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Bone sialoprotein

March 17, 2023

Bone sialoprotein (BSP) is a component of mineralized tissues such as bone, dentin, cementum and calcified cartilage. 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 and cementum.[5] BSP, a SIBLING protein, was originally isolated from bovine cortical bone as a 23-kDa glycopeptide with high sialic acid content.[6][7]

IBSP
Identifiers
AliasesIBSP, BNSP, BSP, BSP-II, SP-II, integrin binding sialoprotein
External IDsOMIM: 147563 MGI: 96389 HomoloGene: 3644 GeneCards: IBSP
Orthologs
SpeciesHumanMouse
Entrez

3381

15891

Ensembl

ENSG00000029559

ENSMUSG00000029306

UniProt

P21815

Q61711

RefSeq (mRNA)

NM_004967

NM_008318

RefSeq (protein)

NP_004958

NP_032344

Location (UCSC)Chr 4: 87.8 – 87.81 MbChr 5: 104.45 – 104.46 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[8]

Structure

Native BSP has an apparent molecular weight of 60-80 kDa based on SDS-PAGE, which is a considerable deviation from the predicted weight (based on cDNA sequence) of approximately 33 kDa.[9] The mammalian BSP cDNAs encode for proteins averaging 317 amino acids, which includes the 16-residue preprotein secretory signal peptide. Among the mammalian cDNAs currently characterized, there is an approximate 45% conservation of sequence identity and a further 10-23% conservative substitution. The protein is highly acidic (pKa of ~ 3.9)[10] and contains a large amount of Glu residues, constituting ~22% of the total amino acid.

Secondary structure prediction and hydrophobicity analyses suggest that the primary sequence of BSP has an open, flexible structure with the potential to form regions of α-helix and some β-sheet.[11] However, the majority of studies have demonstrated that BSP has no α-helical or β-sheet structure by 1D NMR[10][12] and circular dichroism.[13] Analysis of native protein by electron microscopy confirm that the protein has an extended structure approximately 40 nm in length.[14] This flexible conformation suggests that the protein has few structural domains, however it has been suggested that there may be several spatially segmented functional domains including a hydrophobic collagen-binding domain (rattus norvegicus residues 36-57),[15] a hydroxyapatite-nucleating region of contiguous glutamic acid residues (rattus norvegicus residues 78-85, 155-164)[13] and a classical integrin-binding motif (RGD) near the C-terminal (rattus norvegicus residues 288-291).

BSP has been demonstrated to be extensively post-translationally modified, with carbohydrates and other modifications comprising approximately 50% of the molecular weight of the native protein.[16][17] These modifications, which include N- and O-linked glycosylation, tyrosine sulfation and serine and threonine phosphorylation, make the protein highly heterogeneous.

A 3D model of human bone sialoprotein has been developed using molecular modelling techniques, as shown in the picture above. The model suggests that the protein provides a flexible template for the rapid self-assembly of calcium and phosphate ions, so nucleating the growth of hydroxyapatite crystals.[18]

Function

The amount of BSP in bone and dentin is roughly equal,[19] however the function of BSP in these mineralized tissues is not known. One possibility is that BSP acts as a nucleus for the formation of the first apatite crystals.[20] As the apatite forms along the collagen fibres within the extracellular matrix, BSP could then help direct, redirect or inhibit the crystal growth.

