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Comparison of the Nucleotide Sequence of Cloned Osteopontin from Hanwoo and Holstein
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 Title & Authors
Comparison of the Nucleotide Sequence of Cloned Osteopontin from Hanwoo and Holstein
Lee, Tae Young; Ju, Sung Kyu; Nam, Myoung Soo;
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Osteopontin (OPN) is a secreted phosphorylated glycoprotein. It has an important role in multiple biological processes including cell survival, bone remodeling, inhibition of ectopic calcification, as well as, is thought to have potential immune modulation activities. In this work, we isolated and characterized a full-length open reading frame (ORF) of Korean native cow`s OPN from Korean native cow`s (Hanwoo) kidney, and successfully cloned firstly on Hanwoo`s OPN. The sequencing results indicated that the isolated cDNA was 1190 bp in length containing a complete ORF of 837 bp. It encoded a precursor protein Hanwoo`s OPN consisting of 278 amino acids with a signal peptide of 16 amino acids. Amino acid homology was found to be 99.3% as compared to the corresponding sequences of Holstein bone marrow OPN. Hanwoo`s kidney OPN and Holstein bone marrow OPN are different only in two amino acid residues 42 and 56, amino acid residue 42 is Thr (T) Ile (I), and amino acid residue 56 is Ala (A) Thr (T) respectively. These results from the present work would be helpful to elucidate the biological function of Hanwoo`s OPN and provided a foundation for further insight into role of Hanwoo`s OPN.
Korean native cow (Hanwoo);osteopontin;cloning;amino acid;
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Bayless, K. J., Davis, G. E., and Meininger, G. A. (1997) Isolation and biological properties of osteopontin from bovine milk. Protein Expr. Purific. 9, 309-314. crossref(new window)

Chomczynski, P. and Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenolchloroform extraction. Anal. Biochem. 162, 156-159.

Denhardt, D. T. and Guo, X. (1993) Osteopontin: A protein with diverse functions. FASEB J. 7, 1475-1482.

Kohri, K., Nomura, S., Kitamura, Y., Nagata, T., Yoshioka, K., Iguchi, M., Yamate, T., Umekawa, T., Suzuki, Y., and Shinohara, H. (1993) Structure and expression of the mRNA encoding urinary stone protein (osteopontin). J. Biol. Chem. 268, 15180-15184.

Kohri, K., Suzuki, Y.,Yamamoto, K., Amasaki, N., Yamata, T., Umekawa, T., Lguchi, M., Sinohara, H., and Kurita, T. (1992) Molecular cloning and sequencing of cDNA encoding urinary stone protein, which is identical to osteopontin. Biochem. Biophys. Res. Commun. 184, 859-864. crossref(new window)

Liaw, L., Skinner, M. P., Raines, E. W., Ross, R., Cheresh, D. A., Schwartz, S. M., and Giachelli, C. M. (1995) The adhesive and migratory effects of osteopontin are mediated via distinct cell surface integrins. Role of $a_vb_3$ in smooth muscle cell migration to osteopontin in vitro. J. Clin. Invest. 95, 713-724. crossref(new window)

Naficy, A. B., Abu-Elyazeed, R., and Holmes, J. L. (1999) Epidemiology of rotavirus diarrhea in Egyptian children and implications for disease control. Am. J. Epidemiol. 150, 77-777.

Nagatomo, T., Ohga, S., Takada, H., Nomura, A., Hikino, S., Imura, M., Ohshima, K., and Hara, T. (2004) Microarray analysis of human milk cell: Persistent high expression of osteopontin during the lactation period. Clin. Exp. Immuno. 138, 47-52. crossref(new window)

Oldberg, A., Franzen, A., and Heinegard, D.(1986) Cloning and sequence analysis of rat bone sialoprotein(osteopontin) cDNA reveals an Arg-Gly-Asp cell-binding sequence. Proc. Natl. Acad. Sci. U.S.A. 83, 8819-8823. crossref(new window)

Patarca, R., Saavedra. R., and Cantor, H. (1993) Molecular and cellular basis of genetic resistance to bacterial infection: the role of the early T-lymphocyte activation-1/osteopontin gene. Crit. Rev. Immunol. 13, 225-246.

Philip, S. and Kundu, G. C. (2003) Osteopontin induces nuclear factor kappa B-mediated promatrix metalloproteinase- 2 activation through I kappa B alpha /IKK signaling pathways, and curcumin (diferulolylmethane) down-regulates these pathways. J. Biol. Chem. 278, 14487-14497. crossref(new window)

Schack, L., Stapulionis, R., Christensen, B., Kofod-olsen, E., Skov Sorensen, U. B., Vorup-Jensen, T., Sorensen, E. S., and Hollsberg, P. (2009) Osteopontin enhances phagocytosis through a novel osteopontin receptor, the alphaXbeta2 integrin. J. Immunol. 182, 6943-6950. crossref(new window)

Senger, D. R., Peruzzi, C. A., Papadopoulos, A., and Tenen, D. G. (1989) Purification of a human milk protein closely similar to tumor-secreted phosphoproteins and osteopontin. Biochem. Biophys. Acta 996, 43-48. crossref(new window)

Shiraga, H., Min, W., VanDusen, W. J., Clayman, M. D., Miner, D., Terrell, C. H., Sherbotie, J. R., Foreman, J. W., Przysiecki, C., Neilson, E. G., and Hoyer, J. R. (1992) Inhibition of calcium oxalate crystal growth in vitro by uropontin, a new member of the aspartic acid-rich protein superfamily. Proc. Natl. Acad. Sci. U.S.A. 89, 426-430. crossref(new window)

Sorensen, S., Justesen, S. J., and Johnsen A. H. (2003) Purification and characterization of osteopontin from human milk. Protein Expr. Purific. 30, 238-245. crossref(new window)

Sorensen E. S. and Petersen, T. E. (1993) Purification and characterization of three proteins isolated from the proteose peptone fraction of bovine milk. J. Dairy Res. 60, 189-197. crossref(new window)

Sorensen, E. S., Rasmussen, L. K., Moller, L., Jensen, P. H., Hojrup, P., and Petersen, T. E. (1994) Localization of transglutaminase- reactive glutamine residues in bovine osteopontin. Biochem. J. 304, 13-16.

Wang, K. X. and Denhardt, D. T. (2008) Osteopontin: Role in immune regulation and stress responses. Cytokine Growth Factor Res. 19, 333-345. crossref(new window)

Weber, G. F. and Cantor, H. (1996) The immunology of Eta- 1/osteopontin. Cytokine Growth Factor Res. 7, 241-248. crossref(new window)