- About this Journal
- Abstracting and Indexing
- Aims and Scope
- Article Processing Charges
- Articles in Press
- Author Guidelines
- Bibliographic Information
- Citations to this Journal
- Contact Information
- Editorial Board
- Editorial Workflow
- Free eTOC Alerts
- Publication Ethics
- Reviewers Acknowledgment
- Submit a Manuscript
- Subscription Information
- Table of Contents
Journal of Amino Acids
Volume 2013 (2013), Article ID 939804, 7 pages
Potential Anticarcinogenic Peptides from Bovine Milk
1Dipartimento di Scienze Farmaceutiche e Biomediche, Università degli Studi di Salerno, Via Ponte Don Melillo, 84084 Fisciano, Italy
2Dipartimento di Chimica Farmaceutica e Tossicologica, Università di Napoli “Federico II,” Via D. Montesano 49, 80131 Napoli, Italy
3Dipartimento di Biochimica e Biofisica, Seconda Università di Napoli, Via L. De Crecchio 7, 80138 Napoli, Italy
Received 21 December 2012; Accepted 28 January 2013
Academic Editor: Michele Caraglia
Copyright © 2013 Giacomo Pepe et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- I. Lopez-Exposito and I. Recio, “Protective effect of milk peptides: antibacterial and antitumor properties,” Advances in Experimental Medicine and Biology, vol. 606, pp. 271–293, 2008.
- P. W. Parodi, “A role for milk proteins and their peptides in cancer prevention,” Current Pharmaceutical Design, vol. 13, no. 8, pp. 813–828, 2007.
- A. Tellez, M. Corredig, L. Y. Brovko, and M. W. Griffiths, “Characterization of immune-active peptides obtained from milk fermented by Lactobacillus helveticus,” Journal of Dairy Research, vol. 77, no. 2, pp. 129–136, 2010.
- H. Sasaki and H. Kume, “Nutritional and physiological effects of peptides from whey: milk whey proteins/peptides, natural beneficial modulators of inflammation,” Bulletin of the International Dairy Federation, vol. 417, pp. 43–50, 2007.
- L. Sawyer, “β-lactoglobulin,” in Advanced Dairy Chemistry I, P. F. Fox and P. McSweeney, Eds., pp. 319–386, Kluwer, Amsterdam, The Netherlands, 3rd edition, 2003.
- A. Henschen, F. Lottspeich, V. Brantl, and H. Teschemacher, “Novel opioid peptides derived from casein (β-casomorphins). II. Structure of active components from bovine casein peptone,” Hoppe-Seyler's Zeitschrift fur Physiologische Chemie, vol. 360, no. 9, pp. 1217–1224, 1979.
- Z. Sun, Z. Zhang, X. Wang, R. Cade, Z. Elmir, and M. Fregly, “Relation of β-casomorphin to apnea in sudden infant death syndrome,” Peptides, vol. 24, no. 6, pp. 937–943, 2003.
- F. Jänicke, M. Schmitt, L. Pache et al., “Urokinase (uPA) and its inhibitor PAI-1 are strong and independent prognostic factors in node-negative breast cancer,” Breast Cancer Research and Treatment, vol. 24, no. 3, pp. 195–208, 1992.
- A. K. Tandon, G. M. Clark, G. C. Chamness, J. M. Chirgwin, and W. L. McGuire, “Cathepsin D and prognosis in breast cancer,” New England Journal of Medicine, vol. 322, no. 5, pp. 297–302, 1990.
- A. Hatzoglou, E. Bakogeorgou, C. Hatzoglou, P. M. Martin, and E. Castanas, “Antiproliferative and receptor binding properties of α- and β-casomorphins in the T47D human breast cancer cell line,” European Journal of Pharmacology, vol. 310, no. 2-3, pp. 217–223, 1996.
- S. Loukas, D. Varoucha, and C. Zioudrou, “Opioid activities and structures of α-casein-derived exorphins,” Biochemistry, vol. 22, no. 19, pp. 4567–4573, 1983.
- H. Teschemacher, “Opioid receptor ligands derived from food proteins,” Current Pharmaceutical Design, vol. 9, no. 16, pp. 1331–1344, 2003.
- M. Kampa, S. Loukas, A. Hatzoglou, P. Martin, P. M. Martin, and E. Castanas, “Identification of a novel opioid peptide (Tyr-Val-Pro-Phe-Pro) derived from human αs1 casein (αs1-casomorphin, and αs1-casomorphin amide),” Biochemical Journal, vol. 319, no. 3, pp. 903–908, 1996.