Additional roles of BSP are angiogenesis and protection from complement-mediated cell lysis. Regulation of the BSP gene is important to bone matrix mineralization and tumor growth in bone.[21]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000029559 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029306 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Fisher LW, McBride OW, Termine JD, Young MF (February 1990). "Human bone sialoprotein. Deduced protein sequence and chromosomal localization". J. Biol. Chem. 265 (4): 2347–51. doi:10.1016/S0021-9258(19)39982-X. PMID 2404984.
  6. ^ Williams PA, Peacocke AR (November 1965). "The physical properties of a glycoprotein from bovine cortical bone (bone sialoprotein)". Biochim. Biophys. Acta. 101 (3): 327–35. doi:10.1016/0926-6534(65)90011-4. PMID 5862222.
  7. ^ Herring GM (February 1964). "Comparison of bovine bone sialoprotein and serum orosomucoid". Nature. 201 (4920): 709. Bibcode:1964Natur.201..709H. doi:10.1038/201709a0. PMID 14139700. S2CID 4210187.
  8. ^ Kerr JM, Fisher LW, Termine JD, Wang MG, McBride OW, Young MF (August 1993). "The human bone sialoprotein gene (IBSP): genomic localization and characterization". Genomics. 17 (2): 408–15. doi:10.1006/geno.1993.1340. PMID 8406493.
  9. ^ Fisher LW, Whitson SW, Avioli LV, Termine JD (October 1983). "Matrix sialoprotein of developing bone". J. Biol. Chem. 258 (20): 12723–7. doi:10.1016/S0021-9258(17)44236-0. PMID 6355090.
  10. ^ a b Stubbs JT, Mintz KP, Eanes ED, Torchia DA, Fisher LW (August 1997). "Characterization of native and recombinant bone sialoprotein: delineation of the mineral-binding and cell adhesion domains and structural analysis of the RGD domain". J. Bone Miner. Res. 12 (8): 1210–22. doi:10.1359/jbmr.1997.12.8.1210. PMID 9258751. S2CID 26407786.
  11. ^ Shapiro HS, Chen J, Wrana JL, Zhang Q, Blum M, Sodek J (November 1993). "Characterization of porcine bone sialoprotein: primary structure and cellular expression". Matrix. 13 (6): 431–40. doi:10.1016/s0934-8832(11)80109-5. PMID 8309422.
  12. ^ Fisher LW, Torchia DA, Fohr B, Young MF, Fedarko NS (January 2001). "Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin". Biochem. Biophys. Res. Commun. 280 (2): 460–5. doi:10.1006/bbrc.2000.4146. PMID 11162539.
  13. ^ a b Tye CE, Rattray KR, Warner KJ, Gordon JA, Sodek J, Hunter GK, Goldberg HA (March 2003). "Delineation of the hydroxyapatite-nucleating domains of bone sialoprotein". J. Biol. Chem. 278 (10): 7949–55. doi:10.1074/jbc.M211915200. PMID 12493752.
  14. ^ Oldberg A, Franzén A, Heinegård D (December 1988). "The primary structure of a cell-binding bone sialoprotein". J. Biol. Chem. 263 (36): 19430–2. doi:10.1016/S0021-9258(19)77651-0. PMID 3198635.
  15. ^ Tye CE, Hunter GK, Goldberg HA (April 2005). "Identification of the type I collagen-binding domain of bone sialoprotein and characterization of the mechanism of interaction". J. Biol. Chem. 280 (14): 13487–92. doi:10.1074/jbc.M408923200. PMID 15703183.
  16. ^ Kinne RW, Fisher LW (July 1987). "Keratan sulfate proteoglycan in rabbit compact bone is bone sialoprotein II". J. Biol. Chem. 262 (21): 10206–11. doi:10.1016/S0021-9258(18)61099-3. PMID 2956253.
  17. ^ Ganss B, Kim RH, Sodek J (1999). "Bone sialoprotein". Crit. Rev. Oral Biol. Med. 10 (1): 79–98. doi:10.1177/10454411990100010401. PMID 10759428.
  18. ^ Vincent K, Durrant MC (2013). "A structural and functional model for human bone sialoprotein" (PDF). J. Mol. Graph. Model. 39: 108–117. doi:10.1016/j.jmgm.2012.10.007. PMID 23261880.
  19. ^ Qin C, Brunn JC, Jones J, George A, Ramachandran A, Gorski JP, Butler WT (April 2001). "A comparative study of sialic acid-rich proteins in rat bone and dentin". Eur. J. Oral Sci. 109 (2): 133–41. doi:10.1034/j.1600-0722.2001.00001.x. PMID 11347657.
  20. ^ Hunter GK, Goldberg HA (August 1994). "Modulation of crystal formation by bone phosphoproteins: role of glutamic acid-rich sequences in the nucleation of hydroxyapatite by bone sialoprotein". Biochem. J. 302 ( Pt 1) (Pt 1): 175–9. doi:10.1042/bj3020175. PMC 1137206. PMID 7915111.
  21. ^ Ogata Y (April 2008). "Bone sialoprotein and its transcriptional regulatory mechanism". Journal of Periodontal Research. 43 (2): 127–35. doi:10.1111/j.1600-0765.2007.01014.x. PMID 18302613.

