Cloning and sequence analysis of bovine bone sialoprotein cDNA: Conservation of acidic domains, tyrosine sulfation consensus repeats, and RGD cell attachment domain

2009 ◽  
Vol 9 (3) ◽  
pp. 417-421 ◽  
Author(s):  
C. Chenu ◽  
K. Ibaraki ◽  
P. Gehron Robey ◽  
P.D. Delmas ◽  
M.F. Young
Keyword(s):  
Sequence Analysis ◽  
Cell Attachment ◽  
Bone Sialoprotein ◽  
Bovine Bone ◽  
Tyrosine Sulfation

scholarly journals Phosphorylation of Purified Bovine Bone Sialoprotein and Osteopontin by Protein Kinases

1996 ◽  
Vol 271 (28) ◽  
pp. 16897-16905 ◽  
Author(s):  
Erdjan Salih ◽  
Hai-Yan Zhou ◽  
Melvin J. Glimcher
Keyword(s):  
Protein Kinases ◽  
Bone Sialoprotein ◽  
Bovine Bone

scholarly journals Fetal bovine bone cells synthesize bone-specific matrix proteins.

1984 ◽  
Vol 99 (2) ◽  
pp. 607-614 ◽  
Author(s):  
S W Whitson ◽  
W Harrison ◽  
M K Dunlap ◽  
D E Bowers ◽  
L W Fisher ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Bone Cells ◽  
Bone Sialoprotein ◽  
Cell System ◽  
Matrix Proteins ◽  
Type I ◽  
Bovine Bone ◽  
Isolated Cells ◽  
Noncollagenous Proteins

We isolated cells from both calvaria and the outer cortices of long bones from 3- to 5-mo bovine fetuses. The cells were identified as functional osteoblasts by indirect immunofluorescence using antibodies against three bone-specific, noncollagenous matrix proteins (osteonectin, the bone proteoglycan, and the bone sialoprotein) and against type 1 collagen. In separate experiments, confluent cultures of the cells were radiolabeled and shown to synthesize and secrete osteonectin, the bone proteoglycan and the bone sialoprotein by immunoprecipitation and fluorography of SDS polyacrylamide gels. Analysis of the radiolabeled collagens synthesized by the cultures showed that they produced predominantly (approximately 94%) type I collagen, with small amounts of types III and V collagens. In agreement with previous investigators who have employed the rodent bone cell system, we confirmed in bovine bone cells that (a) there was a typical cyclic AMP response to parathyroid hormone, (b) freshly isolated cells possessed high levels of alkaline phosphatase, which diminished during culture but returned to normal levels in mineralizing cultures, and (c) cells grown in the presence of ascorbic acid and beta-glycerophosphate rapidly produced and mineralized an extracellular matrix containing largely type I collagen. These results show that antibodies directed against bone-specific, noncollagenous proteins can be used to clearly identify bone cells in vitro.

Proliferation and Differentiation of MC3T3-E1 Cells on Calcium Phosphate/Chitosan Coatings

2008 ◽  
Vol 87 (7) ◽  
pp. 650-654 ◽  
Author(s):  
J. Wang ◽  
J. de Boer ◽  
K. de Groot
Keyword(s):  
Calcium Phosphate ◽  
Stromal Cell ◽  
Bone Marrow Stromal Cell ◽  
Cell Attachment ◽  
Bone Sialoprotein ◽  
Differentiation Potential ◽  
Collagen Expression ◽  
Significant Difference ◽  
Proliferation And Differentiation ◽  
Proliferative Ability

The incorporation of chitosan into electro-deposited calcium phosphate (CaP) coatings increases bone marrow stromal cell attachment. We hypothesized that such electrodeposited CaP/chitosan coatings can also enhance the proliferative ability and differentiation potential of osteoblasts. To verify this hypothesis, we cultured osteoblast-like MC3T3-E1 cells on these CaP coatings. It was found that MC3T3-E1 cells cultured on the electrodeposited CaP/chitosan coatings had cell proliferation rates higher than those on the electrodeposited CaP coatings. At the same time, both alkaline phosphatase activity and collagen expression were increased, and both bone sialoprotein and osteocalcin genes were up-regulated when MC3T3-E1 cells were cultured on the electrodeposited CaP/chitosan coatings. Additionally, within the range of selected chitosan concentrations in solution, no significant difference was found between the CaP/chitosan coatings. Our results suggest that the electrodeposited CaP/chitosan coatings are favorable to the proliferation and differentiation of MC3T3-E1 cells, which may endow them with great potential for future applications.

scholarly journals Chlorate-induced inhibition of tyrosine sulfation on bone sialoprotein synthesized by a rat osteoblast-like cell line (UMR 106-01 BSP).

1994 ◽  
Vol 269 (7) ◽  
pp. 4845-4852
Author(s):  
K.P. Mintz ◽  
L.W. Fisher ◽  
W.J. Grzesik ◽  
V.C. Hascall ◽  
R.J. Midura
Keyword(s):  
Cell Line ◽  
Bone Sialoprotein ◽  
Tyrosine Sulfation ◽  
Rat Osteoblast ◽  
Umr 106

Cell attachment activity of cementum: bone sialoprotein _ identified in cementum

1991 ◽  
Vol 26 (1) ◽  
pp. 10-16 ◽  
Author(s):  
M. J. Somerman ◽  
J. J. Sauk ◽  
R. A. Foster ◽  
K. Norris ◽  
K. Dickerson ◽  
...  
Keyword(s):  
Cell Attachment ◽  
Bone Sialoprotein

scholarly journals Bone Sialoprotein

1999 ◽  
Vol 10 (1) ◽  
pp. 79-98 ◽  
Author(s):  
B. Ganss ◽  
R.H. Kim ◽  
J. Sodek
Keyword(s):  
Bone Formation ◽  
De Novo ◽  
Cell Attachment ◽  
Chemical Properties ◽  
Bone Sialoprotein ◽  
Crystal Formation ◽  
Polyglutamic Acid ◽  
Isolation And Characterization ◽  
Bona Fide ◽  
Mediate Cell

