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bone sialoprotein also known as

Previously, we showed that BSP knockout ( BSP −/− ) mice have a higher bone mass than wild type ( BSP +/+ ) littermates, with very low bone‐formation activity and reduced osteoclast surfaces and numbers. Sulfated BSP has been isolated in a number of animal species, but the levels appear to be variable. Bone sialoprotein purified from bovine bone has a molecular weight of 59 kDa due to its high content of carbohydrate. 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). 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. BSP is involved in regulating hydroxyapatite crystal formation in bones and teeth (Fisher et al., 2001). 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]. Atkins et al., unpublished data), suggesting further differences between human and rodent responses to 1,25(OH)2D3. 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. BSP also binds with calcium and HA and shows a marked bone-forming capability.21. An RGD sequence is located at the C-terminus of bone sialoprotein, in contrast to the more central location in osteopontin. 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. Bone integrin-binding sialoprotein, usually referred to as bone sialoprotein (BSP), is the second major sialoprotein of bone [7]. Elevated levels of BSP have been reported in tumors and serum from patients with breast, lung, pros-tate, or thyroid cancer [2]. They are also thought to mediate calcification in mineralized tissue. The RGD sequence is located at the carboxy terminus of the molecule, whereas it is located centrally in osteopontin. Bone sialoprotein also contains stretches of polyglutamic acid as opposed to polyaspartic acid in osteopontin. Bone cells attach to the intact molecule in an RGD-dependent fashion. Bone sialoprotein is a predicted 35KD acidic glycoprotein that undergoes extensive posttranslational modifications and is visualized by western blot at up to 70KD. 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). It may also act to provide a scaffold between tissues with different matrix composition, and to provide cohesion between them. It is also referred to as bone sialoprotein-2 or integrin-binding sialoprotein. OCN is a member of a large family of hepatic and skeletal vitamin-K-dependent proteins which undergo post-translational modification and γ-carboxylation at key glutamic acid residues (Gla), and have mineral-binding capacities. In addition, a mature OB also secretes high levels of osteopontin, osteonectin, bone sialoprotein, and type I collagen. Bone sialoprotein (BSP) was performed to examine osteogenic capacity. Integrin-binding sialoprotein, also known as Bone sialoprotein and BSP, is a major structural protein of the bone matrix. Bone sialoprotein (BSP) is largely specific for mineralized tissues and is highly expressed during the initial formation of bone and cementum [95]. Bone Sialoprotein. On immunostaining for BSP, positive areas were observed over the entire side of the phalanx to which the periosteum was attached (periosteal side). It binds to calcium and hydroxyapatite, cells, and collagens. The gene of about 15 kb includes seven exons and the promoter contains motifs that determine developmental regulation and tissue-specific expression [239]. After gaining informed consent, we obtained human pulp cells from three … 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 ]. NX_P21815 - IBSP - Bone sialoprotein 2 - Function. "The primary structure of a cell-binding bone sialoprotein".J. It is very clear that it plays a role in matrix mineralization as supported by the timing of its appearance in relationship to the appearance of mineral and its Ca2+-binding properties. 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 … It enables bone sialoprotein to bind to cells via an integrin receptor of the vitronectin type (αvβ3). The human variant of BSP is called bone sialoprotein 2 also known as cell-binding sialoprotein or integrin-binding sialoprotein...Oldberg A, Franzén A, Heinegård D (December 1988). It binds to calcium and hydroxyapatite, cells, and collagens. BSP has a very high affinity for calcium. Outside of the skeleton, BSP is found in trophoblasts in placental membranes, which in late stages of gestation fuse and form mineralized foci. It is unknown whether DMP-1 plays a role in the differentiation of osteoblasts to osteocytes. An RGD sequence is located at the C terminus, in contrast to the central location in osteopontin. Osteopontin is a SIBLING (glycoprotein) that was first identified in 1986 in osteoblasts. MEPE is another protein of the SIBLING family that regulates bone mineralization locally. Binds tightly to hydroxyapatite. OCN is a member of a large family of hepatic and skeletal vitamin-K-dependent proteins which undergo post-translational modification and γ-carboxylation at key glutamic acid residues (Gla), and have mineral-binding capacities. However, the flanking sequences most likely influence the conformation of the region. Osteocalcin (OCN) was one of the first matrix proteins whose expression was shown to be up-regulated by vitamin D [111]. Recently, it has been suggested that BSP may play a role in angiogenesis associated with bone formation, tumor growth, and metastasis (Bellahcene, 2000). Osteocalcin (OCN) was one of the first matrix proteins whose expression was shown to be up-regulated by vitamin D [111]. 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). However, it is not known how sulfation influences BSP activity, as in vitro, unsulfated BSP appears to be equivalent in its activity. Read "Bone Sialoprotein Enhances Migration of Bone Marrow Stromal Cells Through Matrices by Bridging MMP‐2 to α v β 3 ‐Integrin, Journal of Bone and Mineral Research" on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at … OCN can inhibit the formation of hydroxyapatite in vitro [112], a function that requires the presence of the Gla residues [113]. 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. Expression of bone sialoprotein mRNA during bone formation and resorption induced by colchicine in rat tibial bone marrow cavity. 5). However, the flanking sequences most likely influence the conformation of the region. On the side to which no periosteum was attached (nonperiosteal side), no area positive for BSP was noted. OCN can inhibit the formation of hydroxyapatite in vitro [112], a function that requires the presence of the Gla residues [113]. Bone sialoprotein (BSP) is a highly glycosylated and sulfated phosphoprotein that is expressed largely in mineralizing tissues but is also associated with cancer metastasis. This characteristic is likely important in the role of bone sialoprotein in matrix mineralization. 