External links

Further reading

  • Karadag A, Fisher LW (2006). "Bone sialoprotein enhances migration of bone marrow stromal cells through matrices by bridging MMP-2 to alpha(v)beta3-integrin". J. Bone Miner. Res. 21 (10): 1627–36. doi:10.1359/jbmr.060710. PMID 16995818. S2CID 84886034.
  • Barnes GL, Javed A, Waller SM, et al. (2003). "Osteoblast-related transcription factors Runx2 (Cbfa1/AML3) and MSX2 mediate the expression of bone sialoprotein in human metastatic breast cancer cells". Cancer Res. 63 (10): 2631–7. PMID 12750290.
  • Carlinfante G, Vassiliou D, Svensson O, et al. (2003). "Differential expression of osteopontin and bone sialoprotein in bone metastasis of breast and prostate carcinoma". Clin. Exp. Metastasis. 20 (5): 437–44. doi:10.1023/A:1025419708343. PMID 14524533. S2CID 341938.
  • Hwang Q, Cheifetz S, Overall CM, et al. (2009). "Bone sialoprotein does not interact with pro-gelatinase A (MMP-2) or mediate MMP-2 activation". BMC Cancer. 9: 121. doi:10.1186/1471-2407-9-121. PMC 2679042. PMID 19386107.
  • Styrkarsdottir U, Halldorsson BV, Gretarsdottir S, et al. (2009). "New sequence variants associated with bone mineral density". Nat. Genet. 41 (1): 15–7. doi:10.1038/ng.284. PMID 19079262. S2CID 9876454.
  • Zhang L, Hou X, Lu S, et al. (2010). "Predictive significance of bone sialoprotein and osteopontin for bone metastases in resected Chinese non-small-cell lung cancer patients: a large cohort retrospective study". Lung Cancer. 67 (1): 114–9. doi:10.1016/j.lungcan.2009.03.017. PMID 19376608.
  • Roca H, Phimphilai M, Gopalakrishnan R, et al. (2005). "Cooperative interactions between RUNX2 and homeodomain protein-binding sites are critical for the osteoblast-specific expression of the bone sialoprotein gene". J. Biol. Chem. 280 (35): 30845–55. doi:10.1074/jbc.M503942200. PMID 16000302.
  • Lamour V, Detry C, Sanchez C, et al. (2007). "Runx2- and histone deacetylase 3-mediated repression is relieved in differentiating human osteoblast cells to allow high bone sialoprotein expression". J. Biol. Chem. 282 (50): 36240–9. doi:10.1074/jbc.M705833200. PMID 17956871.
  • Ogata Y (2008). "Bone sialoprotein and its transcriptional regulatory mechanism". Journal of Periodontal Research. 43 (2): 127–35. doi:10.1111/j.1600-0765.2007.01014.x. PMID 18302613.
  • Papotti M, Kalebic T, Volante M, et al. (2006). "Bone sialoprotein is predictive of bone metastases in resectable non-small-cell lung cancer: a retrospective case-control study". J. Clin. Oncol. 24 (30): 4818–24. doi:10.1200/JCO.2006.06.1952. PMID 17050866.
  • Frank O, Heim M, Jakob M, et al. (2002). "Real-time quantitative RT-PCR analysis of human bone marrow stromal cells during osteogenic differentiation in vitro". J. Cell. Biochem. 85 (4): 737–46. doi:10.1002/jcb.10174. PMID 11968014. S2CID 23595289.
  • Yerges LM, Klei L, Cauley JA, et al. (2009). "High-Density Association Study of 383 Candidate Genes for Volumetric BMD at the Femoral Neck and Lumbar Spine Among Older Men". J. Bone Miner. Res. 24 (12): 2039–49. doi:10.1359/jbmr.090524. PMC 2791518. PMID 19453261.
  • Gordon JA, Sodek J, Hunter GK, Goldberg HA (2009). "Bone sialoprotein stimulates focal adhesion-related signaling pathways: role in migration and survival of breast and prostate cancer cells". J. Cell. Biochem. 107 (6): 1118–28. doi:10.1002/jcb.22211. PMID 19492334. S2CID 36937586.
  • Araki S, Mezawa M, Sasaki Y, et al. (2009). "Parathyroid hormone regulation of the human bone sialoprotein gene transcription is mediated through two cAMP response elements". J. Cell. Biochem. 106 (4): 618–25. doi:10.1002/jcb.22039. PMID 19127545. S2CID 5586385.
  • Wuttke M, Müller S, Nitsche DP, Paulsson M, Hanisch FG, Maurer P (September 2001). "Structural characterization of human recombinant and bone-derived bone sialoprotein. Functional implications for cell attachment and hydroxyapatite binding". J. Biol. Chem. 276 (39): 36839–48. doi:10.1074/jbc.M105689200. PMID 11459848.
  • Hilbig H, Wiener T, Armbruster FP, et al. (2005). "Effects of dental implant surfaces on the expression of bone sialoprotein in cells derived from human mandibular bone". Med. Sci. Monit. 11 (4): BR111–5. PMID 15795688.
  • Koller DL, Ichikawa S, Lai D, et al. (2010). "Genome-Wide Association Study of Bone Mineral Density in Premenopausal European-American Women and Replication in African-American Women". J. Clin. Endocrinol. Metab. 95 (4): 1802–9. doi:10.1210/jc.2009-1903. PMC 2853986. PMID 20164292.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Fujisawa R (2002). "[Recent advances in research on bone matrix proteins]". Nippon Rinsho. 60 Suppl 3: 72–8. PMID 11979972.
  • Loibl S, Königs A, Kaufmann M, Costa SD, Bischoff J (December 2006). "[PTHrP and bone sialoprotein as prognostic markers for developing bone metastases in breast cancer patients]". Zentralbl Gynakol (in German). 128 (6): 330–5. doi:10.1055/s-2006-942314. PMID 17213971.
  • Uccello M, Malaguarnera G, Vacante M, et al. (2011). "Serum bone sialoprotein levels and bone metastases". J. Cancer Res. Ther. 7 (2): 115–9. doi:10.4103/0973-1482.82912. PMID 21768695.

