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In situ generation of milk protein-derived peptides in drying-off cows

Published online by Cambridge University Press:  08 September 2010

Chin H Ho ,
Chai J Chang ,
Wen B Liu ,
Huo C Peh ,
Shuen E Chen ,
Hui Y Chen ,
Tsung H Ho ,
Ming T Chen  and
Hajime Nagahata
Chin H Ho
Affiliation:
Department of Animal Science, National Chung Hsing University, Taichung 402, TaiwanROC
Chai J Chang*
Affiliation:
Department of Animal Science, National Chung Hsing University, Taichung 402, TaiwanROC
Wen B Liu
Affiliation:
Department of Animal Science, National Chung Hsing University, Taichung 402, TaiwanROC
Huo C Peh
Affiliation:
Department of Animal Science, National Chung Hsing University, Taichung 402, TaiwanROC
Shuen E Chen
Affiliation:
Department of Animal Science, National Chung Hsing University, Taichung 402, TaiwanROC
Hui Y Chen
Affiliation:
Biotechnology Center, National Chung Hsing University, Taichung 402, Taiwan, ROC
Tsung H Ho
Affiliation:
Department of Animal Science, National Chung Hsing University, Taichung 402, TaiwanROC
Ming T Chen
Affiliation:
Department of Bioindustry Technology, Da Yeh University, Chung Hwa 555, Taiwan, ROC
Hajime Nagahata
Affiliation:
Department of Animal Health, School of Veterinary Medicine, Rakuno Gakuen University, Ebetsu, Hokkaido 069-8501, Japan
*
*For correspondence; e-mail: crchang@mail.nchu.edu.tw
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Abstract

Our previous studies demonstrated prompt elevation of proteinase activity in mammary secretion of drying-off cows and goats. The current study examined the progressive changes in composition of cow mammary secretion following drying-off and, in parallel, characterized the mode of peptide neogenesis using matrix-assisted laser desorption ionization-time-of-flight mass spectrometry (MALDI-TOF MS) and liquid chromatography-electrospray-ionization (LC-ESI) MS/MS. The results show that the percentage of casein of total milk protein at time of drying-off was 76%, which dropped to 41%, 24%, and 16%, respectively, 1, 2, and 3 weeks after drying-off. Levels of β-lactoglobulin and α-lactoalbumin in mammary secretions of drying-off cows decreased prominently while levels of lactoferrin, BSA, and casein derived-proteins increased concomitantly compared with regular milk. A fractionation procedure was applied to remove molecules larger than 10 kDa before MALDI-TOF MS and LC-ESI MS/MS and the results show that the MALDI-TOF MS peptide profile of mammary secretion ranging from m/z 600 to 4000 was apparently modified after drying-off for 1 week, whereas species 1590 m/z and 2460 m/z were most obviously enriched compared with regular milk. LC-ESI MS/MS results were used to map peptide sequence with Mascot search server and under no post translational modification to reduce database size and 202 novel β-casein-derived peptides were successfully identified in mammary secretion after drying-off for 1 week in contrast to regular milk. Accordingly at least 48 additional cleavage positions were assigned on β-casein for mammary secretion. Among the 202 novel peptides, 5 are homologous with confirmed opioid agonists, angiotensin 1-converting enzyme inhibitors, or immuno-modulators. In conclusion, peptides are released in situ from milk proteins within short intervals following drying-off in cows. They might play roles in the transition of mammary glands from lactating to non-lactating. With specified post-translational modifications and focused functional screening, novel peptides are yet to be discovered in dry cow mammary secretion.

Keywords

Bioactive peptidesMALDI-TOF MSLC-ESI MS/MSmammary secretiondry cows
Type
Research Article
Information
Journal of Dairy Research , Volume 77 , Issue 4 , November 2010 , pp. 487 - 497
Copyright
Copyright © Proprietors of Journal of Dairy Research 2010