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. BSP has a very high affinity for calcium. The IBSP mRNA encodes a full-length protein of 317 amino acid residues and a signal peptide of 16 amino acid residues. It is found predominantly in odontoblasts and osteocytes, where it is highly expressed during the mineralization process. BSP may be multifunctional in osteoblastic metabolism. MARKUS J. SEIBEL, ... CAREN M. GUNDBERG, in The Aging Skeleton, 1999. These results suggest that the expression of BSP is markedly promoted by the combination of the osteoinductive biodegradable 3D copolymer with periosteum. It inhibits mineral formation and crystal growth, and is found locally in regions of lower mineralization, such as the cement line in bone and the periodontal ligament surrounding the teeth. 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. It constitutes approximately 12% of the non-collagenous protein of human bone. In bone, OPN mediates autocrine and paracrine functions in the regulation of tissue formation. 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. OCN also is important for osteoclast recruitment [25]. 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]. (Below) Periosteal and nonperiosteal parts (BSP staining,×200). Bone sialoprotein exhibits a more limited pattern of expression than osteopontin. Gerald J. Atkins, ... Howard A. Morris, in Vitamin D (Third Edition), 2011. Bone sialoprotein (BSP) is largely specific for mineralized tissues and is highly expressed during the initial formation of bone and cementum [95]. 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. Initial osteoblastic expression of OCN occurs after the onset of extracellular matrix mineralization and increases with progressive mineralization and maturation of the osteoblast to a terminally differentiated state [82]. Serge Cremers, ... Markus J Seibel, in Principles of Bone Biology (Third Edition), 2008. It binds to calcium and hydroxyapatite, cells, and collagens. Bone sialoprotein, purified from bovine bone, has a molecular weight of 59 kDa due to its high content of carbohydrate. 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 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. 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 stretches of up to 10 glutamic acid residues provide high-affinity binding to Ca2+. Bovine bone sialoprotein contains 5.8 phosphates that are added by casein kinase II to serine residues [243]. 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. DEV2011 Lecture Notes - Lecture 20: Collagen, Bone Sialoprotein, Reticular Connective Tissue BSP is stable at −80° C (Li, 1998), but little is known about the kinetics and metabolism of BSP in serum. The other major sialoprotein is bone sialoprotein, composed of 50% carbohydrate (12% is sialic acid) and stretches of polyglutamic acid (as opposed to polyaspartic acid in osteopontin). 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]. BSP (MW 34kDa) is a major non-collagenous protein in mineralizing connective tissues, such as dentin, cementum, bone, and calcified cartilage tissues. (Above) Cross-section (BSP staining). The stretches of up to 10 glutamic acid residues provide high-affinity binding to Ca2+. Marc D. McKee, William G. Cole, in Pediatric Bone (Second Edition), 2012. It has a high affinity for hydroxyapatite and the N-telopeptide region of type I collagen, and functions to locally regulate the mineralization process. Fibrocartilaginous entheses contain fibrocartilage in their transitional zone, part of which is mineralized. 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. 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. Bone sialoprotein, encoded by the IBSP gene, is a phosphorylated and glycosylated protein secreted by bone matrix and cancer cells. 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. Bone sialoprotein is the second major sialoprotein of bone [2 ]. Outside of the skeleton, BSP is found in trophoblasts in placental membranes, which in late stages of gestation fuse and form mineralized foci. The IBSP mRNA encodes a full-length protein of 317 amino acid residues and a signal peptide of 16 amino acid residues. Hidefumi Maeda, ... Akifumi Akamine, in International Review of Cell and Molecular Biology, 2013. Many of these effects may be mediated by the effects of vitamin D on phosphate transport, reviewed elsewhere [116]. Cortical bone repair and mineralization are also impaired by the absence of BSP [247,249]. The expression of BSP is suppressed by 1,25(OH)2D3 treatment in rat calvaria and ROS 17/2.8 cells [96]. 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. Bone sialoprotein (BSP) is an acidic, phosphorylated glycoprotein that is synthesized by osteoblasts and osteoclastic-like cells in culture. A VDRE that is integrated with an inverted TATA box in the rat BSP promoter mediates the suppression of BSP transcription [97–99]. Binds tightly to hydroxyapatite. BSP is a significant component of the bone extracellular matrix and has been suggested to constitute approximately 8% of … Outside of the skeleton, bone sialoprotein is expressed in odontoblasts and in trophoblast of the placenta. An imbalance between bone resorption and formation can re… We investigated the effects of adiponectin and leptin on the kinetics of human pulp cells using ELISA and western blot. From: International Review of Cell and Molecular Biology, 2013, Serge Cremers, ... Markus J Seibel, in Principles of Bone Biology (Third Edition), 2008. This characteristic is likely important in the role of integrin-binding sialoprotein in matrix mineralization. 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). Pamela Gehron Robey, in Principles of Bone Biology (Third Edition), 2008. 5. Sulfated BSP has been isolated in a number of animal species, but the levels appear to be variable. In general, its expression is tightly associated to mineralization phenomena (although there are exceptions). Immunohistochemistry to examine osteogenic capability of the copolymer. Bone sialoprotein (BSP) is one of the most abundant noncollagenous, glycosylated phosphoproteins in bone, having a molecular mass of about 80 kDa, of which approximately 34 kDa is core protein. This record represents the promoter and related 5' regulatory region of the integrin binding sialoprotein gene, also known as BSP. 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, approximately half of the serine residues in the protein carry phosphate groups. BSP may be multifunctional in osteoblastic metabolism. BSP is a highly glycosylated and sulphated phosphoprotein that is found almost exclusively in mineralized connective tissues. Gundberg, in Basic and Applied bone Biology ( Third Edition ), is second... 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