March 17, 2023
bone, sialoprotein, component, mineralized, tissues, such, bone, dentin, cementum, calcified, cartilage, significant, component, bone, extracellular, matrix, been, suggested, constitute, approximately, collagenous, proteins, found, bone, cementum, sibling, pro. Bone sialoprotein BSP is a component of mineralized tissues such as bone dentin cementum and calcified cartilage 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 and cementum 5 BSP a SIBLING protein was originally isolated from bovine cortical bone as a 23 kDa glycopeptide with high sialic acid content 6 7 IBSPIdentifiersAliasesIBSP BNSP BSP BSP II SP II integrin binding sialoproteinExternal IDsOMIM 147563 MGI 96389 HomoloGene 3644 GeneCards IBSPGene location Human Chr Chromosome 4 human 1 Band4q22 1Start87 799 554 bp 1 End87 812 435 bp 1 Gene location Mouse Chr Chromosome 5 mouse 2 Band5 E5 5 50 68 cMStart104 447 037 bp 2 End104 459 335 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed intibiaperiodontal fibercancellous boneamniotic fluidfrontal polemiddle frontal gyruscerebellar vermisvisceral pleuratracheabody of tongueTop expressed inbody of femurcalvariafossamolarcondyleanklemandibleankle jointolfactory epitheliumintercostal muscleMore reference expression dataBioGPSn aGene ontologyMolecular functionintegrin binding molecular functionCellular componentextracellular matrix extracellular region membrane extracellular space vesicleBiological processbiomineral tissue development bone mineralization cellular response to growth factor stimulus cell adhesion extracellular matrix organization osteoblast differentiation ossification positive regulation of cell adhesionSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez338115891EnsemblENSG00000029559ENSMUSG00000029306UniProtP21815Q61711RefSeq mRNA NM 004967NM 008318RefSeq protein NP 004958NP 032344Location UCSC Chr 4 87 8 87 81 MbChr 5 104 45 104 46 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseThe 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 8 Contents 1 Structure 2 Function 3 References 4 External links 5 Further readingStructure EditNative BSP has an apparent molecular weight of 60 80 kDa based on SDS PAGE which is a considerable deviation from the predicted weight based on cDNA sequence of approximately 33 kDa 9 The mammalian BSP cDNAs encode for proteins averaging 317 amino acids which includes the 16 residue preprotein secretory signal peptide Among the mammalian cDNAs currently characterized there is an approximate 45 conservation of sequence identity and a further 10 23 conservative substitution The protein is highly acidic pKa of 3 9 10 and contains a large amount of Glu residues constituting 22 of the total amino acid Secondary structure prediction and hydrophobicity analyses suggest that the primary sequence of BSP has an open flexible structure with the potential to form regions of a helix and some b sheet 11 However the majority of studies have demonstrated that BSP has no a helical or b sheet structure by 1D NMR 10 12 and circular dichroism 13 Analysis of native protein by electron microscopy confirm that the protein has an extended structure approximately 40 nm in length 14 This flexible conformation suggests that the protein has few structural domains however it has been suggested that there may be several spatially segmented functional domains including a hydrophobic collagen binding domain rattus norvegicus