Bone sialoprotein (BSP) is a sulfated and phosphorylated glycoprotein found almost exclusively in mineralized connective tissues. Tb4 induced BSP expression in MDPC23 cells via ERK and Smad3 signaling pathways, suggesting its role as a signaling molecule in odontoblasts for … In: Biology and chemistry of mineralized tissues. OPN knockout (−/−) mice do not lose bone in a model of hindlimb disuse (tail suspension), showing the importance of OPN in bone remodeling.We report that BSP −/− mice are viable and breed normally, but their weight and size are lower than wild-type (WT) mice. Osf2, a member of the Cbf/runt family of transcription factors, is required for the development of osteoblasts in vivo and has been reported to stimulate the transcription of BSP when overexpressed in mesenchymal cell lines. 3 PP is an extremely acidic protein and well established as a mineral nucleator for dentin mineralization. Bone sialoprotein plays a functional role in bone formation and osteoclastogenesis. Appears to form an integral part of the mineralized matrix. This study receivedfinding from: IRP-NIDCR, NlH, S160 Implication of Two Matrix Proteins in Bone Healing: Osteopontin (OPN) &&I*’, and Bone Sialoprotein (BSP). BSP is characterized by the presence of several polyglutamic acid segments and an RGD motif that mediates cell attachment through a vitronectin-like receptor. BSP, a bone … Bone sialoprotein (BSP) is a phosphorylated and sulfated glycoprotein that is a major noncollagenous protein of bone and other mineralizing connective tissues. OPN, a multifunctional protein, is considered crucial for bone remodeling, biomineralization, and periodontal remodeling during mechanical tension and stress (orthodontic tooth movement). Bone Sialoprotein - Function. Although BSP can mediate cell attachment through an RGD sequence and binds selectively to hydroxyapatite, its precise function in mineralized tissues is unknown. Luc Malaval, Nd ey e Mari eme Wade-Gu eye, Maya Boudi a, Jia Fei, Ralph Zirngibl, Frieda Chen, Norbert Laroche, Jean-Paul Roux, Brigitte Burt-Pichat, Fran˘cois Duboeuf, et al. Tartrate-resistant acid phosphatase (TRAP or TRAPase), also called acid phosphatase 5, tartrate resistant (ACP5), is a glycosylated monomeric metalloprotein enzyme expressed in mammals. bone sialoprotein 2, bone sialoprotein II, cell-binding sialoprotein. Bone Sialoprotein (BSP-II) Based on chromatographic characteristics and compositional analysis, it is apparently a fragment of the sialoprotein (BSP-II) molecule that was initially described by Herring and coworkers68, 141 and later isolated in an intact form93,105 and found to have an apparent molecular weight of ~75,000 by SDS-PAGE. BSP is a significant component of the bone extracellular matrix and has been suggested to constitute approximately 8% of all non-collagenous proteins found in bone … Bone sialoprotein knockout (Bsp-/-) mice feature increased circulating pyrophosphate (PP i)Bsp knock-out cementoblasts exhibit significantly decreased mineralization capacity and increased PP i in culture media. Function. Since distribution of Binds tightly to hydroxyapatite. Disclosures: Y Bi, None. To test this hypothesis, the effects of BSP and osteopontin on hydroxyapatite crystal formation were determined by using a steady-state agarose gel system. Bone sialoprotein (BSP) is a component of mineralized tissues such as bone, dentin, cementum and calcified cartilage. Amsterdam: Elsevier Science, pp. IBSP (Integrin Binding Sialoprotein) is a Protein Coding gene. One possibility is that BSP acts as a nucleus for the formation of the first apatite crystals. Addition of recombinant BSP altered Spp1, Ank, and Enpp1 mRNA expression in cementoblasts, in vitro. The primary structure of a bone-specific sialoprotein was deduced from cloned cDNA. (A) To stimulate forward or reverse signaling, ephrin B1-Fc, ephrin B2-Fc, or IgG-Fc fragments were clustered with anti-Fc antibody at 2 µg/mL for 1 hr, and then primary mouse osteoblasts were cultured with 50 µg/mL ascorbic acid and 10 mM β-glycerophosphate for 17 days on the clustered proteins. This review describes normal bone anatomy and physiology as an introduction to the subsequent articles in this section that discuss clinical applications of iliac crest bone biopsy. Positive staining (arrows) is present in the nidus of cartilage for bone sialoprotein. Bone sialoprotein (BSP) is an extracellular matrix protein that is intimately associated with the process of biomineralization. Figure 4. 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. Bellahcene A, Menard S, Bufalino R, Moreau L & Castronovo V (1996). E, Negative control histological section incubated with IgG indicating the lack of specific staining. glycoprotein of bone and is also expressed in a wide variety of other cells and tissues, including immune cells, skin, and blood vessels. Probably important to cell-matrix interaction. View mouse Ibsp Chr5:104299287-104311472 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression Two distinctly different proteins rich in sialic acid have been identi- fied (5-7): bone sialoprotein I, now known as osteo- pontin, and bone sialoprotein 11, presently referred to as bone sialoprotein (BSP) (8). Expression of bone sialoprotein in primary human breast cancer is associated with poor survival. Bone sialoprotein expression in primary human breast cancer is associated with bone metastases development. Bone sialoprotein (BSP) and osteopontin (OPN) are both highly expressed in bone, but their functional specificities are unknown. In this review, most of the known and postulated mechanisms of osteopontin (OPN) and its role in bone remodeling and orthodontic tooth movement are discussed based on available literature. Bone Sialoprotein (BSP) is a member of the "Small Integrin-Binding Ligand N-linked Glycoproteins" (SIBLING) extracellular matrix protein family of mineralized tissues. Google Scholar Study analyzed circulating bone sialoprotein (BSP) in a large cohort of patients with liver cirrhosis. It has a molecular weight of approximately 35kDa, a basic isoelectric point (7.6–9.5), and optimal activity in acidic conditions. Bone sialoprotein (BSP) and osteopontin, the major phosphorylated proteins of mammalian bone, have been proposed to function in the initiation of mineralization. Promotes Arg-Gly-Asp-dependent cell attachment. ABSTRACT Background: Bone sialoprotein (BSP) and osteopontin (OPN), two major noncollagenous proteins (NCPs) in collagen-based mineralized tissues, have been implicated in mineral deposition and cell-and matrix-matrix interactions during root development. 1,2 PP was identified in 1967 by Veis and Perry. L. Bone sialoprotein functions as a potent stimulator of hydroxyapatite nucleation. [ Links ] 15. Elucidating the functions of bone sialoprotein and OPN in bone formation. Bone sialoprotein (BSP) is a highly sulphated and glycosylated phosphoprotein that is a major constituent of bone and other mineralized connective tissues. 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.