- C. De Simone, P. Ferranti, G. Picariello et al., “Peptides from water buffalo cheese whey induced senescence cell death via ceramide secretion in human colon adenocarcinoma cell line,” Molecular Nutrition and Food Research, vol. 55, no. 2, pp. 229–238, 2011.
- C. De Simone, G. Picariello, G. Mamone et al., “Characterisation and cytomodulatory properties of peptides from Mozzarella di Bufala Campana cheese whey,” Journal of Peptide Science, vol. 15, no. 3, pp. 251–258, 2009.
- R. Berrocal, S. Chanton, M. A. Juillerat, B. Pavillard, J. C. Scherz, and R. Jost, “Tryptic phosphopeptides from whole casein. II. Physicochemical properties related to the solubilization of calcium,” Journal of Dairy Research, vol. 56, no. 3, pp. 335–341, 1989.
- A. Zawadzki, Q. Liu, Y. Wang, A. Melander, B. Jeppsson, and H. Thorlacius, “Verapamil inhibits L-type calcium channel mediated apoptosis in human colon cancer cells,” Diseases of the Colon and Rectum, vol. 51, no. 11, pp. 1696–1702, 2008.
- S. Perego, S. Cosentino, A. Fiorilli, G. Tettamanti, and A. Ferraretto, “Casein phosphopeptides modulate proliferation and apoptosis in HT-29 cell line through their interaction with voltage-operated L-type calcium channels,” The Journal of Nutritional Biochemistry, vol. 23, no. 7, pp. 808–816, 2012.
- K. Brew, F. J. Castellino, T. C. Vanaman, and R. L. Hill, “The complete amino acid sequence of bovine alpha-lactalbumin,” Journal of Biological Chemistry, vol. 245, no. 17, pp. 4570–4582, 1970.
- P. F. Fox, “The milk protein system,” in Developments of Dairy Chemistry-4-Functional Peptides, P. F. Fox, Ed., pp. 35–45, Elsevier Applied Science Publishers, London, UK, 1989.
- J. Fast, A. K. Mossberg, H. Nilsson, C. Svanborg, M. Akke, and S. Linse, “Compact oleic acid in HAMLET,” FEBS Letters, vol. 579, no. 27, pp. 6095–6100, 2005.
- M. Svensson, J. Fast, A. K. Mossberg et al., “α-lactalbumin unfolding is not sufficient to cause apoptosis, but is required for the conversion to HAMLET (human α-lactalbumin made lethal to tumor cells),” Protein Science, vol. 12, no. 12, pp. 2794–2804, 2003.
- A. Håkansson, B. Zhivotovsky, S. Orrenius, H. Sabharwal, and C. Svanborget, “Apoptosis induced by a human milk protein,” Proceedings of the National Academy of Sciences of the United States of America, vol. 92, no. 17, pp. 8064–8068, 1995.
- E. A. Permyakov and L. J. Berliner, “α-Lactalbumin: structure and function,” FEBS Letters, vol. 473, no. 3, pp. 269–274, 2000.
- L. G. Sternhagen and J. C. Allen, “Growth rates of a human colon adenocarcinoma cell line are regulated by the milk protein alpha-lactalbumin,” Advances in Experimental Medicine and Biology, vol. 501, pp. 115–120, 2001.
- A. S. Goldman, R. M. Goldblum, and L. A. Hanson, “Anti-inflammatory systems in human milk,” in Antioxidant Nutrients and Immune Functions, A. Bendich, M. Phillips, and R. P. Tengerdy, Eds., pp. 69–76, Plenum Press, New York, NY, USA, 1990.
- D. E. W. Chatterton, G. Smithers, P. Roupas, and A. Brodkorb, “Bioactivity of β-lactoglobulin and α-lactalbumin-Technological implications for processing,” International Dairy Journal, vol. 16, no. 11, pp. 1229–1240, 2006.
- J. E. Kinsella and D. M. Whitehead, “Proteins in whey: chemical, physical, and functional properties,” Advances in Food and Nutrition Research, vol. 33, no. C, pp. 343–438, 1989.
- J. N. de Wit, “Functional properties of whey proteins,” in Developments of Dairy Chemistry-4-Functional Peptides, P. F. Fox, Ed., pp. 285–322, Elsevier Applied Science Publishers, London, UK, 1989.
- I. Laursen, P. Briand, and A. E. Lykkesfeldt, “Serum albumin as a modulator on growth of the human breast cancer cell line, MCF-7,” Anticancer Research A, vol. 10, no. 2, pp. 343–351, 1990.