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References

Chabance, B, Marteau, P, Rambaud, JC, Migliore-Samour, D, Boynard, M, Perrotin, P, Guillet, R, Jolles, P & Fiat, AM 1998 Casein peptide release and passage to the blood in humans during digestion of milk or yogurt. Biochimie 80 155–165CrossRefGoogle ScholarPubMed
Chen, WY, Weng, MH, Chen, SE, Peh, HC, Liu, WB, Yu, TC, Chen, MT, Naganata, H & Chang, CJ 2007 Profile of gelatinolytic capacity in raw goat milk and the implication for milk quality. Journal of Dairy Science 90 4954–4965CrossRefGoogle ScholarPubMed
Chou, WK, Yu, TC, Chen, SE, Peh, HC, Liu, WB, Chen, MT, Naganata, H & Chang, CJ 2009 TNF-α-mediated-plasminogen activation on neutrophils is involved in the high plasmin activity in mammary secretion of drying-off cows. Journal of Dairy Research 76 459–468CrossRefGoogle ScholarPubMed
Clare, DA & Swaisgood, HE 2000 Bioactive milk peptides: A prospectus. Journal of Dairy Science 83 1187–1195CrossRefGoogle ScholarPubMed
Cross, KJ, Huq, NL, Bicknell, W & Reynolds, EC 2001 Cation-dependent structural features of β-casein 1–25. Biochemical Journal 356 277–286CrossRefGoogle ScholarPubMed
Das, S, Mandal, M, Mandalm, A, Chakraborti, T & Chakraborti, S 2004 Identification, purification and characterization of matrix metalloproteinase-2 in bovine pulmonary artery smooth muscle plasma membrane. Molecular and Cell Biochemistry 258 73–89CrossRefGoogle ScholarPubMed
Delom, F & Chevet, E 2006 Phosphoprotein analysis: from proteins to proteomes. Proteome Science 4 15–26CrossRefGoogle ScholarPubMed
Eng, JK, McCormack, AL & Yates, JR 3rd 1994 An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. Journal of American Society of Mass Spectrum 5 976–989CrossRefGoogle Scholar
Ferranti, P, Traisci, MV, Picariello, G, Nasi, A, Boschi, V, Siervo, M, Falconi, C, Chianese, L & Addeo, F 2004 Casein proteolysis in human milk: tracing the pattern of casein breakdown and the formation of potential abioactive peptides. Journal of Dairy Research 71 74–87CrossRefGoogle Scholar
Fichna, J, Janecka, A, Costentin, J & Do Rego, JC 2007 The endomorphin system and its evolving neurophysiological role. Pharmacological Review 59 88–123CrossRefGoogle ScholarPubMed
Gagnaire, V, Jardin, J, Jan, G & Lortal, S 2009 Invited review: Proteomics of milk and bacteria used in fermented dairy products: from qualitative to quantitative advances. Journal of Dairy Science 92 811–825CrossRefGoogle ScholarPubMed
Hortin, G 2006 The MALDI-TOF mass spectrometric view of the plasma proteome and peptidome. Clinical Chemistry 52 1223–1237CrossRefGoogle ScholarPubMed
Hurley, MJ, Larsen, LB, Kelly, AL & McSweeney, PLH 2000 The milk acid proteinase cathepsin D: a review. International Dairy Journal 10 673–681CrossRefGoogle Scholar
Kang, JH, Toita, R, Jiang, Y, Niidome, T & Katayama, Y 2006 Simultaneous analysis of phosphorylated peptides by MALDI-TOF-MS. Chromatographia 63 595–598CrossRefGoogle Scholar
Korhonen, H & Pihlanto, A 2006 Bioactive peptides: Production and functionality. International Dairy Journal 16 945–960CrossRefGoogle Scholar
Korkmaz, B, Moreau, T & Gauthier, F 2008 Neutrophil elastase, proteinase 3 and cathepsin G: physicochemical properties, activity and physiopathological functions. Biochimie 90 227–242CrossRefGoogle ScholarPubMed
Krieger, TJ & Hook, VY 1992 Purification and characterization of a cathepsin D protease from ovine chromaffin granules. Biochemistry 31 4223–4231CrossRefGoogle Scholar
Laemmli, UK 1970 Cleavage of structural proteins during assembly of the head bacteriophage T4. Nature 227 680–685CrossRefGoogle ScholarPubMed
Leitner, G, Krifucks, O, Merin, U, Lavi, Y & Silanikove, N 2006 Interactions between bacteria type, proteolysis of casein and physico-chemical properties of bovine milk. International Dairy Journal 16 648–654CrossRefGoogle Scholar
Marco, M, Baz, A, Fernandez, C, Gonzalez, G, Hellman, U, Salinas, G & Nieto, A 2006 A relevant enzyme in granulomatous reaction, active matrix metalloproteinase-9, found in bovine Echinococcus granulosus hydatid cyst wall and fluid. Parasitological Research 100 131–139CrossRefGoogle Scholar
Meisel, H 1998 Overview on milk protein-derived peptides. International Dairy Journal 8 363–373CrossRefGoogle Scholar
