[1] H. Ichikawa, Y. Koketsu, Standard operating procedures for sows and piglets in farrowing and lactation in Japanese commercial herds., J. Vet. Med. Sci. 74 (2012) 1423–8. http://www.ncbi.nlm.nih.gov/pubmed/22785179 (accessed January 29, 2019).
[2] C. Vanderhaeghe, J. Dewulf, S. Ribbens, A. de Kruif, D. Maes, A cross-sectional study to collect risk factors associated with stillbirths in pig herds, Anim. Reprod. Sci. 118 (2010) 62–68. https://doi.org/10.1016/j.anireprosci.2009.06.012.
[3] K.R. White, D.M. Anderson, L.A. Bate, Increasing piglet survival through an improved farrowing management protocol, Can. J. Anim. Sci. 76 (1996) 491–495. https://doi.org/10.4141/cjas96-075.
[4] K. Nguyen, G. Cassar, R.M. Friendship, C. Dewey, A. Farzan, R.N. Kirkwood, D. Hodgins, An investigation of the impacts of induced parturition, birth weight, birth order, litter size, and sow parity on piglet serum concentrations of immunoglobulin G, J. Swine Heal. Prod. 21 (2013) 139–143. http://digital.library.adelaide.edu.au/dspace/handle/2440/79321 (accessed July 21, 2014).
[5] R.A. Cabrera, X. Lin, J.M. Campbell, A.J. Moeser, J. Odle, Influence of birth order, birth weight, colostrum and serum immunoglobulin G on neonatal piglet survival., J. Anim. Sci. Biotechnol. 3 (2012) 42. https://doi.org/10.1186/2049-1891-3-42.
[6] A. Foisnet, C. Farmer, C. David, H. Quesnel, Farrowing induction induces transient alterations in prolactin concentrations and colostrum composition in primiparous sows1, J. Anim. Sci. 89 (2011) 3048–3059. https://doi.org/10.2527/jas.2010-3507.
[7] J.L. Vallet, J.R. Miles, L.A. Rempel, A simple novel measure of passive transfer of maternal immunoglobulin is predictive of preweaning mortality in piglets, Vet. J. 195 (2013). https://doi.org/10.1016/j.tvjl.2012.06.009.
[8] H. Salmon, M. Berri, V. Gerdts, F. Meurens, Humoral and cellular factors of maternal immunity in swine., Dev. Comp. Immunol. 33 (2009) 384–93. https://doi.org/10.1016/j.dci.2008.07.007.
[9] E. Wagstrom, K. Yoon, J. Zimmerman, Immune components in porcine mammary secretions, Viral Immunol. 10 (2000) 153–93. http://www.ncbi.nlm.nih.gov/pubmed/1101660 (accessed July 22, 2013).
[10] C. Le Jan, A study by flow cytometry of lymphocytes in sow colostrum., Res. Vet. Sci. 57 (1994) 300–4.
[11] K. Hlavova, H. Stepanova, M. Faldyna, The phenotype and activation status of T and NK cells in porcine colostrum suggest these are central/effector memory cells, Vet. J. 202 (2014) 477–482. https://doi.org/10.1016/j.tvjl.2014.09.008.
[12] K. Nechvatalova, H. Kudlackova, L. Leva, K. Babickova, M. Faldyna, Transfer of humoral and cell-mediated immunity via colostrum in pigs, Vet. Immunol. Immunopathol. 142 (2011) 95–100. https://doi.org/10.1016/j.vetimm.2011.03.022.
[13] J.V. Sarma, P.A. Ward, The complement system, Cell Tissue Res. 343 (2011) 227–235. https://doi.org/10.1007/s00441-010-1034-0.
[14] J.H. Brock, F. Ortega, A. Piñeiro, Bactericidal and haemolytic activity of complement in bovine colostrum and serum: effect of proteolytic enzymes and ethylene glycol tetraacetic acid (EGTA)., Ann. Immunol. (Paris). 126C (1975) 439–51. http://www.ncbi.nlm.nih.gov/pubmed/813560 (accessed January 30, 2019).
[15] B. Reiter, J.H. Brock, Inhibition of Escherichia coli by Bovine Colostrum and Post-colostral Milk, (1975) 71–82.
