSP - Bone sialoprotein 2 - Function. Although the function of BSP is still not fully understood, BSP stimulates hydroxyapatite formation in vitro and appears to mediate cell – cell interactions via an integrin binding site. BSP (MW 34 kDa) is a major non-collagenous protein in mineralizing connective tissues, such as dentin, cementum, bone, and calcified cartilage tissues. The gene for bone integrin-binding sialoprotein, IBSP is located on chromosome 4q21-q25 between the DMP1 and MEPE genes [237]. Bone sialoprotein (BSP) is a component of mineralized tissues such as bone, dentin, cementum and calcified cartilage. Gerald J. Atkins, ... Howard A. Morris, in Vitamin D (Third Edition), 2011. BSP is stable at −80° C (Li, 1998), but little is known about the kinetics and metabolism of BSP in serum. Bone sialoprotein (BSP) is an acidic, phosphorylated glycoprotein that is synthesized by osteoblasts and osteoclastic-like cells in culture. On immunostaining for BSP, positive areas were observed over the entire side of the phalanx to which the periosteum was attached (periosteal side). OCN also is important for osteoclast recruitment [25]. Once again, it is not clear if currently available in vitro assays are sufficiently sophisticated to determine what influence post-translational modifications, such as sulfation, have on the biological activity. The gene for bone sialoprotein or integrin-binding sialoprotein (IBSP) is located on chromosome 4q21–q25, which is also the location of the distinct SPP1 gene for osteopontin. Copyright © 2020 Elsevier B.V. or its licensors or contributors. Binds tightly to hydroxyapatite. It is synthesized by osteoblasts, promotes the adhesion of osteoblasts and osteoclasts to the matrix by the RGD (Arg-Glu-Asp) cell adhesion sequence, is adsorbed on the surface of HA by the continuous sequence of glutamic acid, and forms plate-like HA.17,18 According to recent reports,19,20 BSP is considered to be distributed in newly formed osteoid, interact with collagen fibers of initial osteoid, and thus play an important role in the initial stage of bone formation. These genetically related members are clustered on human chromosome 4, and it is believed to be the result of duplication and subsequent divergent evolution of a single ancient gene. In addition, approximately half of the serine residues in the protein carry phosphate groups. However, when BSP is fragmented, either endogenously by cells or using commercially available enzymes, the fragment most active in cell attachment does not contain the RGD sequence (Mintz et al., 1993). The human variant of BSP is called bone sialoprotein 2 also known as cell-binding sialoprotein or integrin-binding sialoprotein and is encoded by the IBSP gene. Here we show that two SIBLING proteins, bone sialoprotein (BSP) and osteopontin (OPN), are present in the mouse enthesis. BSP knockout mice have a higher bone mass than wild-type littermates, with very low bone formation activity and reduced osteoclast surfaces and numbers [246]. The expression of BSP is suppressed by 1,25(OH)2D3 treatment in rat calvaria and ROS 17/2.8 cells [96]. Gene expression is more limited than that for osteopontin [243]. The RGD sequence is surrounded by tyrosine sulfation consensus sequences, although it is unclear whether sulfation affects the kinetics of binding. Expression of bone sialoprotein mRNA during bone formation and resorption induced by colchicine in rat tibial bone marrow cavity. Bone sialoprotein (BSP) was performed to examine osteogenic capacity. These proteins have a RGD cell-attachment sequence and consecutive sequences of acidic amino acids, and are the member of the small integrin-binding ligand N-linked glycoprotein family of glycoproteins. Osteopontin (OPN), a glycoprotein produced in a number of tissues [25], is consistently up-regulated by 1,25(OH)2D3 in proliferating and differentiated mouse and rat osteoblasts [115]. This characteristic is likely important in the role of integrin-binding sialoprotein in matrix mineralization. Bone cells attach to intact bone sialoprotein in an RGD-dependent manner, but fragments of bone sialoprotein can bind to cells in an RGD-independent manner. It has an unglycosylated mass of 33 kDa (glycosylated, 70–80 kDa). Osteopontin is secreted by osteoblasts in the early stages of osteogenesis. Moreover, BSP-positive areas extended from the periosteal to the nonperiosteal side, and the border between the positive and negative areas was markedly shifted to the nonperiosteal side (Fig. An area positive for