Lactoferrin induces growth arrest and nuclear accumulation of Smad-2 in HeLa cells

Biochimie

Volumn 92, Issue 7, 2010, Pages 880-884

  Zemann, Nina ^a   Klein, Petra ^a   Wetzel, Ellen ^a   Huettinger, Felix ^a   Huettinger, Manfred ^a  

^a MEDICAL UNIVERSITY OF VIENNA   (Austria)

Author keywords

Cell proliferation; HeLa cells; Lactoferrin; MAPkinases; Transforming growth factor beta

Indexed keywords

LACTOFERRIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38; SMAD2 PROTEIN; TRANSFORMING GROWTH FACTOR BETA; TRANSFORMING GROWTH FACTOR BETA1;

ARTICLE; CELL FRACTIONATION; CELL NUCLEUS; CELL PROLIFERATION; CELLULAR DISTRIBUTION; CONTROLLED STUDY; GROWTH INHIBITION; HELA CELL; HUMAN; HUMAN CELL; IMMUNOCYTOCHEMISTRY; SIGNAL TRANSDUCTION; ANIMAL; BOVINAE; DRUG EFFECTS; ENZYME ACTIVATION; HELA CELL LINE; KINETICS; METABOLISM; PROTEIN TRANSPORT;

ANIMALS; CATTLE; CELL NUCLEUS; CELL PROLIFERATION; ENZYME ACTIVATION; HELA CELLS; HUMANS; KINETICS; LACTOFERRIN; MITOGEN-ACTIVATED PROTEIN KINASE 1; MITOGEN-ACTIVATED PROTEIN KINASE 3; P38 MITOGEN-ACTIVATED PROTEIN KINASES; PROTEIN TRANSPORT; SMAD2 PROTEIN; TRANSFORMING GROWTH FACTOR BETA1;

EID: 77953544756     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.03.013     Document Type: Article

References (28)