[16] W.P. Eckblad, K.M. Hendrix, D.P. Olson, Total complement hemolytic activity of colostral whey and sera from dairy cows., Cornell Vet. 71 (1981) 54–8. http://www.ncbi.nlm.nih.gov/pubmed/7226847 (accessed January 29, 2019).
[17] H. Korhonen, E.L. Syväoja, H. Ahola-Luttila, S. Sivelä, S. Kopola, J. Husu, T.U. Kosunen, Bactericidal effect of bovine normal and immune serum, colostrum and milk against Helicobacter pylori., J. Appl. Bacteriol. 78 (1995) 655–62. http://www.ncbi.nlm.nih.gov/pubmed/7615421 (accessed September 16, 2013).
[18] B. Masschalck, C.W. Michiels, Antimicrobial Properties of Lysozyme in Relation to Foodborne Vegetative Bacteria, Crit. Rev. Microbiol. 29 (2003) 191–214. https://doi.org/10.1080/713610448.
[19] R.T. Ellison, T.J. Giehl, T.J. Giehl, Killing of gram-negative bacteria by lactoferrin and lysozyme., J. Clin. Invest. 88 (1991) 1080–91. https://doi.org/10.1172/JCI115407.
[20] W.T. Oliver, J.E. Wells, Lysozyme as an alternative to growth promoting antibiotics in swine production., J. Anim. Sci. Biotechnol. 6 (2015) 35. https://doi.org/10.1186/s40104-015-0034-z.
[21] G. Huang, X. Li, D. Lu, S. Liu, X. Suo, Q. Li, N. Li, Lysozyme improves gut performance and protects against enterotoxigenic Escherichia coli infection in neonatal piglets., Vet. Res. 49 (2018) 20. https://doi.org/10.1186/s13567-018-0511-4.
[22] S. Elahi, D.R. Thompson, J. Van Kessel, L.A. Babiuk, V. Gerdts, Protective role of passively transferred maternal cytokines against Bordetella pertussis infection in newborn piglets, Infect. Immun. 85 (2017) 1–16. https://doi.org/10.1128/IAI.01063-16.
[23] R.-J. Xu, Q.C. Doan, G.O. Regester, Detection and Characterisation of Transforming Growth Factor-Beta in Porcine Colostrum, Neonatology. 75 (1999) 59–64. https://doi.org/10.1159/000014078.
[24] K.T. Nguyen, G. Cassar, R.M. Friendship, C.E. Dewey, A. Farzan, R.N. Kirkwood, Stillbirth and preweaning mortality in litters of sows induced to farrow with supervision compared to litters of naturally farrowing sows with minimal supervision, J. Swine Heal. Prod. 19 (2011) 214–217. https://www.semanticscholar.org/paper/Stillbirth-and-preweaning-mortality-in-litters-of-Nguyen-Cassar/0c227bca081c46e1fe7dff38f7ddd4e91b6de3fb (accessed February 1, 2019).
[25] S. Tuboly, S. Bernáth, Intestinal absorption of colostral lymphoid cells in newborn animals., Adv. Exp. Med. Biol. 503 (2002) 107–14.
[26] W. Luo, F.J. Diaz, M.C. Wiltbank, Induction of mRNA for Chemokines and Chemokine Receptors by Prostaglandin F2α Is Dependent upon Stage of the Porcine Corpus Luteum and Intraluteal Progesterone, Endocrinology. 152 (2011) 2797–2805. https://doi.org/10.1210/en.2010-1247.
[27] H. Salmon, Mammary gland immunology and neonate protection in pigs. Homing of lymphocytes into the MG., Adv. Exp. Med. Biol. 480 (2000) 279–86. https://doi.org/10.1007/0-306-46832-8_32.
[28] A. Maheshwari, R.D. Christensen, D.A. Calhoun, ELR+ CXC chemokines in human milk, Cytokine. 24 (2003) 91–102. https://doi.org/10.1016/j.cyto.2003.07.002.
[29] K.M. Gautvik, M. Kriz, Effects of Prostaglandins on Prolactin and Growth Hormone Synthesis and Secretion in Cultured Rat Pituitary Cells, Endocrinology. 98 (1976) 352–358. https://doi.org/10.1210/endo-98-2-352.