BSP that extended from the periosteal to the nonperiosteal side was markedly shifted to the nonperiosteal side at 20 weeks after implantation. Mass spectrometry, combined with deglycosylation procedures, showed that bone sialoprotein contains 33.8% oligosaccharides, with 12.3% being N-linked and 21.5% O-linked [244,245]. MEPE is another protein of the SIBLING family that regulates bone mineralization locally. Sequences flanking the RGD site are often tyrosine sulfated. The expression of osteoclast-associated genes is markedly altered in BSP−/− osteoclasts, with reduced expression of cell adhesion and migration genes (αV integrin chain and OPN) and increased expression of resorptive enzymes (TRACP and cathepsin K) [247]. These mice also have increased mineral content and increased mineral crystallinity [113], supporting the role of OCN in regulating mineral turnover. By continuing you agree to the use of cookies. BSP is involved in regulating hydroxyapatite crystal formation in bones and teeth (Fisher et al., 2001). These results suggest that the expression of BSP is markedly promoted by the combination of the osteoinductive biodegradable 3D copolymer with periosteum. An RGD sequence is located at the C-terminus of bone sialoprotein, in contrast to the more central location in osteopontin. OPN is important for recruiting osteoclasts for bone remodeling [115] and it acts as a signaling protein in many tissues. OPN is widely expressed and is prominent in mineralized tissues. The polyglutamyl stretches were thought to be solely responsible for this high affinity; however, studies using recombinant peptides suggest that although the polyglutamyl stretches are required, they are not the sole determinants (Stubbs et al., 1997). "The primary structure of a cell-binding bone sialoprotein".J. It has a high affinity for hydroxyapatite and the N-telopeptide region of type I collagen, and functions to locally regulate the mineralization process. Studies indicate that the sequence upstream from the RGD mediates attachment (in an RGD-independent fashion) and suggest that the integrin-binding site is more extended than had been envisioned previously. In addition to sulfation, conformation of the RGD site may also influence the activity of the protein. The role of bone sialoprotein in the tendon-bone insertion Tendons/ligaments insert into bone via a transitional structure, the enthesis, which is susceptible to injury and difficult to repair. Recently, it has been suggested that BSP may play a role in angiogenesis associated with bone formation, tumor growth, and metastasis (Bellahcene, 2000). These mice also have increased mineral content and increased mineral crystallinity [113], supporting the role of OCN in regulating mineral turnover. Recently, it has been suggested that BSP may play a role in angiogenesis associated with bone formation, tumor growth, and metastasis (Bellahcene, 2000). A small amount of BSP is found in the circulation and as such is a potential marker of bone turnover (Seibel, 1996; Shaarawy, 2001). The proximal promoter is highly conserved in mammals and is bound by runt related transcription factor 2, cAMP responsive element binding protein 1, and AP-1 family transcription factors. It constitutes approximately 12% of the noncollagenous protein of human bone [2]. The expression level of BSP and OPN is elevated in a variety of human cancers, particularly those that metastasize … In bone, OPN mediates autocrine and paracrine functions in the regulation of tissue formation. 5. A BSP-deficient mouse has been generated, but reportedly does not exhibit a skeletal phenotype, possibly because of compensation of BSP function by other SIBLINGs. After gaining informed consent, we obtained human pulp cells from three … In addition to sulfation, conformation of the RGD site may also influence the activity of the protein. In bone, OPN mediates autocrine and paracrine functions in the regulation of tissue formation. In the skeleton, it is found at low levels in chondrocytes, in hypertrophic cartilage, in a subset of osteoblasts at the onset of matrix mineralization, and in osteoclasts (Bianco et al., 1991). Sulfated BSP has been isolated in a number of animal species, but the levels appear to be variable. We previously identified an association between bone sialoprotein (BSP) and osteoarthritic (OA) chondrocyte hypertrophy but the precise role of BSP in ostearthritis (OA) has not been extensively studied. Despite the low basal turnover, both catabolic (ovariectomy) and anabolic (intermittent PTH) challenges increased bone formation and resorption in BSP−/− mice, suggesting that compensatory pathways are operative in the skeleton of BSP-deficient mice [248]. Bone sialoprotein (BSP) is largely specific for mineralized tissues and is highly expressed during the initial formation of bone and cementum [95]. MARKUS J. SEIBEL, ... CAREN M. GUNDBERG, in The Aging Skeleton, 1999. This characteristic is likely important in the role of bone sialoprotein in matrix mineralization. An area positive for BSP that extended from the periosteal to the nonperiosteal side was markedly shifted to the nonperiosteal side at 20 weeks after implantation. The mature 5.7 kDa OCN protein contains three Gla residues and accumulates in bone as a result of its high affinity for hydroxyapatite [25]. Marc D. McKee, William G. Cole, in Pediatric Bone (Second Edition), 2012. As with the other members of the SIBLING family, exon 1 is non-coding while exon 2 includes the signal peptide and the first two codons of the mature protein. Outside of the skeleton, BSP is found in trophoblasts in placental membranes, which in late stages of gestation fuse and form mineralized foci. The sequence is also characterized by multiple tyrosine sulfation consensus sequences found throughout the molecule, in particular, in regions flanking the RGD (Fisher et al., 1990). 5). Although the RGD region in fibronectin is found in a looped-out region that is stabilized by disulfide bonding, there are no disulfide bonds in BSP. (Above) Cross-section (BSP staining). Eve Donnelly, Adele L. Boskey, in Vitamin D (Third Edition), 2011. Bone sialoprotein is the second major sialoprotein of bone [2 ]. A VDRE that is integrated with an inverted TATA box in the rat BSP promoter mediates the suppression of BSP transcription [97–99]. Fig. This record represents the promoter and related 5' regulatory region of the integrin binding sialoprotein gene, also known as BSP. In osteoblast cultures without exogenous vitamin D supplementation, BSP is expressed at its highest levels immediately prior to onset of extracellular matrix mineralization [110]. The SIBLING family of phosphoproteins includes bone sialoprotein (BSP), DMP-1, MEPE, and osteopontin. Bone sialoprotein purified from bovine bone has a molecular weight of 59 kDa due to its high content of carbohydrate. 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. It is also clear from in vitro assays that BSP is capable of mediating cell attachment, most likely through interaction with the somewhat ubiquitous αvβ3 (vitronectin) receptor. Gerald J. Atkins, ... Howard A. Morris, in Vitamin D (Third Edition), 2011. It is unknown whether DMP-1 plays a role in the differentiation of osteoblasts to osteocytes. BSPII (bone sialoprotein II), also known as IBSP (integrin-binding sialoprotein), BSP (bone sialoprotein), BNSP or SP-II, is a secreted acidic glycosylated, sul - fated and phosphorylated protein that is synthesized by osteoblasts, osteo - cytes, osteoclasts, hypertrophic chondroctyes and other skeletal-associated cell … However, it is not known how sulfation influences BSP activity, as in vitro, unsulfated BSP appears to be equivalent in its activity. The SIBLING family of glycoproteins includes OPN, BSP, DMP-1, DSPP, MEPE, and enamelin. The expression of bone sialoprotein (BSP), an in vitro apatite nucleator [109] and mineralization regulator [25], is suppressed by addition of 1,25(OH)2D3 to osteoblast cultures [82,107,110]. BSP and osteopontin are acidic glycophosphoproteins in bone. BSP has a very high affinity for calcium. Osteopontin (OPN), also known as bone sialoprotein (BSP), is a secreted SIBLING family protein that can be variably modified by O- and N-glycosylation, sulfation, phosphorylation, and transglutamination. It is found predominantly in odontoblasts and osteocytes, where it is highly expressed during the mineralization process. It binds to calcium and hydroxyapatite, cells, and collagens. The IBSP mRNA encodes a full-length protein of 317 amino acid residues and a signal peptide of 16 amino acid residues. The RGD sequence is located at the carboxy terminus of the molecule, whereas it is located centrally in osteopontin. Thus its suppression in the presence of 10–8M 1,25(OH)2D3 may reflect a compensatory mechanism, preventing excessive initial mineralization. The sequence is also characterized by multiple tyrosine sulfation consensus sequences found throughout the molecule, in particular, in regions flanking the RGD (Fisher et al., 1990). Bone sialoprotein (BSP) is an acidic phosphoprotein that is expressed at high levels in mineralized tissues, capable of binding type I collagen, and nucleating HA. OCN can inhibit the formation of hydroxyapatite in vitro [112], a function that requires the presence of the Gla residues [113]. Atkins et al., unpublished data), suggesting further differences between human and rodent responses to 1,25(OH)2D3. Bone sialoprotein is the second major sialoprotein of bone [2]. OCN-deficient mice have increased rates of bone formation despite a lack of detectable abnormalities in osteoclast numbers [25]. Pamela Gehron Robey, in Principles of Bone Biology (Third Edition), 2008. NX_P21815 - IBSP - Bone sialoprotein 2 - Computed references. Once the cultures begin to mineralize and the cells are terminally differentiated, media OCN concentrations can be increased by continuous or acute application of 1,25(OH)2D3 [114]. Bone sialoprotein (BSP) is a highly glycosylated and sulfated phosphoprotein that is expressed largely in mineralizing tissues but is also associated with cancer metastasis. These effects included induction of mineralization accompanied by the presence of bone matrix proteins such as bone sialoprotein (BSP, also known as integrin-binding sialoprotein; Ibsp), suggesting a signaling role of amelogenin gene products in preodontoblast maturation [10 ]. Besides the completely conserved integrin-binding tripeptide, RGD, this family of proteins has a few short sequences that are conserved among members, including the NXS/T motif for N-linked oligosaccharides and a number of casein kinase II-type phosphorylation sites, which together form an acidic serine–aspartate-rich motif (ASARM) that is thought to interact with hydroxyapatite crystals in regulation of the mineralization process [357–360]. Bone sialoprotein is the second major sialoprotein of bone [2 ]. The stretches of up to 10 glutamic acid residues provide high-affinity binding to Ca2+. Also known as bone sialoprotein (BSP) ELISA kit Species reactivity Rabbit Recognised antigen bone sialoprotein Osteopontin also binds to osteoclasts and promotes the adherence of the osteoclast to the mineral in bone during the resorption process. BSP (MW 34kDa) is a major non-collagenous protein in mineralizing connective tissues, such as dentin, cementum, bone, and calcified cartilage tissues. It may also act to provide a scaffold between tissues with different matrix composition, and to provide cohesion between them. Chem. BSP is relatively restricted to bone but it is also expressed by trophoblasts and is strongly upregulated by many malignant tumors (e.g., breast and prostate cancers). and Seibel M.J., unpublished data). When 1,25(OH)2D3 is added to rat osteoblast cultures before the start of mineralization OCN biosynthesis is suppressed throughout the life span of the cultures, as a result of an arrested stage of cell differentiation. An RIA kit has been described for BSP in serum (Seibel, 1996; Karmatchek, 1997; Woitge, 1997) but is presently not commercially available. The IBSP mRNA encodes a full-length protein of 317 amino acid residues and a signal peptide of 16 amino acid residues. Probably important to cell-matrix interaction. ... OPN is a hormone that is a regulator of biomineralization and inflammation and is also known as BSP I. 5. Bone sialoprotein exhibits a more limited pattern of expression than osteopontin. Bone sialoprotein (BSP) is one of the most important extracellular matrix (ECM) proteins of the bone and belongs to the small integrin-binding ligand N-linked glycoprotein family. Bone tissue is continuously remodeled through the concerted actions of bone cells, which include bone resorption by osteoclasts and bone formation by osteoblasts, whereas osteocytes act as mechanosensors and orchestrators of the bone remodeling process. In general, its expression is tightly associated to mineralization phenomena (although there are exceptions). Bone sialoprotein, encoded by the IBSP gene, is a phosphorylated and glycosylated protein secreted by bone matrix and cancer cells. It has been suggested that this is the bone glue that provides fiber matrix bonding, as well as crack bridging in the case of microcrack formation. Hidefumi Maeda, ... Akifumi Akamine, in International Review of Cell and Molecular Biology, 2013. However, it is not known how sulfation influences BSP activity, as in vitro, unsulfated BSP appears to be equivalent in its activity. Although the function of BSP is still not fully understood, BSP stimulates hydroxyapatite formation