- I. E. M. Bosselaers, P. W. J. R. Caessens, M. A. J. S. Van Boekel, and G. M. Alink, “Differential effects of milk proteins, BSA and soy protein on 4NQO- or MNNG-induced SCEs in V79 cells,” Food and Chemical Toxicology, vol. 32, no. 10, pp. 905–909, 1994.
- J. Hauer, W. Voetsh, and F. A. Anderer, “Identification of a mannose-acetate-specific 87-kDa receptor responsible for human NK and LAK activity,” Immunology Letters, vol. 42, no. 1-2, pp. 7–12, 1994.
- T. Zagulski, P. Lipinski, A. Zagulska, S. Broniek, and Z. Jarzabek, “Lactoferrin can protect mice against a lethal dose of Escherichia coli in experimental infection in vivo,” British Journal of Experimental Pathology, vol. 70, no. 6, pp. 697–704, 1989.
- J. He and P. Furmanski, “Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA,” Nature, vol. 373, no. 6516, pp. 721–724, 1995.
- P. E. Florian, M. Trif, R. W. Evans, and A. Roşeanu, “An overview on the antiviral activity of Lactoferrin,” Romanian Journal of Biochemistry, vol. 46, no. 2, pp. 187–197, 2009.
- M. Tomita, W. Bellamy, M. Takase, K. Yamauchi, H. Wakabayashi, and K. Kawase, “Potent antibacterial peptides generated by pepsin digestion of bovine lactoferrin,” Journal of Dairy Science, vol. 74, no. 12, pp. 4137–4142, 1991.
- W. Bellamy, M. Takase, K. Yamauchi, H. Wakabayashi, K. Kawase, and M. Tomita, “Identification of the bactericidal domain of lactoferrin,” Biochimica et Biophysica Acta, vol. 1112, no. 1-2, pp. 130–136, 1992.
- Y. C. Yoo, R. Watanabe, Y. Koike et al., “Apoptosis in human leukemic cells induced by lactoferricin, a bovine milk protein-devived peptide: involvement of reactive oxygen species,” Biochemical and Biophysical Research Communications, vol. 237, no. 3, pp. 624–628, 1997.
- L. T. Eliassen, G. Berge, B. Sveinbjørnsson, J. S. Svendsen, L. H. Vorland, and Ø. Rekdal, “Evidence for a direct antitumor mechanism of action of bovine lactoferricin,” Anticancer Research, vol. 22, no. 5, pp. 2703–2710, 2002.
- J. S. Mader, J. Salsman, D. M. Conrad, and D. W. Hoskin, “Bovine lactoferricin selectively induces apoptosis in human leukemia and carcinoma cell lines,” Molecular Cancer Therapeutics, vol. 4, no. 4, pp. 612–624, 2005.
- L. T. Eliassen, G. Berge, A. Leknessund et al., “The antimicrobial peptide, Lactoferricin B, is cytotoxic to neuroblastoma cells in vitro and inhibits xenograft growth in vivo,” International Journal of Cancer, vol. 119, no. 3, pp. 493–500, 2006.
- S. J. Furlong, J. S. Mader, and D. W. Hoskin, “Lactoferricin-induced apoptosis in estrogen-nonresponsive MDA-MB-435 breast cancer cells is enhanced by C6 ceramide or tamoxifen,” Oncology reports., vol. 15, no. 5, pp. 1385–1390, 2006.
- M. D. Burdick, A. Harris, C. J. Reid, T. Iwamura, and M. A. Hollingsworth, “Oligosaccharides expressed on MUC1 by pancreatic and colon tumor cell lines,” Journal of Biological Chemistry, vol. 272, no. 39, pp. 20202–24198, 1997.
- J. W. Dennis, “N-linked oligosaccharide processing and tumor cell biology,” Seminars in Cancer Biology, vol. 2, no. 6, pp. 411–420, 1991.
- T. Utsugi, A. J. Schroit, J. Connor, C. D. Bucana, and I. J. Fidler, “Elevated expression of phosphatidylserine in the outer membrane leaflet of human tumor cells and recognition by activated human blood monocytes,” Cancer Research, vol. 51, no. 11, pp. 3062–3066, 1991.
- I. Dobrzyńska, B. Szachowicz-Petelska, S. Sulkowski, and Z. Figaszewski, “Changes in electric charge and phospholipids composition in human colorectal cancer cells,” Molecular and Cellular Biochemistry, vol. 276, no. 1-2, pp. 113–119, 2005.