Merin, U, Fleminger, G, Komanovsky, J, Silanikove, N, Bernstein, S & Leitner, G 2008 Subclinical udder infection with Streptococcus dysgalactiae impairs milk coagulation properties: the emerging role of proteose peptones. Dairy Science and Technology 88 407–419CrossRefGoogle Scholar
Mezyk-Kopee, R, Bzowska, M, Bzowska, M, Mickowska, B, Mak, P, Oitenm, J & Bereta, J 2005 Effects of elastase and cathepsin G on the levels of membrane and soluble TNF alpha. Journal of Biological Chemistry 386 801–811Google Scholar
Napoli, A, Aiello, D, Di Donna, L, Prendushi, H & Sindona, G 2007 Exploitation of endogenous protease activity in raw mastitic milk by MALDI-TOF/TOF. Analytical Chemistry 79 5941–5948CrossRefGoogle ScholarPubMed
Nielsen, SS 2002 Plasmin system and microbial proteases in milk: characteristics, roles, and relationship. Journal of Agricultural and Food Chemistry 50 6628–6634CrossRefGoogle ScholarPubMed
Opdenakker, G, Van den Steen, PE, Dubois, B, Nelissen, I, Van Coillie, E & Masure, S 2001 Gelatinase B functions as regulator and effector in leukocyte biology. Journal of Leukocyte Biology 69 851–859CrossRefGoogle ScholarPubMed
Pihlanto, A, Virtanen, T & Korhonen, H 2010 Angiotnesin 1 converting enzyme (ACE) inhibitory activity and antihypertensive effect of fermented milk. International Dairy Journal 20 3–10CrossRefGoogle Scholar
Ruzza, P, Quinteri, L, Osler, A, Calderan, A, Biondi, B & Floreani, L 2006 Fluorescent, internally quenched, peptides for exploring the pH-dependent substrate specificity of cathepsin B. Journal of Peptide Science 12 455–461CrossRefGoogle ScholarPubMed
Sandre, C, Gleizes, A, Forestier, F, Gorges-Kergot, R, Chilmonczyk, S & Leonil, J 2001 A peptide derived from vovine β-casein modulates functional properties of bone marrow-derived macrophages from germfree and human glora-associated mice. Journal of Nutrition 131 2936–2942CrossRefGoogle ScholarPubMed
Sentandreu, MA, Aubry, L & Ouali, A 2003 Purification of bovine cathepsin B: proteomic characterization the different forms and production of specific antibodies. Biochemistry and Cell Biology 81 317–326CrossRefGoogle ScholarPubMed
Shamay, A, Shapiro, F, Mabjeesh, SJ & Silanikove, N 2002 Casein-derived phosphopeptides disrupt tight junction integrity, and precipitously dry up milk secretion in goats. Life Sciences 70 2707–2719CrossRefGoogle ScholarPubMed
Shamay, A, Shapiro, F, Leitner, G & Silanikove, N 2003 Infusions of casein hydrolyzates into the mammary gland disrupt tight junction integrity and induce involution in cows. Journal of Dairy Science 86 1250–1258CrossRefGoogle ScholarPubMed
Silanikove, N, Shamay, A, Shinder, D & Moran, A 2000 Stress down regulates milk yield in cows by plasmin induced β-casein product that blocks K+ channels on the apical membranes. Life Science 67 2201–2212CrossRefGoogle ScholarPubMed
Silanikove, N, Iscovich, J & Leitner, G 2005 Therapeutic treatment with casein hydrolyzate eradicate effectively bacterial infection in treated mammary quarters in cows. Proceedings of the 4th International Mastitis Conference, IDF, Maastricht, The NetherlandsCrossRefGoogle Scholar
Silanikove, N, Merin, U & Leitner, G 2006 Physiological role of indigenous milk enzymes: an overview of an ovolving picture. International Dairy Journal 16 533–545CrossRefGoogle Scholar
Wedholm, A, Moller, HS, Lindmark-Mansson, H, Rasmussen, MD, Andren, A & Larsen, LB 2008 Identification of peptides in milk as a result of proteolysis at different levels of somatic cell counts using LC MALDI MS/MS detection. Journal of Dairy Research 75 76–83CrossRefGoogle ScholarPubMed
Weng, MH, Chang, CJ, Chen, WY, Chou, WK, Peh, HC, Huang, MC, Chen, MT & Nagahata, H 2006 Contribution of somatic cell-associated activation of plasminogen to caseinolysis within the goat mammary gland. Journal of Dairy Science 89 2025–2037CrossRefGoogle ScholarPubMed
Weng, MH, Yu, TC, Chen, SE, Peh, HC, Liu, WB, Chen, MT, Nagahata, H & Chang, CJ 2008 Regional accretion of gelatinase B in mammary gland during gradual and acute involution of dairy animals. Journal of Dairy Research 75 202–210CrossRefGoogle ScholarPubMed
Yamamoto, N, Akino, A & Takano, T 1994 Antihypertensive effect of the peptides derived from casein by an extracellular proteinase from Lactobacillus heiveticus CP790. Journal of Dairy Science 77 917–922CrossRefGoogle ScholarPubMed