The search for a protein nucleator of hydroxyapatite crystal formation has been a focus for the isolation and characterization of the major non-collagenous proteins in bone. Of the proteins characterized to date, bone sialoprotein (BSP) has emerged as the only bona fide candidate for nucleation. BSP is a highly glycosylated and sulphated phosphoprotein that is found almost exclusively in mineralized connective tissues. Characteristically, polyglutamic acid and arginine-glycine-aspartate (RGD) motifs with the ability to bind hydroxyapatite and cell-surface integrins, respectively, have been conserved in the protein sequence. Expression of the BSP gene, which is induced in newly formed osteoblasts, is up-regulated by hormones and cytokines that promote bone formation and down-regulated by factors that suppress bone formation. Thus, BSP has the biophysical and chemical properties of a nucleator, and its temporo-spatial expression coincides with de novo mineralization in bone and cementum. Moreover, BSP has been associated with mineral crystal formation in several pathologies, including breast carcinomas. However, the ability of BSP to mediate cell attachment and to signal through the RGD motif points to alternate functions for BSP which need further investigation. In combination, the hydroxyapatite-binding polyglutamic acid sequences and the RGD provide bi-functional entities through which BSP may mediate the targeting and attachment of normal and metastasizing cells to the bone surface.

scholarly journals Comparison of Bovine Bone Sialoprotein and Serum Orosomucoid

Nature ◽  
1964 ◽  
Vol 201 (4920) ◽  
pp. 709-709 ◽  
Author(s):  
G. M. HERRING
Keyword(s):  
Bone Sialoprotein ◽  
Bovine Bone

Anorganic Bovine Bone Supports Osteoblastic Cell Attachment and Proliferation

1999 ◽  
Vol 70 (4) ◽  
pp. 364-369 ◽  
Author(s):  
Eugena B. Stephan ◽  
Di Jiang ◽  
Samuel Lynch ◽  
Peter Bush ◽  
Rosemary Dziak
Keyword(s):  
Cell Attachment ◽  
Osteoblastic Cell ◽  
Bovine Bone

scholarly journals Evidence of ectokinase-mediated phosphorylation of osteopontin and bone sialoprotein by osteoblasts during bone formation in vitro

1997 ◽  
Vol 323 (3) ◽  
pp. 637-643 ◽  
Author(s):  
XinLi ZHU ◽  
Chun LUO ◽  
Jack M. FERRIER ◽  
Jaro SODEK
Keyword(s):  
Cell Surface ◽  
Bone Cells ◽  
Cell Attachment ◽  
Biological Properties ◽  
Bone Cell ◽  
Bone Sialoprotein ◽  
Surface Proteins ◽  
Pulse Labelling ◽  
Mediate Cell

Osteopontin (OPN) and bone sialoprotein (BSP) are phosphorylated glycoproteins that, together with osteonectin/secreted protein, acidic, rich in cysteine (SPARC) and osteocalcin, comprise the major non-collagen proteins of bone. Although phosphorylation of OPN and BSP, which is known to influence the biological properties of these proteins, has been shown to occur intracellularly, recent studies have demonstrated ectokinase activity in bone cell populations [Mikuni-Takagaki, Kakai, Satoyoshi, Kawano, Suzuki, Kawase and Saito (1995) J. Bone Miner. Res. 10, 231–241]. To determine whether OPN and BSP are phosphorylated by ectokinase activity we have used [γ-32P]ATP and [γ-32P]GTP as cell-impenetrable phosphate donors to analyse for ectokinase activity in osteoblastic UMR106.06 cells and fetal rat calvarial cells (FRCCs). By pulse-labelling confluent cells with radiolabelled nucleotides, the phosphorylation of endogenous and exogenously added OPN and BSP was demonstrated together with the labelling of a number of cell surface proteins. These phosphorylation reactions were inhibited by a cell-impermeable ectokinase inhibitor, K252b, and cell surface phosphorylation was also inhibited by exogenously added OPN and BSP substrates, indicating competition for the ectokinase enzyme. However, phosphorylation of OPN and BSP, both of which can mediate cell attachment through Arg-Gly-Asp (RGD) motifs, was not inhibited by an RGD peptide, suggesting that binding of OPN and BSP to cell surface integrins is not required. In similar experiments, ectokinase-mediated phosphorylation of OPN and BSP was demonstrated during mineralized tissue formation by FRCCs in vitro. These studies demonstrate that OPN and BSP secreted by bone cells are phosphorylated by a casein kinase II-like ectokinase present on the surface of osteoblastic cells.

scholarly journals The periodate oxidation of bovine bone sialoprotein, and some observations on its structure

1969 ◽  
Vol 111 (5) ◽  
pp. 621-627 ◽  
Author(s):  
A. T. De B. Andrews ◽  
G. M. Herring ◽  
P. W. Kent
Keyword(s):  
Sialic Acid ◽  
Periodate Oxidation ◽  
Peptide Bond ◽  
Bone Sialoprotein ◽  
Bovine Bone ◽  
Acetylneuraminic Acid ◽  
Terminal Sialic Acid ◽  
Smith Degradation ◽  
Fucose Residue ◽  
Oligosaccharide Structures

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.

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