residues 36 57 15 a hydroxyapatite nucleating region of contiguous glutamic acid residues rattus norvegicus residues 78 85 155 164 13 and a classical integrin binding motif RGD near the C terminal rattus norvegicus residues 288 291 BSP has been demonstrated to be extensively post translationally modified with carbohydrates and other modifications comprising approximately 50 of the molecular weight of the native protein 16 17 These modifications which include N and O linked glycosylation tyrosine sulfation and serine and threonine phosphorylation make the protein highly heterogeneous A 3D model of human bone sialoprotein has been developed using molecular modelling techniques as shown in the picture above The model suggests that the protein provides a flexible template for the rapid self assembly of calcium and phosphate ions so nucleating the growth of hydroxyapatite crystals 18 Function EditThe amount of BSP in bone and dentin is roughly equal 19 however the function of BSP in these mineralized tissues is not known One possibility is that BSP acts as a nucleus for the formation of the first apatite crystals 20 As the apatite forms along the collagen fibres within the extracellular matrix BSP could then help direct redirect or inhibit the crystal growth Additional roles of BSP are angiogenesis and protection from complement mediated cell lysis Regulation of the BSP gene is important to bone matrix mineralization and tumor growth in bone 21 References Edit a b c GRCh38 Ensembl release 89 ENSG00000029559 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000029306 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Fisher LW McBride OW Termine JD Young MF February 1990 Human bone sialoprotein Deduced protein sequence and chromosomal localization J Biol Chem 265 4 2347 51 doi 10 1016 S0021 9258 19 39982 X PMID 2404984 Williams PA Peacocke AR November 1965 The physical properties of a glycoprotein from bovine cortical bone bone sialoprotein Biochim Biophys Acta 101 3 327 35 doi 10 1016 0926 6534 65 90011 4 PMID 5862222 Herring GM February 1964 Comparison of bovine bone sialoprotein and serum orosomucoid Nature 201 4920 709 Bibcode 1964Natur 201 709H doi 10 1038 201709a0 PMID 14139700 S2CID 4210187 Kerr JM Fisher LW Termine JD Wang MG McBride OW Young MF August 1993 The human bone sialoprotein gene IBSP genomic localization and characterization Genomics 17 2 408 15 doi 10 1006 geno 1993 1340 PMID 8406493 Fisher LW Whitson SW Avioli LV Termine JD October 1983 Matrix sialoprotein of developing bone J Biol Chem 258 20 12723 7 doi 10 1016 S0021 9258 17 44236 0 PMID 6355090 a b Stubbs JT Mintz KP Eanes ED Torchia DA Fisher LW August 1997 Characterization of native and recombinant bone sialoprotein delineation of the mineral binding and cell adhesion domains and structural analysis of the RGD domain J Bone Miner Res 12 8 1210 22 doi 10 1359 jbmr 1997 12 8 1210 PMID 9258751 S2CID 26407786 Shapiro HS Chen J Wrana JL Zhang Q Blum M Sodek J November 1993 Characterization of porcine bone sialoprotein primary structure and cellular expression Matrix 13 6 431 40 doi 10 1016 s0934 8832 11 80109 5 PMID 8309422 Fisher LW Torchia DA Fohr B Young MF Fedarko NS January 2001 Flexible structures of SIBLING proteins bone sialoprotein and osteopontin Biochem Biophys Res Commun 280 2 460 5 doi 10 1006 bbrc 2000 4146 PMID 11162539 a b Tye CE Rattray KR Warner KJ Gordon JA Sodek J Hunter GK Goldberg