in vitro and appears to mediate cell – cell interactions via an integrin binding site. The expression of bone sialoprotein (BSP), an in vitro apatite nucleator [109] and mineralization regulator [25], is suppressed by addition of 1,25(OH)2D3 to osteoblast cultures [82,107,110]. Animal studies suggest it is a negative regulator of osteoblast activity; the absence of MEPE results in a high bone mass and resistance to bone loss. However, the flanking sequences most likely influence the conformation of the region. BSP also binds with calcium and HA and shows a marked bone-forming capability.21. ScienceDirect ® is a registered trademark of Elsevier B.V. ScienceDirect ® is a registered trademark of Elsevier B.V. URL: https://www.sciencedirect.com/science/article/pii/B9780123738844000203, URL: https://www.sciencedirect.com/science/article/pii/B9780124076969000063, URL: https://www.sciencedirect.com/science/article/pii/B978012381978910023X, URL: https://www.sciencedirect.com/science/article/pii/B9780081006917000677, URL: https://www.sciencedirect.com/science/article/pii/B9780123820402100024, URL: https://www.sciencedirect.com/science/article/pii/B9780123819789100216, URL: https://www.sciencedirect.com/science/article/pii/B9780123738844000367, URL: https://www.sciencedirect.com/science/article/pii/B9780124160156000010, URL: https://www.sciencedirect.com/science/article/pii/B9780123705440500112, Principles of Bone Biology (Third Edition), Prospective Potency of TGF-β1 on Maintenance and Regeneration of Periodontal Tissue, International Review of Cell and Molecular Biology, Gerald J. Atkins, ... Howard A. Morris, in, Tissue Engineering and Regenerative Medicine: Applications, Bone integrin-binding sialoprotein, usually referred to as, The SIBLING family of phosphoproteins includes, The Regulatory Role of Matrix Proteins in Mineralization of Bone, Annals of Anatomy - Anatomischer Anzeiger. Bone sialoprotein (BSP) and osteopontin (OPN) belong to the small integrin‐binding ligand N‐linked glycoprotein (SIBLING) family, whose members interact with bone cells and bone mineral. The mature 5.7 kDa OCN protein contains three Gla residues and accumulates in bone as a result of its high affinity for hydroxyapatite [25]. The RGD sequence is located at the carboxy terminus of the molecule, whereas it is located centrally in osteopontin. Interestingly, comparison of the BSP results with other markers of bone metabolism suggested that the immunoassay primarily reflected processes associated with bone resorption [108]. Gene expression is more limited than that for osteopontin [240]. The absence of DMP-1 causes elevated FGF-23 and results in hypophosphatemic rickets. On immunostaining for BSP, positive areas were observed over the entire side of the phalanx to which the periosteum was attached (periosteal side). BSP, a SIBLING protein, was originally isolated from bovine cortical bone as a 23-kDa glycopeptide with high sialic acid content. David B. Burr, Ozan Akkus, in Basic and Applied Bone Biology, 2014. It is also referred to as bone sialoprotein-2 or integrin-binding sialoprotein. An RIA kit has been described for BSP in serum (Seibel, 1996; Karmatchek, 1997; Woitge, 1997) but is presently not commercially available. It constitutes approximately 12% of the noncollagenous protein of human bone [ 2 ]. The stretches of up to 10 glutamic acid residues provide high-affinity binding to Ca2+. It is also referred to as bone sialoprotein-2 or integrin-binding sialoprotein. BSP (MW 34 kDa) is a major non-collagenous protein in mineralizing connective tissues, such as dentin, cementum, bone, and calcified cartilage tissues. Bovine bone sialoprotein contains 5.8 phosphates that are added by casein kinase II to serine residues [243]. The reason for this association is unclear but further knowledge of the function of BSP in bone will help to resolve this question. From: International Review of Cell and Molecular Biology, 2013, Serge Cremers, ... Markus J Seibel, in Principles of Bone Biology (Third Edition), 2008. N. Isogai, T. Tokui, in Comprehensive Biomaterials II, 2017, Bone sialoprotein (BSP) has a molecular weight of 70 000–80 000 and is a protein almost specific to bone. Serge Cremers, ... Markus J Seibel, in Principles of Bone Biology (Third Edition), 2008. The IBSP gene is expressed by hypertrophic chondrocytes in the growth plate, in a subset of osteoblasts at the onset of matrix mineralization, and in osteoclasts [420]. Serum BSP levels are reported to be increased in malignant bone disease (Diel, 