Asian Pacific Journal of Cancer Prevention

Asian Pacific Journal of Cancer Prevention (아시아태평양암예방학회)
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Expression and Clinical Significance of Osteopontin in Calcified Breast Tissue

  • Huan, Jin-Liang (General Surgery Department, The Eighth People's Hospital Of Shanghai) ;
  • Xing, Li (Gynaecology and Obstetrics Department, The Eighth People's Hospital Of Shanghai) ;
  • Qin, Xian-Ju (General Surgery Department, The Eighth People's Hospital Of Shanghai) ;
  • Gao, Zhi-Guang (General Surgery Department, The Eighth People's Hospital Of Shanghai) ;
  • Pan, Xiao-Feng (General Surgery Department, The Eighth People's Hospital Of Shanghai) ;
  • Zhao, Zhi-Dong (General Surgery Department, The Eighth People's Hospital Of Shanghai)
  • Published : 2012.10.31
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Abstract

Osteopontin (OPN) is an integrin-binding protein, believed to be involved in a variety of physiological cellular functions. The physiology of OPN is best documented in the bone where this secreted adhesive glycoprotein appears to be involved in osteoblast differentiation and bone formation. In our study, we used semi-quantitative RT-PCR of osteopontin in calcification tissue of breast to detect breast cancer metastasis. The obtained data indicate that the expression of osteopontin is related to calcification tissue of breast, and possibly with the incidence of breast cancer. The expression strength of OPN by RT-PCR detection was related to the degree of malignancy of breast lesions, suggesting a close relationship between OPN and breast calcification tissue. The results revealed that expression of OPN mRNA is related to calcification of breast cancer tissue and to the development of breast cancer. Determination of OPN mRNA expression can be expected to be a guide to clinical therapy and prediction of the prognosis of breast cancer patients.

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References

  1. Baht GS, Hunter GK, Goldberg HA (2008). Bone sialoprotein-collagen interaction promotes hydroxyapatite nucleation. Matrix Biol, 27, 600-8. https://doi.org/10.1016/j.matbio.2008.06.004
  2. Baughman RW, Bader CR (1977). Biochemical characterization and cellular localization of the cholinergic system in the chicken retina. Brain res, 138, 469-85. https://doi.org/10.1016/0006-8993(77)90684-9
  3. Behera R, Kumar V, Lohite K, et al (2010). Activation of JAK2/STAT3 signaling by osteopontin promotes tumor growth in human breast cancer cells. Carcinogenesis, 31, 192-200. https://doi.org/10.1093/carcin/bgp289
  4. Bianco P, Silvestrini G, Termine J, Bonucci E (1988). Immunohistochemical localization of osteonectin in developing human and calf bone using monoclonal antibodies. Calcified tissue int, 43, 155-61. https://doi.org/10.1007/BF02571313
  5. Bruder SP, Horowitz M, Mosca J, Haynesworth S (1997). Monoclonal antibodies reactive with human osteogenic cell surface antigens. Bone, 21, 225-35. https://doi.org/10.1016/S8756-3282(97)00127-0
  6. Catteau X, Simon P, Noël JC (2012). Predictors of invasive breast cancer in mammographically detected microcalcification in patients with a core biopsy diagnosis of flat epithelial atypia, atypical ductal hyperplasia or ductal carcinoma in situ and recommendations for a selective approach to sentinel lymph node biopsy. Pathol Res Pract, 208, 217-20. https://doi.org/10.1016/j.prp.2012.02.003
  7. El-Abbadi MM, Pai AS, Leaf EM, et al (2009). Phosphate feeding induces arterial medial calcification in uremic mice: role of serum phosphorus, fibroblast growth factor-23, and osteopontin. Kidney int, 75, 1297-307. https://doi.org/10.1038/ki.2009.83
  8. Kiefer MC, Bauer DM, Barr PJ (1989). The cDNA and derived amino acid sequence for human osteopontin. Nucleic acids res, 17, 3306. https://doi.org/10.1093/nar/17.8.3306
  9. Merry K, Dodds R, Littlewood A, Gowen M (1993). Expression of osteopontin mRNA by osteoclasts and osteoblasts in modelling adult human bone. J cell sci, 104, 1013-20.
  10. Mizobuchi M, Towler D, Slatopolsky E (2009). Vascular calcification: the killer of patients with chronic kidney disease. J Am Soc Nephrol, 20, 1453-64. https://doi.org/10.1681/ASN.2008070692
  11. Nomura S, Wills AJ, Edwards DR, et al (1988). Developmental expression of 2ar (osteopontin) and SPARC (osteonectin) RNA as revealed by in situ hybridization. J cell biol, 106, 441-50. https://doi.org/10.1083/jcb.106.2.441
  12. Rangaswami H, Bulbule A, Kundu GC (2006). Osteopontin: role in cell signaling and cancer progression. Trends in cell biol, 16, 79-87. https://doi.org/10.1016/j.tcb.2005.12.005
  13. Reinholt FP, Hultenby K, Oldberg A, Heinegård D (1990). Osteopontin--a possible anchor of osteoclasts to bone. P Natl Acad Sci, 87, 4473. https://doi.org/10.1073/pnas.87.12.4473
  14. Saad FA, Salih E, Glimcher MJ (2008). Identification of osteopontin phosphorylation sites involved in bone remodeling and inhibition of pathological calcification. J cellular biochem, 103, 852-6. https://doi.org/10.1002/jcb.21453
  15. Senger D, Perruzzi C, Papadopoulos A (1989). Elevated expression of secreted phosphoprotein I (osteopontin, 2ar) as a consequence of neoplastic transformation. Anticancer Res, 9, 1291.
  16. Senger DR, Perruzzi CA (1985). Secreted phosphoprotein markers for neoplastic transformation of human epithelial and fibroblastic cells. Cancer Res, 45, 5818.
  17. Staal A, Van Wijnen AJ, Birkenhäger J, et al (1996). Distinct conformations of vitamin D receptor/retinoid X receptor-alpha heterodimers are specified by dinucleotide differences in the vitamin D-responsive elements of the osteocalcin and osteopontin genes. Mol Endocrinol, 10, 1444-56. https://doi.org/10.1210/me.10.11.1444
  18. Uaesoontrachoon K, Yoo HJ, Tudor EM, et al (2008). Osteopontin and skeletal muscle myoblasts: Association with muscle regeneration and regulation of myoblast function< i> in vitro. Int J Biochem Cell Biol, 40, 2303-14. https://doi.org/10.1016/j.biocel.2008.03.020
  19. Vetrone SA, Montecino-Rodriguez E, Kudryashova E, et al (2009). Osteopontin promotes fibrosis in dystrophic mouse muscle by modulating immune cell subsets and intramuscular TGF-${\beta}$. J Clinical Invest, 119, 1583. https://doi.org/10.1172/JCI37662
  20. Wai PY, Kuo PC (2008). Osteopontin: regulation in tumor metastasis. Cancer Metastasis Rev, 27, 103-18. https://doi.org/10.1007/s10555-007-9104-9
  21. Wang KX, Denhardt DT (2008). Osteopontin: role in immune regulation and stress responses. Cytokine Growth Factor Rev, 19, 333-45. https://doi.org/10.1016/j.cytogfr.2008.08.001
  22. Young MF, Kerr JM, Termine JD, et al (1990). cDNA cloning, mRNA distribution and heterogeneity, chromosomal location, and RFLP analysis of human osteopontin (OPN). Genomics, 7, 491-502. https://doi.org/10.1016/0888-7543(90)90191-V

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