1. Metz-Boutigue M.H., Jolles J., Mazurier J., et al. Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins. Eur. J. Biochem. 1984, 145:659-676.
2. Montreuil J., Tonnelat J., Mullet S. Preparation and properties of lactosiderophilin (lactotransferrin) of human milk. Biochim. Biophys. Acta 1960, 45:413-421.
3. Masson P.L., Heremans J.F., Schonne E. Lactoferrin, an iron-binding protein in neutrophilic leukocytes. J. Exp. Med. 1969, 130:643-658.
4. Cornish J., Callon K.E., Naot D., et al. Lactoferrin is a potent regulator of bone cell activity and increases bone formation in vivo. Endocrinology 2004, 145:4366-4374.
5. Hagiwara T., Shinoda I., Fukuwatari Y., Shimamura S. Effects of lactoferrin and its peptides on proliferation of rat intestinal epithelial cell line, IEC-18, in the presence of epidermal growth factor. Biosci. Biotechnol. Biochem. 1995, 59:1875-1881.
6. Yamada K., Ikeda I., Sugahara T., Hashizume S., Shirahata S., Murakami H. Stimulation of proliferation and immunoglobulin M production by lactoferrin in human-human and mouse-mouse hybridomas cultures in serum-free conditions. Cytotechnology 1990, 3:123-131.
7. Huang N., Bethell D., Card C., et al. Bioactive recombinant human lactoferrin, derived from rice, stimulates mammalian cell growth. In Vitro Cell. Dev. Biol.-Anim. 2008, 44:464.
8. Damiens E., El Yazidi I., Mazurier J., Duthille I., Spik G., Boilly-Marer Y. Lactoferrin inhibits G1 cyclin-dependent kinases during growth arrest of human breast carcinoma cells. J. Cell. Biochem. 1999, 74:486-498.
9. Yanhong Z., Zhaoyang Z., Wenling Z., et al. Lactotransferrin: a candidate tumor suppressor - deficient expression in human nasopharyngeal carcinoma and inhibition of NPC cell proliferation by modulating the mitogen-activated protein kinase pathway. Int. J. Cancer 2008, 123:2065-2072.
10. Oh S.-M., Pyo C.-W., Kim Y., Choi S.-Y. Neutrophil lactoferrin upregulates the human p53 gene through induction of NF-[kappa]B activation cascade. Oncogene 2004, 23:8282.
11. Haversen L., Ohlsson B.G., Hahn-Zoric M., Hanson L.A., Mattsby-Baltzer I. Lactoferrin down-regulates the LPS-induced cytokine production in monocytic cells via NF-kappa B. Cell. Immunol. 2002, 220:83-95.
12. Oh S.M., Hahm D.H., Kim I.H., Choi S.Y. Human neutrophil lactoferrin trans-activates the matrix metalloproteinase 1 gene through stress-activated MAPK signaling modules. J. Biol. Chem. 2001, 276:42575-42579.
13. Brandl N., Zemann A., Kaupe I., et al. Signal transduction and metabolism in chondrocytes is modulated by lactoferrin. Osteoarthr. Cartil. 2010, 18:117-125.
14. Massague J. TGF-beta signal transduction. Annu. Rev. Biochem. 1998, 67:753-791.
15. Shi Y., Massague J. Mechanisms of TGF-beta signaling from cell membrane to the nucleus. Cell 2003, 113:685-700.
16. Massagué J., Blain S.W., Lo R.S. TGF[beta] signaling in growth control, cancer, and heritable disorders. Cell 2000, 103:295.
17. Wrana J.L., Attisano L., Carcamo J., et al. Tgf-beta signals through a heteromeric protein-kinase receptor complex. Cell 1992, 71:1003-1014.
18. Persson U., Souchelnytskyi S., Franzén P., Miyazono K., ten Dijke P., Heldin C.-H. Transforming growth factor (TGF-β)-specific signaling by chimeric TGF-β type II receptor with intracellular domain of activin type IIB receptor. J. Biol. Chem. 1997, 272:21187-21194.
19. Holzmann J., Brandl N., Zemann A., et al. Assorted effects of TGF[beta] and chondroitinsulfate on p38 and ERK1/2 activation levels in human articular chondrocytes stimulated with LPS. Osteoarthr. Cartil. 2006, 14:519.
20. Kuhara T., Yamauchi K., Tamura Y., Okamura H. Oral administration of lactoferrin increases NK cell activity in mice via increased production of IL-18 and type I IFN in the small intestine. J. Interferon Cytokine Res. 2006, 26:489-499.
21. Grey A., Banovic T., Zhu Q., et al. The low-density lipoprotein receptor-related protein 1 is a mitogenic receptor for lactoferrin in osteoblastic cells. Mol. Endocrinol. 2004, 18:2268-2278.
22. Nicolas F.J., Hill C.S. Attenuation of the TGF-[beta]-Smad signaling pathway in pancreatic tumor cells confers resistance to TGF-[beta]-induced growth arrest. Oncogene 2003, 22:3698.
23. Suzuki Y.A., Lonnerdal B. Characterization of mammalian receptors for lactoferrin. Biochem. Cell Biol. 2002, 80:75-80.
24. Suzuki Y.A., Lopez V., Lonnerdal B. Mammalian lactoferrin receptors: structure and function. Cell. Mol. Life Sci. 2005, 62:2560-2575.
25. Legrand D., Vigie K., Said E.A., et al. Surface nucleolin participates in both the binding and endocytosis of lactoferrin in target cells. Eur. J. Biochem. 2004, 271:303-317.
26. Huettinger M., Retzek H., Hermann M., Goldenberg H. Lactoferrin specifically inhibits endocytosis of chylomicron remnants but not alpha-macroglobulin. J. Biol. Chem. 1992, 267:18551-18557.
27. Huang S.S., Ling T.Y., Tseng W.F., et al. Cellular growth inhibition by IGFBP-3 and TGF-beta1 requires LRP-1. Faseb J 2003, 17:2068-2081.
28. Tseng W.F., Huang S.S., Huang J.S. LRP-1/TbetaR-V mediates TGF-beta1-induced growth inhibition in CHO cells. FEBS Lett. 2004, 562:71-78.