Bone Sialoprotein (BSP) is a Crucial Factor for the Expression of Osteoblastic Phenotypes of Bone Marrow Cells Cultured on Type I Collagen Matrix

Mizuno, Morimichi; Imai, Toshiro; Fujisawa, Ryuichi; Tani, Hiroshi; Kuboki, Yoshinori

doi:10.1007/s002230010078

Cited by 77 publications

(58 citation statements)

References 44 publications

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“…In particular, cells lining the bone surface showed stronger expressions. The interaction between the cells on the bone surface and bone matrix molecules, such as type I collagen (Jikko et al, 1999;Takeuchi et al, 1996Takeuchi et al, , 1997, fibronectin (Moursi et al, 1997), osteopontin (Liu et al, 1997) or bone sialoprotein (Mizuno et al, 2000) may be involved in osteoblastic differentiation, since it has been suggested that the bone matrix molecules are recognized by the integrin receptors of osteoprogenitors and promote osteoblastic differentiation via activation of the focal adhesion kinase and its downstream signals (Takeuchi et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

Osteoblastic differentiation of periosteum‐derived cells is promoted by the physical contact with the bone matrix in vivo

et al. 2001

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The periosteum contains osteoprogenitors that differentiate to osteoblasts in bone growth or repair. Our previous studies suggested the hypothesis that the physical contact of the periosteum with the bone matrix is requisite for the differentiation of osteoblasts. To test the hypothesis, the present study was designed to investigate how the contact between the periosteum and the bone matrix influences the osteoblastic differentiation of periosteal cells with establishing a new experimental model in vivo. Differentiation of osteoblasts was assessed by gene expression of type I collagen, osteocalcin and bone sialoprotein using in situ hybridization. A barrier was designed to prevent periosteal cells from contacting the bone matrix using the membrane filter. The membrane filter was inserted surgically between the surface of rat parietal bone and the periosteum after being punched out with pin holes. Periosteal cells were allowed to contact with the bone surface only through the pin holes. The pin hole was filled with cells derived from the periosteum 1 week after inserting the filter. Differentiation of osteoblasts in week 2 and noticeable bone formation in week 3 were identified on the bone surface only under the pin hole but not under the filter. The present study demonstrated that the physical contact with the bone matrix promotes osteoblastic differentiation of periosteumderived cells in vivo. Anat Rec 264:72-81, 2001.

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Section: Discussionmentioning

confidence: 99%

Osteoblastic differentiation of periosteum‐derived cells is promoted by the physical contact with the bone matrix in vivo

et al. 2001

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“…Moreover, it has been shown that as little as 9 nM BSP is required to nucleate HA, and recently the overexpression of BSP in osteoblasts has been shown to enhance mineralisation (Hunter et al 1996, Gordon et al 2007. Similarly, osteoblast cultures grown in the presence of an anti-BSP antibody exhibit reduced mineralisation (Cooper et al 1998, Mizuno et al 2000. This nucleation potency is increased on BSP binding to collagen, suggesting a cooperative relationship (Baht et al 2008).…”

Section: Bone Sialoproteinmentioning

confidence: 99%

The importance of the SIBLING family of proteins on skeletal mineralisation and bone remodelling

Staines¹,

MacRae²,

Farquharson³

2012

Journal of Endocrinology

187

109

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The small integrin-binding ligand N-linked glycoprotein (SIBLING) family consists of osteopontin, bone sialoprotein, dentin matrix protein 1, dentin sialophosphoprotein and matrix extracellular phosphoglycoprotein. These proteins share many structural characteristics and are primarily located in bone and dentin. Accumulating evidence has implicated the SIBLING proteins in matrix mineralisation. Therefore, in this review, we discuss the individual role that each of the SIBLING proteins has in this highly orchestrated process. In particular, we emphasise how the nature and extent of their proteolytic processing and post-translational modification affect their functional role. Finally, we describe the likely roles of the SIBLING proteins in clinical disorders of hypophosphataemia and their potential therapeutic use.