HA March 2003 Delineation of the hydroxyapatite nucleating domains of bone sialoprotein J Biol Chem 278 10 7949 55 doi 10 1074 jbc M211915200 PMID 12493752 Oldberg A Franzen A Heinegard D December 1988 The primary structure of a cell binding bone sialoprotein J Biol Chem 263 36 19430 2 doi 10 1016 S0021 9258 19 77651 0 PMID 3198635 Tye CE Hunter GK Goldberg HA April 2005 Identification of the type I collagen binding domain of bone sialoprotein and characterization of the mechanism of interaction J Biol Chem 280 14 13487 92 doi 10 1074 jbc M408923200 PMID 15703183 Kinne RW Fisher LW July 1987 Keratan sulfate proteoglycan in rabbit compact bone is bone sialoprotein II J Biol Chem 262 21 10206 11 doi 10 1016 S0021 9258 18 61099 3 PMID 2956253 Ganss B Kim RH Sodek J 1999 Bone sialoprotein Crit Rev Oral Biol Med 10 1 79 98 doi 10 1177 10454411990100010401 PMID 10759428 Vincent K Durrant MC 2013 A structural and functional model for human bone sialoprotein PDF J Mol Graph Model 39 108 117 doi 10 1016 j jmgm 2012 10 007 PMID 23261880 Qin C Brunn JC Jones J George A Ramachandran A Gorski JP Butler WT April 2001 A comparative study of sialic acid rich proteins in rat bone and dentin Eur J Oral Sci 109 2 133 41 doi 10 1034 j 1600 0722 2001 00001 x PMID 11347657 Hunter GK Goldberg HA August 1994 Modulation of crystal formation by bone phosphoproteins role of glutamic acid rich sequences in the nucleation of hydroxyapatite by bone sialoprotein Biochem J 302 Pt 1 Pt 1 175 9 doi 10 1042 bj3020175 PMC 1137206 PMID 7915111 Ogata Y April 2008 Bone sialoprotein and its transcriptional regulatory mechanism Journal of Periodontal Research 43 2 127 35 doi 10 1111 j 1600 0765 2007 01014 x PMID 18302613 External links EditHuman IBSP genome location and IBSP gene details page in the UCSC Genome Browser Further reading EditKaradag A Fisher LW 2006 Bone sialoprotein enhances migration of bone marrow stromal cells through matrices by bridging MMP 2 to alpha v beta3 integrin J Bone Miner Res 21 10 1627 36 doi 10 1359 jbmr 060710 PMID 16995818 S2CID 84886034 Barnes GL Javed A Waller SM et al 2003 Osteoblast related transcription factors Runx2 Cbfa1 AML3 and MSX2 mediate the expression of bone sialoprotein in human metastatic breast cancer cells Cancer Res 63 10 2631 7 PMID 12750290 Carlinfante G Vassiliou D Svensson O et al 2003 Differential expression of osteopontin and bone sialoprotein in bone metastasis of breast and prostate carcinoma Clin Exp Metastasis 20 5 437 44 doi 10 1023 A 1025419708343 PMID 14524533 S2CID 341938 Hwang Q Cheifetz S Overall CM et al 2009 Bone sialoprotein does not interact with pro gelatinase A MMP 2 or mediate MMP 2 activation BMC Cancer 9 121 doi 10 1186 1471 2407 9 121 PMC 2679042 PMID 19386107 Styrkarsdottir U Halldorsson BV Gretarsdottir S et al 2009 New sequence variants associated with bone mineral density Nat Genet 41 1 15 7 doi 10 1038 ng 284 PMID 19079262 S2CID 9876454 Zhang L Hou X Lu S et al 2010 Predictive significance of bone sialoprotein and osteopontin for bone metastases in resected Chinese non small cell lung cancer patients a large cohort retrospective study Lung Cancer 67 1 114 9 doi 10 1016 j lungcan 2009 03 017 PMID 19376608 Roca H Phimphilai M Gopalakrishnan R et al 2005 Cooperative interactions between RUNX2 and homeodomain protein binding sites are critical for the osteoblast specific expression of the bone sialoprotein gene J Biol Chem 280 35 