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Development of a Novel, Anti-idiotypic Monoclonal Anti-prolactin Antibody That Mimics the Physiological Functions of Prolactin

  • Wang, Meng (Endocrine Department, Yidu Central Hospital of Weifang) ;
  • Zhang, Dian-Cai (Dermatological Department, Yidu Central Hospital of Weifang) ;
  • Wang, Shen-Tian (Endocrine Department, Yidu Central Hospital of Weifang) ;
  • Li, Ming-Long (China Shandong Provincial Hospital)
  • Received : 2015.06.26
  • Accepted : 2015.09.03
  • Published : 2016.04.01

Abstract

In this work, we prepared a panel of monoclonal anti-idiotypic antibodies to ovine prolactin (oPRL) by the hybridoma technique. Among these antibodies, one anti-idotypic antibody (designated B7) was chosen for further characterization by a series of experiments. We first demonstrated that B7 behaved as a typical $Ab2{\beta}$ based on a series of enzyme-linked immunosorbent assays. Subsequently, the results of a competitive receptor-binding assay confirmed that B7 could specifically bind to the prolactin receptor (PRLR) expressed on target cells. Finally, we examined its biological activities in CHO-PRLR and Nb2 cells and observed that B7 could activate Janus kinase 2-signal transducer and activator of transcription signalling in CHO-PRLR and Nb2 cells and induce BaF3 proliferation. The present study suggests that i) B7 can serve as a PRLR agonist or PRL mimic and has potential applications in regulating mammary gland development, milk production and maintenance of lactation in domestic animals and ii) B7 may be a biological reagent that can be used to explore the mechanism of PRLR-mediated intracellular signalling.

Keywords

References

  1. Amit, T., R. J. Barkey, M. Gavish, and M. B. H. Youdim. 1986. Antiidiotypic antibodies raised against anti-prolactin (prl) antibodies recognize the prl receptor. Endocrinology 118:835-843. https://doi.org/10.1210/endo-118-2-835
  2. Bar-Pelled, U., E. Maltz, I. Bruckental, Y. Folman, Y. Kali, H. Gacitua, A. R. Lehrer., C. H. Knigh., B. Robinzon., H. Voet, and H. Tagari. 1995. Relationship between frequent milking or suckling in early lactation and milk production of high producing dairy cows. J. Dairy Sci. 78:2726-2736. https://doi.org/10.3168/jds.S0022-0302(95)76903-X
  3. Bole-Feysot, C., V. Goffin, M. Edery, N. Binart, and P. A. Kelly. 1998. Prolactin (PRL) and its receptor: actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice. Endocr. Rev. 19:225-268. https://doi.org/10.1210/edrv.19.3.0334
  4. Brooks, C. L. 2012. Molecular mechanisms of prolactin and its receptor. Endocr. Rev. 33:504-525. https://doi.org/10.1210/er.2011-1040
  5. Clevenger, C. V., T. Torigoe, and J. C. Reed. 1994. Prolactin induces rapid phosphorylation and activation of prolactin receptor-associated RAF-1 kinase in a T-cell line. J. Biol. Chem. 269:5559-5565.
  6. Djiane, J., I. Dusanter-Fourt, M. Katoh, and P. A. Kelly. 1985. Biological activities of binding site specific monoclonal antibodies to prolactin receptors of rabbit mammary gland. J. Biol. Chem. 260:11430-11435.
  7. Djiane, J., L. M. Houdebine, and P. A. Kelly. 1981. Prolactin-like activity of anti-prolactin receptor antibodies on casein and DNA synthesis in the mammary gland. Proc. Natl. Acad. Sci. USA. 78:7445-7448. https://doi.org/10.1073/pnas.78.12.7445
  8. Dybus, A. 2002. Associations of growth hormone (GH) and prolactin (PRL) genes polymorphisms with milk production traits in Polish Black-and-White cattle. Anim. Sci. Pap. Rep. 20:203-212.
  9. Farmer, C., M. T. Sorensen, and D. Petitclerc. 2000. Inhibition of prolactin in the last trimester of gestation decreases mammary gland development in gilts. J. Anim. Sci. 78:1303-1309. https://doi.org/10.2527/2000.7851303x
  10. Feuermann, Y., S. J. Mabjeesh, and A. Shamay. 2004. Leptin affects prolactin action on milk protein and fat synthesis in the bovine mammary gland. J. Dairy Sci. 87:2941-2946. https://doi.org/10.3168/jds.S0022-0302(04)73425-6
  11. Freeman, M. E., B. Kanyicska, A. Lerant, and G. Nagy. 2000. Prolactin: Structure, function, and regulation of secretion. Physiol. Rev. 80:1523-1631. https://doi.org/10.1152/physrev.2000.80.4.1523
  12. He, F., D. Sun, Y. Yu, Y. Wang, and Y. Zhang. 2006. Association between SNPs within prolactin gene and milk performance traits in Holstein dairy cattle. Asian Australas. J. Anim. 19:1384-1389. https://doi.org/10.5713/ajas.2006.1384
  13. Jerne, N. K. 1974. Towards a network theory of the immune system. Ann. Immunol. 125:373-389.
  14. Knight, C. H. 2001. Overview of prolactin's role in farm animal lactation. Livest. Prod. Sci. 70:87-93. https://doi.org/10.1016/S0301-6226(01)00200-7
  15. Lan, H. N., W. Li, Z. L. Fu, Y. H. Yang, T. C. Wu, Y. Liu, H. Zhang, H. Z. Cui, Y. M. Li, P. Hong, J. S. Liu, and X. Zheng. 2014. Differential intracellular signalling properties of the growth hormone receptor induced by the activation of an anti-GHR antibody. Mol. Cell. Endocrinol. 390:54-64. https://doi.org/10.1016/j.mce.2014.04.004
  16. Lan, H. N., H. L. Jiang, W. Li, T. C. Wu, P. Hong, Y. M. Li, H. Zhang, H. Z. Cui, and X. Zhing. 2015. Development and characterization of a novel anti-idiotypic monoclonal antibody to growth hormone, which can mimic physiological functions of growth hormone in primary porcine hepatocytes. Asian Australas. J. Anim. Sci. 28:573-583. https://doi.org/10.5713/ajas.14.0600
  17. Lan, H. N, X. Zheng, M. A. Khan, and S. Li. 2015. Anti-idiotypic antibody: A new strategy for the development of a growth hormone receptor antagonist. Int. J. Biochem. Cell. B. 68:101-108. https://doi.org/10.1016/j.biocel.2015.09.004
  18. McLaughlin, C. L., J. C. Byatt, D. F. Curran, J. J. Veenhuizen, M. F. McGrath, F. C. Buonomo, R. L. Hintz, and C. A. Baile. 1997. Growth performance, endocrine, and metabolite responses of finishing hogs to porcine prolactin. J. Anim. Sci. 75:959-967. https://doi.org/10.2527/1997.754959x
  19. Okamura, H., J. Zachwieja, S. Raguet, and P. A. Kelly. 1989. Characterization and Applications of Monoclonal Antibodies to the prolactin receptor. Endocrinology 124:2499-2508. https://doi.org/10.1210/endo-124-5-2499
  20. Ramos, A. M., C. A. P. Matos, P. A. Russo-Almeida, C. M. V. Bettencourt, J. Matos, A. Martins, C. Pinheiro, and T. Rangel-Figueiredo. 2009. Candidate genes for milk production traits in Portuguese dairy sheep. Small Rumin. Res. 82:117-121. https://doi.org/10.1016/j.smallrumres.2009.02.007
  21. Reddy, I. J., C. G. David, and K. Singh. 2005. Relationship between Intersequence pauses, laying persistency and concentration of prolactin during the productive period in white Leghorn hens. Asian Australas. J. Anim. Sci. 18:686-691. https://doi.org/10.5713/ajas.2005.686
  22. Rui, H., J. J. Lebrun, R. A. Kirken, P. A. Kelly, and W. L. Farrar. 1994. JAK2 activation and cell proliferation induced by antibody-mediated prolactin receptor dimerization. Endocrinology 135:1299-1306. https://doi.org/10.1210/endo.135.4.7925093
  23. Tygesen, M. P., M. O. Nielsen, P. Norgaard, H. Ranvig, A. P. Harrison, and A. H. Tauson. 2008. Late gestational nutrient restriction: Effects on ewes' metabolic and homeorhetic adaptation, consequences for lamb birth weight and lactation performance. Arch. Anim. Nutr. 62:44-59. https://doi.org/10.1080/17450390701780276

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