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“…The coupling of the state of phosphorylation of BSP with that of OPN in regulating the rate of calcium phosphate deposition pre- sents a unique biological interrelationship between these two proteins. Other studies have indicated that BSP promotes mineral deposition in cell cultures (9,43) and differentiation of bone marrow cells to osteoblasts (44). Additional in vivo work using implants of native bone BSP-collagen composites in bone repair (19) and reparative dentinogenesis (7, 8, 20 -22) elaborated on the multifunctional capacity of this protein.…”

Section: (Les(p)deengvfk) Residues 42-62 (Favqsssdss(p)eengngds(p)s(mentioning

confidence: 99%

Complete Topographical Distribution of Both the in Vivo and in Vitro Phosphorylation Sites of Bone Sialoprotein and Their Biological Implications

Salih

Flückiger

2004

Journal of Biological Chemistry

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Bone sialoprotein (BSP) is a multifunctional, highly phosphorylated, and glycosylated protein with key roles in biomineralization and tissue remodeling. This work identifies the complete topographical distribution and precise location of both the in vitro and in vivo phosphorylation sites of bovine BSP by a combination of stateof-the-art techniques and approaches. In vitro phosphorylation of native and deglycosylated BSPs by casein kinase II identified seven phosphorylation sites by solidphase N-terminal peptide sequencing that were within peptides 12-22 (LEDS(P)EENGVFK), 42-62 (FAVQSSSD- SS(P)EENGNGDS(P)S(P)EE), 80 -91 (EDS(P)DENEDEE-S(P)E), and 135-145 (EDES(P)DEEEEEE). The in vivo phosphorylation regions and sites were identified by use of a novel thiol reagent, 1-S-mono[14 C]carboxymethyldithiothreitol. This approach identified all of the phosphopeptides defined by in vitro phosphorylation, but two additional phosphopeptides were defined at residues, 250 -264 (DNGYEIYES(P)ENGDPR), and 282-289 (GYDS(P)YDGQ). Furthermore, use of native BSP and matrix-assisted laser desorption ionization time-offlight mass spectrometry identified several of the above peptides, including an additional phosphopeptide at residues 125-130 (AGAT(P)GK) that was not defined in either of the in vitro and in vivo studies described above. Overall, 7 in vitro and 11 in vivo phosphorylation sites were identified unequivocally, with natural variation in the quantitative extent of phosphorylation at each in vivo phosphorylation site.Evidence supporting many facets of the observed biological functions of bone sialoprotein (BSP) 1 and osteopontin (OPN) has been accumulating, with a wide range of implications in both mineralizing and non-mineralizing tissues. BSP and OPN are the major non-collagenous extracellular matrix (ECM) phosphoproteins of calcified tissues such as bone and cartilage. Their intimate relationship with biomineralization suggests that they play key roles during the development and maintenance of these tissues (1-8). In vitro studies using BSP and OPN indicate that, whereas BSP induces calcium phosphate apatite formation (4 -6, 9), OPN lacks this property or is inhibitory (3, 4, 10). The biological functions of BSP and OPN are not limited to mineral deposition, but impact cell behavior such as cell motility, cell adhesion, and bone resorption (10 -16). Despite extensive studies, however, the precise roles of these phosphoproteins remain to be clearly defined. Although some in vitro studies indicate that BSP promotes bone resorption and hence participates in bone degradation (17), other studies such as those using glucocorticoids, which increase expression of this protein, suggest its involvement in the anabolic phase of bone remodeling (18). In this laboratory, in vivo implants of BSP-collagen composites in the calvarial critical defect bone repair model (19) and during reparative dentinogenesis (7, 8, 20 -22) highlighted the impact of BSP during biomineralization and new bone/dentin formation.As interest continues and evid...

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Bone Sialoprotein (BSP) is a Crucial Factor for the Expression of Osteoblastic Phenotypes of Bone Marrow Cells Cultured on Type I Collagen Matrix

Cited by 77 publications

References 44 publications

Osteoblastic differentiation of periosteum‐derived cells is promoted by the physical contact with the bone matrix in vivo

Osteoblastic differentiation of periosteum‐derived cells is promoted by the physical contact with the bone matrix in vivo

The importance of the SIBLING family of proteins on skeletal mineralisation and bone remodelling

Complete Topographical Distribution of Both the in Vivo and in Vitro Phosphorylation Sites of Bone Sialoprotein and Their Biological Implications

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