30845 55 doi 10 1074 jbc M503942200 PMID 16000302 Lamour V Detry C Sanchez C et al 2007 Runx2 and histone deacetylase 3 mediated repression is relieved in differentiating human osteoblast cells to allow high bone sialoprotein expression J Biol Chem 282 50 36240 9 doi 10 1074 jbc M705833200 PMID 17956871 Ogata Y 2008 Bone sialoprotein and its transcriptional regulatory mechanism Journal of Periodontal Research 43 2 127 35 doi 10 1111 j 1600 0765 2007 01014 x PMID 18302613 Papotti M Kalebic T Volante M et al 2006 Bone sialoprotein is predictive of bone metastases in resectable non small cell lung cancer a retrospective case control study J Clin Oncol 24 30 4818 24 doi 10 1200 JCO 2006 06 1952 PMID 17050866 Frank O Heim M Jakob M et al 2002 Real time quantitative RT PCR analysis of human bone marrow stromal cells during osteogenic differentiation in vitro J Cell Biochem 85 4 737 46 doi 10 1002 jcb 10174 PMID 11968014 S2CID 23595289 Yerges LM Klei L Cauley JA et al 2009 High Density Association Study of 383 Candidate Genes for Volumetric BMD at the Femoral Neck and Lumbar Spine Among Older Men J Bone Miner Res 24 12 2039 49 doi 10 1359 jbmr 090524 PMC 2791518 PMID 19453261 Gordon JA Sodek J Hunter GK Goldberg HA 2009 Bone sialoprotein stimulates focal adhesion related signaling pathways role in migration and survival of breast and prostate cancer cells J Cell Biochem 107 6 1118 28 doi 10 1002 jcb 22211 PMID 19492334 S2CID 36937586 Araki S Mezawa M Sasaki Y et al 2009 Parathyroid hormone regulation of the human bone sialoprotein gene transcription is mediated through two cAMP response elements J Cell Biochem 106 4 618 25 doi 10 1002 jcb 22039 PMID 19127545 S2CID 5586385 Wuttke M Muller S Nitsche DP Paulsson M Hanisch FG Maurer P September 2001 Structural characterization of human recombinant and bone derived bone sialoprotein Functional implications for cell attachment and hydroxyapatite binding J Biol Chem 276 39 36839 48 doi 10 1074 jbc M105689200 PMID 11459848 Hilbig H Wiener T Armbruster FP et al 2005 Effects of dental implant surfaces on the expression of bone sialoprotein in cells derived from human mandibular bone Med Sci Monit 11 4 BR111 5 PMID 15795688 Koller DL Ichikawa S Lai D et al 2010 Genome Wide Association Study of Bone Mineral Density in Premenopausal European American Women and Replication in African American Women J Clin Endocrinol Metab 95 4 1802 9 doi 10 1210 jc 2009 1903 PMC 2853986 PMID 20164292 Strausberg RL Feingold EA Grouse LH et al 2002 Generation and initial analysis of more than 15 000 full length human and mouse cDNA sequences Proc Natl Acad Sci U S A 99 26 16899 903 Bibcode 2002PNAS 9916899M doi 10 1073 pnas 242603899 PMC 139241 PMID 12477932 Fujisawa R 2002 Recent advances in research on bone matrix proteins Nippon Rinsho 60 Suppl 3 72 8 PMID 11979972 Loibl S Konigs A Kaufmann M Costa SD Bischoff J December 2006 PTHrP and bone sialoprotein as prognostic markers for developing bone metastases in breast cancer patients Zentralbl Gynakol in German 128 6 330 5 doi 10 1055 s 2006 942314 PMID 17213971 Uccello M Malaguarnera G Vacante M et al 2011 Serum bone sialoprotein levels and bone metastases J Cancer Res Ther 7 2 115 9 doi 10 4103 0973 1482 82912 PMID 21768695 Retrieved from https en wikipedia org w index php title Bone sialoprotein amp oldid 1075478686, wikipedia, wiki, book, books, library,

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