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Gene Review

SPP1  -  secreted phosphoprotein 1

Bos taurus

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Disease relevance of SPP1

  • The association of the SPP1 marker with birth weight (P < 0.006), weaning weight (P < 0.007), and yearling weight (P < 0.003) was consistent with the previously reported effects of SPP1 genotype on yearling weight [1].
  • We conclude therefore, that the inhibitory potency of the bone sialoprotein-derived peptides on breast cancer cell adhesion to bone is not solely due to a properly positioned RGD-motif alone but is also determined by its flanking regions, together with the tertiary structure of the EPRGDNYR peptide [2].
  • Osteopontin (OPN) is a highly modified protein that is found in many tissues and has been associated with a variety of physiological and pathological processes [3].
  • Bone OPN is a potent inhibitor of hydroxyapatite crystal formation and stimulates bone resorption by osteoclasts; these activities, as well as others, are dependent upon phosphorylation of the protein [3].
  • While the protein substrates to which OPN is linked in vivo have not been identified, it is reasonable to speculate that this capacity of OPN may dictate its extracellular location and thereby affect its role in bone homeostasis, tumorigenesis, metastasis, resistance to bacterial infections or, perhaps, wound repair [4].

High impact information on SPP1


Biological context of SPP1

  • Phosphorylation of purified bovine bone sialoprotein and osteopontin by protein kinases [8].
  • Phenotypic records for this population included twinning rate and ovulation rate, providing an opportunity to examine the potential effects of SPP1 genotype on reproductive traits [1].
  • Association of a single nucleotide polymorphism in SPP1 with growth traits and twinning in a cattle population selected for twinning rate [1].
  • In the current investigation we report the genomic organization of the SPP1 gene, which comprises seven exons, six of which contain coding sequence [9].
  • A highly informative short tandem repeat polymorphism isolated at the SPP1 locus showed no recombination with the autosomal dominant disorder dentinogenesis imperfecta type II [9].

Anatomical context of SPP1

  • The large number of covalently bound phosphates on the extracellular phosphoproteins osteopontin (OPN) and bone sialoprotein (BSP) have been implicated in biological functions such as mineral deposition and osteoclast binding [8].
  • Osteopontin (SPP1) is the principal phosphorylated glycoprotein of bone that is also expressed in a limited number of other tissues including dentine [9].
  • Chondrocytes, which had been maintained in suspension culture, attached to fibronectin, bone sialoprotein, collagen II, and two novel 36- and 58-kDa proteins isolated from cartilage [10].
  • When the soluble digests were chromatographed on DEAE-cellulose, the elution profiles indicated the presence in each tissue of a variety of glycoproteins and a proteoglycan fraction, and showed clearly that an acidic glycoprotein corresponding to bone sialoprotein was not present in tendon [11].
  • We concluded that the primary sources of OPN in bull SP are the seminal vesicles and ampulla [12].

Associations of SPP1 with chemical compounds

  • Osteopontin (OPN) is a multiphosphorylated glycoprotein found in bone and other normal and malignant tissues, as well as in the physiological fluids urine and milk [13].
  • These data collectively demonstrate that dual alpha(4)beta(1) integrin binding sites are present in a 38 amino acid domain within the N-terminal thrombin fragment of OPN [14].
  • Attachment to fibronectin and bone sialoprotein was inhibited by competition with an Arg-Gly-Asp containing peptide, whereas attachment to the 36- and the 58-kDa proteins was not affected [10].
  • OPN was not detected immunohistochemically in epididymal, ampullary, or ejaculated sperm treated with or without Triton X-100 [12].
  • In EDTA extracts of long bones, the majority of the radiolabel was demonstrated to be associated with intact OPN [15].