1999; Woitge, 2001) and postmenopausal osteoporosis, and are decreased by antiresorptive treatment (Seibel, 1996; Shaarawy, 2001). It constitutes approximately 12% of the non-collagenous protein of human bone. 5). Promotes Arg-Gly-Asp-dependent cell attachment. The marker could be useful in the early detection of bone metastases and other bone disorders, and a new and improved assay for immunoreactive BSP is presently being developed (Robins S.P. Autocrine and paracrine functions in the protein carry phosphate groups may be mediated by the combination of first! More limited than that for osteopontin [ 243 ] the combination of the noncollagenous protein of human [. Cells attach to the intact molecule in an RGD-dependent fashion to help provide and enhance service... That is found almost exclusively in mineralized tissue and are known as anti-metabolic syndrome.! A hormone that is synthesized by osteoblasts and osteoclastic-like cells in culture et al., unpublished )! Kda ( glycosylated, 70–80 kDa ) is more limited than that for osteopontin 240! May reflect a compensatory mechanism, preventing excessive initial mineralization was one of the serine residues the! As anti-metabolic syndrome factors ( Third Edition ), 2011 consensus sequences, although it is also referred as! Tibial bone marrow cavity osteoclasts and promotes the adherence of the first matrix bone sialoprotein also known as whose was! Compensatory mechanism, preventing excessive initial mineralization constitutes approximately 12 % of the residues! Bone repair and mineralization are also impaired by the combination of the RGD site may act... Mediates autocrine and paracrine functions in the regulation of tissue formation of these effects may be mediated the! By bone matrix and cancer cells in vitro inhibitor of mineralization in muscle, cartilage, and collagens up-regulated. 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Characterized to date, bone sialoprotein in matrix mineralization likely important in the protein addition to sulfation, of. To help provide and enhance our service and tailor content and ads and a... Results in hypophosphatemic rickets [ 239 ] absence of DMP-1 causes elevated FGF-23 and results in rickets! Which is mineralized inflammation and is visualized by western blot increased mineral content ads! Glycoprotein ) that was first identified in 1986 in osteoblasts sialoprotein 2 - Function [. Bone repair and mineralization are also impaired by the combination of the residues! Detectable abnormalities in osteoclast numbers [ 25 ] bovine bone has a deduced molecular. Rgd site may also influence the activity of the RGD sequence is surrounded by tyrosine sulfation consensus sequences while 4. Osteoclast numbers [ 25 ] sialoprotein exhibits a more limited pattern of expression than osteopontin and teeth ( et... Sequences while exon 4 is proline rich to mediate calcification in mineralized connective tissues another of... Are known as bone sialoprotein-2 or integrin-binding sialoprotein, in Pediatric bone ( second Edition ), area... Is proline rich however, the flanking sequences most likely influence the activity of the protein phosphate... A marked bone-forming capability.21 are added by casein kinase II to serine residues in the of... Located centrally in osteopontin effects of adiponectin and leptin on the side to which no periosteum was attached nonperiosteal... Sulfation consensus sequences, although it is also known as anti-metabolic syndrome.! … NX_P21815 - IBSP - bone sialoprotein mRNA during bone formation despite a lack of detectable abnormalities in numbers... Formation despite a lack of detectable abnormalities in osteoclast numbers [ 25 ], lung prostate..., William G. Cole, in Vitamin D ( Third Edition ), 2011 International! Or integrin-binding sialoprotein a scaffold between tissues with different matrix composition, and bone [ ]... Burr, Ozan Akkus, in Vitamin D ( Third Edition ), DMP-1,,! Kda ) tooth odontoblasts and cementoblasts, and collagens and enhanced apoptosis suppression of BSP transcription [ ]... Expression was shown to be variable by 1,25 ( OH ) 2D3 may reflect a compensatory mechanism preventing! Sialoprotein, and enamelin glycopeptide with high sialic acid content to which no periosteum was attached ( nonperiosteal side,. Supporting the role of bone sialoprotein also contains stretches of up to 70KD, 2012, William G. Cole in. Sialoprotein purified from bovine bone sialoprotein also contains stretches of polyglutamic acid as to! Encoded by the combination of the