- W. H. Yoon, H. D. Park, K. Lim, and B. D. Hwang, “Effect of O-glycosylated mucin on invasion and metastasis of HM7 human colon cancer cells,” Biochemical and Biophysical Research Communications, vol. 222, no. 3, pp. 694–699, 1996.
- L. T. Eliassen, B. E. Haug, G. Berge, and Ø. Rekdal, “Enhanced antitumour activity of 15-residue bovine lactoferricin derivatives containing bulky aromatic amino acids and lipophilic N-terminal modifications,” Journal of Peptide Science, vol. 9, no. 8, pp. 510–517, 2003.
- N. Yang, M. B. Strøm, S. M. Mekonnen, J. S. Svendsen, and Ø. Rekdal, “The effects of shortening lactoferrin derived peptides against tumour cells, bacteria and normal human cells,” Journal of Peptide Science, vol. 10, no. 1, pp. 37–46, 2004.
- J. L. Gifford, H. N. Hunter, and H. J. Vogel, “Lactoferricin: a lactoferrin-derived peptide with antimicrobial, antiviral, antitumor and immunological properties,” Cellular and Molecular Life Sciences, vol. 62, no. 22, pp. 2588–2598, 2005.
- S. Riedl, B. Rinner, S. Tumer, H. Schaider, K. Lohner, and D. Zweytick, “Targeting the cancer cell membrane specifically with human lactoferricin derivatives,” Annals of Oncology, vol. 22, pp. 31–34, 2011.
- E. Staudegger, E. J. Prenner, M. Kriechbaum et al., “X-ray studies on the interaction of the antimicrobial peptide gramicidin S with microbial lipid extracts: evidence for cubic phase formation,” Biochimica et Biophysica Acta, vol. 1468, no. 1-2, pp. 213–230, 2000.
- R. Willumeit, M. Kumpugdee, S. S. Funari et al., “Structural rearrangement of model membranes by the peptide antibiotic NK-2,” Biochimica et Biophysica Acta, vol. 1669, no. 2, pp. 125–134, 2005.
- A. Hickel, S. Danner-Pongratz, H. Amenitsch et al., “Influence of antimicrobial peptides on the formation of nonlamellar lipid mesophases,” Biochimica et Biophysica Acta, vol. 1778, no. 10, pp. 2325–2333, 2008.
- D. Zweytick, S. Tumer, S. E. Blondelle, and K. Lohner, “Membrane curvature stress and antibacterial activity of lactoferricin derivatives,” Biochemical and Biophysical Research Communications, vol. 369, no. 2, pp. 395–400, 2008.
- D. Zweytick, G. Deutsch, J. Andrä et al., “Studies on Lactoferricin-derived Escherichia coli membrane-active peptides reveal differences in the mechanism of N-acylated versus nonacylated peptides,” Journal of Biological Chemistry, vol. 286, no. 24, pp. 21266–21276, 2011.
- J. S. Mader, A. Richardson, J. Salsman et al., “Bovine lactoferricin causes apoptosis in Jurkat T-leukemia cells by sequential permeabilization of the cell membrane and targeting of mitochondria,” Experimental Cell Research, vol. 313, no. 12, pp. 2634–2650, 2007.
- J. Onishi, M. K. Roy, L. R. Juneja, Y. Watanabe, and Y. Tamai, “A lactoferrin-derived peptide with cationic residues concentrated in a region of its helical structure induces necrotic cell death in a leukemic cell line (HL-60),” Journal of Peptide Science, vol. 14, no. 9, pp. 1032–1038, 2008.
- S. J. Furlong, J. S. Mader, and D. W. Hoskin, “Bovine lactoferricin induces caspase-independent apoptosis in human B-lymphoma cells and extends the survival of immune-deficient mice bearing B-lymphoma xenografts,” Experimental and Molecular Pathology, vol. 88, no. 3, pp. 371–375, 2010.
- J. S. Mader, D. Smyth, J. Marshall, and D. W. Hoskin, “Bovine lactoferricin inhibits basic fibroblast growth factor- and vascular endothelial growth factor165-induced angiogenesis by competing for heparin-like binding sites on endothelial cells,” American Journal of Pathology, vol. 169, no. 5, pp. 1753–1766, 2006.
- D. W. Hoskin and A. Ramamoorthy, “Studies on anticancer activities of antimicrobial peptides,” Biochimica et Biophysica Acta, vol. 1778, no. 2, pp. 357–375, 2008.