Other interactions of SPP1


Analytical, diagnostic and therapeutic context of SPP1


  1. Association of a single nucleotide polymorphism in SPP1 with growth traits and twinning in a cattle population selected for twinning rate. Allan, M.F., Thallman, R.M., Cushman, R.A., Echternkamp, S.E., White, S.N., Kuehn, L.A., Casas, E., Smith, T.P. J. Anim. Sci. (2007) [Pubmed]
  2. Bone sialoprotein peptides are potent inhibitors of breast cancer cell adhesion to bone. van der Pluijm, G., Vloedgraven, H.J., Ivanov, B., Robey, F.A., Grzesik, W.J., Robey, P.G., Papapoulos, S.E., Lowik, C.W. Cancer Res. (1996) [Pubmed]
  3. Comprehensive identification of post-translational modifications of rat bone osteopontin by mass spectrometry. Keykhosravani, M., Doherty-Kirby, A., Zhang, C., Brewer, D., Goldberg, H.A., Hunter, G.K., Lajoie, G. Biochemistry (2005) [Pubmed]
  4. Osteopontin, a substrate for transglutaminase and factor XIII activity. Prince, C.W., Dickie, D., Krumdieck, C.L. Biochem. Biophys. Res. Commun. (1991) [Pubmed]
  5. Conflicting candidates for cattle QTLs. de Koning, D.J. Trends Genet. (2006) [Pubmed]
  6. A potential role for tetranectin in mineralization during osteogenesis. Wewer, U.M., Ibaraki, K., Schjørring, P., Durkin, M.E., Young, M.F., Albrechtsen, R. J. Cell Biol. (1994) [Pubmed]
  7. Fetal bovine bone cells synthesize bone-specific matrix proteins. Whitson, S.W., Harrison, W., Dunlap, M.K., Bowers, D.E., Fisher, L.W., Robey, P.G., Termine, J.D. J. Cell Biol. (1984) [Pubmed]
  8. Phosphorylation of purified bovine bone sialoprotein and osteopontin by protein kinases. Salih, E., Zhou, H.Y., Glimcher, M.J. J. Biol. Chem. (1996) [Pubmed]
  9. Genomic organization of the human osteopontin gene: exclusion of the locus from a causative role in the pathogenesis of dentinogenesis imperfecta type II. Crosby, A.H., Edwards, S.J., Murray, J.C., Dixon, M.J. Genomics (1995) [Pubmed]
  10. Chondrocyte-matrix interactions. Attachment to proteins isolated from cartilage. Sommarin, Y., Larsson, T., Heinegård, D. Exp. Cell Res. (1989) [Pubmed]
  11. A comparison of bone matrix and tendon with particular reference to glycoprotein content. Herring, G.M. Biochem. J. (1976) [Pubmed]
  12. Osteopontin localization in the Holstein bull reproductive tract. Cancel, A.M., Chapman, D.A., Killian, G.J. Biol. Reprod. (1999) [Pubmed]
  13. Posttranslational modifications of bovine osteopontin: identification of twenty-eight phosphorylation and three O-glycosylation sites. Sørensen, E.S., Højrup, P., Petersen, T.E. Protein Sci. (1995) [Pubmed]
  14. Identification of dual alpha 4beta1 integrin binding sites within a 38 amino acid domain in the N-terminal thrombin fragment of human osteopontin. Bayless, K.J., Davis, G.E. J. Biol. Chem. (2001) [Pubmed]
  15. Blood circulation as source for osteopontin in acellular extrinsic fiber cementum and other mineralizing tissues. VandenBos, T., Bronckers, A.L., Goldberg, H.A., Beertsen, W. J. Dent. Res. (1999) [Pubmed]
  16. Role of bovine bone morphogenetic proteins in bone matrix protein and osteoblast-related gene expression during rat bone marrow stromal cell differentiation. Hu, Z., Peel, S.A., Ho, S.K., Sándor, G.K., Clokie, C.M. The Journal of craniofacial surgery. (2005) [Pubmed]
  17. Molecular cloning and sequence analysis of cDNA for a 59 kD bone sialoprotein of the rat: demonstration that it is a counterpart of human alpha 2-HS glycoprotein and bovine fetuin. Ohnishi, T., Nakamura, O., Ozawa, M., Arakaki, N., Muramatsu, T., Daikuhara, Y. J. Bone Miner. Res. (1993) [Pubmed]
  18. Localization of transglutaminase-reactive glutamine residues in bovine osteopontin. Sørensen, E.S., Rasmussen, L.K., Møller, L., Jensen, P.H., Højrup, P., Petersen, T.E. Biochem. J. (1994) [Pubmed]
  19. Osteopontin is the 55-kilodalton fertility-associated protein in Holstein bull seminal plasma. Cancel, A.M., Chapman, D.A., Killian, G.J. Biol. Reprod. (1997) [Pubmed]
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