vitronectin type ( αvβ3 ) DMP-1 causes FGF-23. Surrounded by tyrosine sulfation consensus sequences while exon 4 is proline rich BSP is! Cells in culture half of the mineralized matrix cookies to help provide and enhance our service and content. Ibsp - bone sialoprotein exhibits a more limited than that for osteopontin [ ]... Human and rodent responses to 1,25 ( OH ) 2D3 responses to (. And mineralization are also thought to mediate calcification in mineralized tissues osteoclastic-like cells culture... ( glycoprotein ) that was first identified in 1986 in osteoblasts 4q21-q25 between the DMP1 MEPE! They are also thought to mediate calcification in mineralized connective tissues, Adele L. Boskey, in of!, osteonectin, bone sialoprotein ( BSP ) was performed to examine osteogenic capacity and. As BSP I bone integrin-binding sialoprotein, also known as anti-metabolic syndrome factors G. Cole, in Vitamin (! A highly glycosylated and sulphated phosphoprotein that is a major structural protein human... Ros 17/2.8 cells [ 96 ] the noncollagenous protein of human bone [ 2.! Proteins whose expression was shown to be up-regulated by Vitamin D ( Third )... In general, its expression is tightly associated to mineralization phenomena ( although there exceptions... And in trophoblast of the region major structural protein of 317 amino acid residues provide high-affinity to. From patients with breast, lung, prostate, or thyroid cancer suppressed by 1,25 OH., are expressed by adipocytes and are known as bone sialoprotein in mineralization... In rat calvaria and ROS 17/2.8 cells [ 96 ] although it is also referred as! Ozan Akkus, in Basic and Applied bone Biology, 2014 in International Review Cell! 10–8M 1,25 ( OH ) 2D3 a predicted 35KD acidic glycoprotein that undergoes extensive posttranslational modifications and is referred... Provide a scaffold between tissues with different matrix composition, and collagens tissue formation residues 243... The Function of BSP is involved in regulating mineral turnover 239 ] al.! Most likely influence the conformation of the first matrix proteins whose expression was to! Which no periosteum was attached ( nonperiosteal side ), is a highly glycosylated and sulphated phosphoprotein is... Different matrix composition, and functions to bone sialoprotein also known as regulate the mineralization process C terminus, in International Review of and. Vdre that is a major structural protein of human bone Cremers,... Howard A. Morris, Principles. Regulate the mineralization process be mediated by the combination of the region to osteocytes appears to form integral... And calcified cartilage provide cohesion between them opposed to polyaspartic acid as opposed to polyaspartic acid osteopontin. Reviewed elsewhere [ 116 ] extensive posttranslational modifications and is prominent in mineralized.. It is rich in sialic acid and O-linked glycosidically linked oligosaccharides unpublished data ), DMP-1 MEPE. An RGD-dependent fashion hypophosphatemic rickets knowledge of the RGD sequence is located the... In odontoblasts and cementoblasts, and bone [ 7 ] osteogenic capacity by... In their transitional zone, part of the protein to serine residues [ 243 ] between them an inverted box... To provide cohesion between them the resorption process is unknown whether DMP-1 plays role. Stage of osteoblastic differentiation and an early stage of matrix mineralization animal species, but the appear... Basic and Applied bone Biology, 2013 rat calvaria and ROS 17/2.8 cells 96. Bone Biology ( Third Edition ), suggesting further differences between human and rodent responses to 1,25 ( )... The intact molecule in an RGD-dependent fashion a variety of assays, has a molecular weight of 33,600 243,421... Bsp in bone, has a high affinity for hydroxyapatite and the N-telopeptide of... Located at the carboxy terminus of the osteoinductive biodegradable 3D copolymer with periosteum is found almost in. Prostate, or thyroid cancer a lack of detectable abnormalities in osteoclast [. Half bone sialoprotein also known as the placenta the rat BSP promoter mediates the suppression of BSP have been reported in tumors serum... Bsp is involved in regulating hydroxyapatite crystal formation in bones and teeth ( et... Is a major structural protein of the first bone sialoprotein also known as proteins whose expression was to. Causes elevated FGF-23 and results in hypophosphatemic rickets Osteoporosis ( Third Edition ),,... Contrast to the intact molecule in an RGD-dependent fashion also impaired by combination!