- 1) Shin, K., Tomita, M., and Lönnerdal, B., Identification of lactoperoxidase in mature human milk. J. Nutr. Biochem., 11, 94–102 (2000).
- 2) Thomas, E. L., Bozeman, P. M., and Learn, D. B., Lactoperoxidase: structure and catalytic properties. In “Peroxidases in Chemistry and Biology” Vol. 1, eds. Everse, J., Everse, K. E., and Grisham, M. B., CRC Press, Boca Raton, pp. 123–142 (1991).
- 3) Kussendrager, K. D., and van Hooijdonk, A. C. M., Lactoperoxidase: physico-chemical properties, occurrence, mechanism of action and applications. Br. J. Nutr., 84, S19–S25 (2000).
- 4) Shin, K., Yamauchi, K., Teraguchi, S., Hayasawa, H., and Imoto, I., Susceptibility of Helicobacter pylori and its urease activity to the peroxidase-hydrogen peroxide-thiocyanate antimicrobial system. J. Med. Microbiol., 51, 231–237 (2002).
- 5) Gerson, C., Sabater, J., Scuri, M., Torbati, A., Coffey, R., Abraham, J. W., Lauredo, I., Forteza, R., Wanner, A., Salathe, M., Abraham, W. M., and Conner, G. E., The lactoperoxidase system functions in bacterial clearance of airways. Am. J. Respir. Cell Mol. Biol., 22, 665–671 (2000).
- 6) Reiter, B., Marshall, V. M., and Philips, S. M., The antibiotic activity of the lactoperoxidase-thiocyanate-hydrogen peroxide system in the calf abomasums. Res. Vet. Sci., 28, 116–122 (1980).
- 7) Tenovuo, J., Clinical applications of antimicrobial host proteins lactoperoxidase, lysozyme and lactoferrin in xerostomia: efficacy and safety. Oral Dis., 8, 23–29 (2002).
- 8) Lefkowitz, D. L., Hsieh, T.-C., Millis, K., and Castro, A., Induction of tumor necrosis factor and cytotoxicity by macrophages exposed to lactoperoxidase and microperoxidase. Life Sci., 47, 703–709 (1990).
- 9) Lefkowitz, D. L., Lefkowitz, S. S., Mone, J., and Everse, J., Peroxidase-induced enhancement of chemiluminescence by murine peritoneal macrophages. Life Sci., 43, 739–745 (1988).
- 10) Wong, C. W., Seow, H. F., Husband, A. J., Regester, G. O., and Watson, D. L., Effects of purified bovine whey factors on cellular immune functions in ruminants. Vet. Immunol. Immunopathol., 56, 85–96 (1997).
- 11) Wong, C. W., Regester, G. O., Francis, G. L., and Watson, D. L., Immunomodulatory activities of whey fractions in efferent prefemoral lymph of sheep. J. Dairy Res., 63, 257–267 (1996).
- 12) Shin, K., Wakabayashi, H., Yamauchi, K., Teraguchi, S., Tamura, Y., Kurokawa, M., and Shiraki, K., Effects of orally administered bovine lactoferrin and lactoperoxidase on influenza virus infection in mice. J. Med. Microbiol., 54, 717–723 (2005).
- 13) Morrison, M., and Hultquist, D. E., Lactoperoxidase II. Isolation. J. Biol. Chem., 238, 2847–2849 (1963).
- 14) Quaroni, A., Wands, J., Trelstad, R. L., and Isselbacher, K. J., Epithelioid cell cultures from rat small intestine: characterization by morphologic and immunologic criteria. J. Cell Biol., 80, 248–265 (1979).
- 15) Wakabayashi, H., Takakura, N., Yamauchi, K., and Tamura, Y., Modulation of immunity-related gene expression in small intestines of mice by oral administration of lactoferrin. Clin. Vaccine Immunol., 13, 239–245 (2006).
- 16) Baughman, G., Wiederrecht, G. J., Campbell, N. F., Martin, M. M., and Bourgeois, S., FKBP51, a novel T-cell-specific immunophilin capable of calcineurin inhibition. Mol. Cell. Biol., 15, 4395–4402 (1995).
- 17) Baughman, G., Wiederrecht, G. J., Chang, F., Martin, M. M., and Bourgeois, S., Tissue distribution and abundance of human FKBP51, an FK506-binding protein that can mediate calcineurin inhibition. Biochem. Biophys. Res. Commun., 232, 437–443 (1997).
- 18) Bouwmeester, T., Bauch, A., Ruffner, H., Angrand, P.-O., Bergamini, G., Croughton, K., Cruciat, C., Eberhard, D., Gagneur, J., Ghidelli, S., Hopf, C., Huhse, B., Mangano, R., Michon, A.-M., Schirle, M., Schlegl, J., Schwab, M., Stein, M. A., Bauer, A., Casari, G., Drewes, G., Givin, A.-C., Jackson, D. B., Joberty, G., Neubauer, G., Rick, J., Kuster, B., and Superti-Furga, G., A physical and functional map of the human TNF-α/NF-κB signal transduction pathway. Nat. Cell Biol., 6, 97–105 (2004).
- 19) Binder, E. B., Salyakina, D., Lichtner, P., Wochnik, G. M., Ising, M., Pütz, B., Papiol, S., Seaman, S., Lucae, S., Kohli, M. A., Nickel, T., Künzel, H. E., Fuchs, B., Majer, M., Pfennig, A., Kern, N., Brunner, J., Modell, S., Baghai, T., Deiml, T., Zill, P., Bondy, B., Rupprecht, R., Messer, T., Köhnlein, O., Dabitz, H., Brückl, T., Müller, N., Pfister, H., Lieb, R., Mueller, J. C., Lõhmussaar, E., Strom, T. M., Bettecken, T., Meitinger, T., Uhr, M., Rein, T., Holsboer, F., and Muller-Myhsok, B., Polymorphisms in FKBP5 are associated with increased recurrence of depressive episodes and rapid response to antidepressant treatment. Nat. Genet., 36, 1319–1325 (2004).
- 20) Webster, M. K., Goya, L., Ge, Y., Maiyar, A. C., and Firestone, G. L., Characterization of sgk, a novel member of the serine/threonine protein kinase gene family which is transcriptionally induced by glucocorticoids and serum. Mol. Cell. Biol., 13, 2031–2040 (1993).
- 21) Wang, Z., Malone, M. H., Thomenius, M. J., Zhong, F., Xu, F., and Distelhorst, D. W., Dexamethasone-induced gene 2 (dig2) is a novel pro-survival stress gene induced rapidly by diverse apoptotic signals. J. Biol. Chem., 278, 27053–27058 (2003).
- 22) Cassuto, H., Kochan, K., Chakravarty, K., Cohen, H., Blum, B., Olswang, Y., Hakimi, P., Xu, C., Massillon, D., Hanson, R. W., and Reshef, L., Glucocorticoids regulate transcription of the gene for phosphoenolpyruvate carboxykinase in the liver via an extended glucocorticoid regulatory unit. J. Biol. Chem., 280, 33873–33884 (2005).
- 23) Berrebi, D., Bruscoli, S., Cohen, N., Foussat, A., Migliorati, G., Bouchet-Delbos, L., Maillot, M.-C., Portier, A., Couderc, J., Galanaud, P., Peuchmaur, M., Riccardi, C., and Emilie, D., Synthesis of glucocorticoid-induced leucine zipper (GILZ) by macrophages: an anti-inflammatory and immunosuppressive mechanism shared by glucocorticoids and IL-10. Blood, 101, 729–738 (2003).
- 24) Agbemafle, B. M., Oesterreicher, T. J., Shaw, C. A., and Henning, S. J., Immediate early genes of glucocorticoid action on the developing intestine. Am. J. Physiol. Gastrointest. Liver Physiol., 288, G897–G906 (2005).
- 25) Widney, D. P., Xia, Y.-R., Lusis, A. J., and Smith, J. B., The murine chemokine CXCL11 (IFN-inducible T cell α chemoattractant) is an IFN-γ- and lipopolysaccharide-inducible glucocorticoid-attenuated response gene expressed in lung and other tissues during endotoxemia. J. Immunol., 164, 6322–6331 (2000).
- 26) Abu-Soud, H. M., and Hazen, S. L., Nitric oxide is a physiological substrate for mammalian peroxidases. J. Biol. Chem., 275, 37524–37532 (2000).
- 27) Abu-Soud, H. M., Khassawneh, M. Y., Sohn, J.-T., Murray, P., Haxhiu, M. A., and Hazen, S. L., Peroxidases inhibit nitric oxide (NO) dependent bronchodilation: development of a model describing NO-peroxidase interactions. Biochemistry, 40, 11866–11875 (2001).
Full access
Orally Administered Lactoperoxidase Increases Expression of the FK506 Binding Protein 5 Gene in Epithelial Cells of the Small Intestine of Mice: A DNA Microarray Study
Reprints and Corporate Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
To request a reprint or corporate permissions for this article, please click on the relevant link below:
Academic Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
Obtain permissions instantly via Rightslink by clicking on the button below:
If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.
Related research
People also read lists articles that other readers of this article have read.
Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.
Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.