[30] J.E. Väänänen, B.L.P. Tong, C.C.M. Väänänen, I.H.H. Chan, B.H. Yuen, P.C.K. Leung, Interaction of Prostaglandin F2αand Prostaglandin-E2on Progesterone Production in Human Granulosa-Luteal Cells, NeuroSignals. 10 (2001) 380–388. https://doi.org/10.1159/000046905.
[31] E. Ricciotti, G.A. Fitzgerald, Prostaglandins and inflammation, Arterioscler. Thromb. Vasc. Biol. 31 (2011) 986–1000. https://doi.org/10.1161/ATVBAHA.110.207449.
[32] A. Cabinian, D. Sinsimer, M. Tang, O. Zumba, H. Mehta, A. Toma, D. Sant’Angelo, Y. Laouar, A. Laouar, Transfer of Maternal Immune Cells by Breastfeeding: Maternal Cytotoxic T Lymphocytes Present in Breast Milk Localize in the Peyer’s Patches of the Nursed Infant, PLoS One. 11 (2016) e0156762. https://doi.org/10.1371/journal.pone.0156762.
[33] S. Maye, Title Investigation of the presence and activity of the innate immune component, Complement, in bovine milk, University College Cork, 2016. http://hdl.handle.net/10468/3510 (accessed May 7, 2020).
[34] R. Sakai, E. Kitano, M. Hatanaka, P. Lo, R. Matsuura, K. Deguchi, H. Eguchi, A. Maeda, M. Watanabe, H. Matsunari, H. Nagashima, H. Okuyama, S. Miyagawa, Studies of Pig Complement: Measurement of Pig CH50, ACH50, and Components, Transplant. Proc. 48 (2016) 1282–1284. https://doi.org/10.1016/j.transproceed.2015.10.066.
[35] H.D. Guthrie, C.E. Rexroad, Blockade of Luteal Prostaglandin F Release in vitro During Cloprostenol-Induced Luteolysis in the Pig, Biol. Reprod. 23 (1980) 358–362. https://doi.org/10.1095/biolreprod23.2.358.
[36] R.M. Roberts, F.W. Bazer, N. Baldwin, W.E. Pollard, Progesterone induction of lysozyme and peptidase activities in the porcine uterus, Arch. Biochem. Biophys. 177 (1976) 499–507. https://doi.org/10.1016/0003-9861(76)90461-6.
[37] J. Brenmoehl, D. Ohde, E. Wirthgen, Cytokines in milk and the role of TGF-beta, Best Pract. Res. Clin. Endocrinol. Metab. 32 (2018) 47–56. https://doi.org/10.1016/J.BEEM.2018.01.006.
[38] B.M. Fischer, T.M. Krunkosky, D.T. Wright, M. Dolan-O’Keefe, K.B. Adler, Tumor Necrosis Factor-Alpha (TNF-α) Stimulates Mucin Secretion and Gene Expression in Airway Epithelium In Vitro, Chest. 107 (1995) 133S-135S. https://doi.org/10.1378/CHEST.107.3_SUPPLEMENT.133S.
[39] R. Garofalo, Cytokines in human milk., J. Pediatr. 156 (2010) S36-40. https://doi.org/10.1016/j.jpeds.2009.11.019.
[40] J.M. Wells, O. Rossi, M. Meijerink, P. van Baarlen, Epithelial crosstalk at the microbiota–mucosal interface, Proc. Natl. Acad. Sci. 108 (2011) 4607–4614. https://doi.org/10.1073/PNAS.1000092107.
[41] J. Ogawa, A. Sasahara, T. Yoshida, M.M. Sira, T. Futatani, H. Kanegane, T. Miyawaki, Role of transforming growth factor-β in breast milk for initiation of IgA production in newborn infants, Early Hum. Dev. 77 (2004) 67–75. https://doi.org/10.1016/J.EARLHUMDEV.2004.01.005.
[42] I.R. Tizard, Veterinary immunology : an introduction, Saunders, 2004.
[43] M.T. Chiriac, B. Buchen, A. