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Colostral Growth Factors

Possible Role in Bovine Udder Epithelial Cell Regeneration

Tillväxtstimulerande faktorer i kolostrum: möjlig roll i epitelcellregenerationen i kojuver.

Abstract

Growth of the secretory epithelium during prepartum time, and for a short period after calving, is under hormonal control by estrogen, progesterone and prolactin. The mechanism(s) by which these hormones act is not known but colostrum and milk have been shown to contain different growth promoting substances. In an attempt to unravel these relationships the effect of bovine colostrum on cellular proliferation in vitro have been characterized. Colostral thermostabile factors not present in milk nor associated with fat, potently induce the proliferation associated enzyme, ornithine decarboxylase, in fibroblast cell lines. However, mammary epithelial cells appear to proliferate in response to different colostral heat sensitive factor(s) that await further characterization.

Sammandrag

Det sekretoriska epitelets tillväxt i juvret under prepartum och en kort period efter kalvinigen står under hormonal kontroll genom estrogen, progesteron och prolaktin. De mekanismer genom vilka dessa hormoner utövar sin verkan är ej kända, men kolostrum och mjölk har påvisats innehålla tillväxtstimulerande faktorer. I ett försök att komma till klarhet med dessa mekanismer har vi studerat effekten av kolosrum från ko på cellers tillväxt in vitro. Kolostrala värmestabila faktorer, ej närvarande i mjölk eller associerade med fett, inducerar i fibroblastcellinjer en kraftig ökning i aktiviteten av ornitindekarboxylas, som är ett tillväxtassocierat enzym. Men epiteliala celler i juvret verkar även känna igen andra, ännu inte karaktiserade faktorer i kolostrum.

References

  1. Antoniades HN, Scher CD, Stiles CD: Purification of human platelet-derived growth factor. Proc. Natl. Acad. Sci. U.S.A. 1979, 76, 1809–1813.

    CAS  Article  Google Scholar 

  2. Carpenter G: Epidermal growth factor is a major growth-promoting agent in human milk. Science 1980, 210, 198–199.

    CAS  Article  Google Scholar 

  3. Di Fiore PP, Pierce JH, Fleming TP, Hazan R, Ullrich A, King CR, Schlessinger J, Aaronson SA: Overexpression of the human EGF receptor confers an EGF-dependent transformed phenotype to NIH-3T3 cells. Cell 1987, 51, 1063–1070.

    Article  Google Scholar 

  4. Goustin AS, Besholtz C, Pfeifer-Ohlsson S, Persson H, Rydnert J, Bywater M, Holmgren G, Heldin C-H, Westermark B, Ohlsson R: Coexpression of the sis and myc proto-oncogenes in developing human placenta suggests autocrine control of trophoblast growth. Cell 1985, 41, 301–312.

    CAS  Article  Google Scholar 

  5. Hanks SK, Quinn AM, Hunter T: The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains. Science 1988, 241, 42–52.

  6. Jaeger LA, Lamar CH, Bottoms GD, Cline TR: Growth stimulating substances in porcine milk. Amer. J. vet. Res. 1987, 48, 1531–1533.

    CAS  PubMed  Google Scholar 

  7. Jänne J, Pösö H, Raina A: Polyamines in rapid growth and cancer. Biochem. Biophys. Acta 1978, 473, 241–293.

    PubMed  Google Scholar 

  8. Kaartinen L, Veijalainen K, Kuosa PL, Pyörälä S, Sandholm M: Endotoxin- induced mastitis: Inhibition of casein synthesis and activation of the caseinolytic system. J. vet. Med. B 1988, 35, 353–360.

    CAS  Article  Google Scholar 

  9. Kraus MH, Issing W, Miki T, Popescu NC, Aaronson SA: Isolation and characterization of ERBB3, a third member of the ERBB/epidermal growth factor receptor family: Evidence for overexpression in a subset of human mammary tumors. Proc. Natl. Acad. Sci. U.S.A. 1989, 86, 9193–9197.

    CAS  Article  Google Scholar 

  10. Lee J, Dull TJ, Lax 1, Schlessinger J, Ullrich A.: HER2 cytoplasmic domain generates normal mitogenic and transforming signals in a chimeric receptor. EMBO J. 1989, 8, 167–173.

    CAS  Article  Google Scholar 

  11. Lehväslaiho H, Lehtola L, Sistonen L, Alitalo K: A chimeric EGF-R -neu proto-oncogene allows EGF to regulate neu tyrosine kinase and cell transformation. EMBO J. 1989, 8, 159–166.

  12. Mead JE, Fausto N: Transforming growth factor α may be a physiological regulator of liver regeneration by means of an autocrine mechanism. Proc. Natl. Acad. Sci. U.S.A. 1989, 86, 1558–1562.

    CAS  Article  Google Scholar 

  13. Muller WJ, Sinn E, Pattengale PK, Wallace R, Leder P: Single-step induction of mammary adenocarcinoma in transgenic mice bearing the activated c-neu oncogene. Cell 1988, 54, 105–109.

    CAS  Article  Google Scholar 

  14. Rinderknecht E, Humbel RE: Polypeptides with nonsuppressible insulin-like and cell-growth promoting activities in human serum: Isolation, chemical characterization, and some biological properties of forms I and II. Proc. Natl. Acad. Sci U.S.A. 1976, 73, 2365–2369.

    CAS  Article  Google Scholar 

  15. Ross R, Raines EW, Bowen-Pope DF: The biology of platelet-derived growth factor. Cell 1986, 46, 155–169.

    CAS  Article  Google Scholar 

  16. Sastrowidjojo S, Frost AJ: Cell cultures derived from bovine ductural epithelium for the investigation of mastitis. Austr. vet. J. 1986, 63, 194.

  17. Seely JE, Pösö H, Pegg AE: Purification of ornithine decarboxylase from kidneys of androgen-treated mice. Biochemistry 1982, 21, 3394–3399.

    CAS  Article  Google Scholar 

  18. Simmen FA, Simmen CM, Reinhart G: Maternal and neonatal somatomedin C/insulin-like growth factor -I (IGF-I) and IGF binding proteins during early lactation in the pig. Dev. Biol. 1988, 130, 16–27.

    CAS  Article  Google Scholar 

  19. Slamon DJ, Clark GM, Wong SG, Levin WJ, Ullrich A, McGiure WL: Human breast cancer: Correlation of relapse and survival with amplification of the HER-2/neu oncogene. Science 1987, 325, 177–182.

    Article  Google Scholar 

  20. Smith KA: Interleukin-2. Sci. Amer. 1990, 262, 26–33.

    Article  Google Scholar 

  21. Swamp G, Speeg KV Jr, Cohen S, Garbers DL: Phosphotyrosyl-protein phosphatase of TCRC-2 cells. J. Biol. Chem. 1982, 257, 7298–7301.

    Article  Google Scholar 

  22. Tonks NK, Charbonneau H, Diltz CD, Kumar S, Cicirelli MF, Krebs EG, Walsh KA, Fischer EH: Protein tyrosine phosphatases: structure, properties and role in signal transduction. Adv. Protein Phosphatases 1989, 5, 149–180.

    CAS  Article  Google Scholar 

  23. Tucker HA: Endocrine and neural control of the mammary gland. In: Larson BL (ed.): Lactation, The Iowa State University Press, Ames, 1985. pp. 39–79.

  24. Ullrich A, Schlessinger J: Signal transduction by receptors with tyrosine kinase activity. Cell 1990, 61, 203–212.

    CAS  Article  Google Scholar 

  25. Virtanen I, Miettinen M, Lehto V-P, Kariniemi AL, Paasivuo R: Diagnostic application of monoclonal antibodies to intermediate filaments. Ann. NY. Acad. Sciences 1985, 455, 635–648.

    CAS  Article  Google Scholar 

  26. Walker LN, Bowen-Pope DF, Ross R, Reidy MA: Production of PDGF-like molecules by cultured arterial smooth muscle cells accompanies proliferation after arterial injury. Proc. Natl. Acad. Sci. U.S.A. 1986, 83, 7311–7315.

    CAS  Article  Google Scholar 

  27. Walker-Smith JA, Phillips AD, Walford N, Gregory H, Fitzgerald JD, MacCullagh K, Wright NA: Intravenous epidermal growth factor/urogastro- ne increases small intestinal cell proliferation in congenital microvillous atrophy. Lancet 1985, ii, 1239–1240.

  28. Wright NA, Pike C, Elia G: Induction of a novel epidermal growth factor -secreting cell lineage by mucosal ulceration in human gastrointestinal stem cells. Nature 1990, 343, 82–85.

    CAS  Article  Google Scholar 

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Correspondence to A. Iivanainen.

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Iivanainen, A., Hölttä, E., Ståhls, A. et al. Colostral Growth Factors. Acta Vet Scand 33, 197–203 (1992). https://doi.org/10.1186/BF03547309

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Keywords

  • colostrum
  • cell growth
  • ornithine decarboxylase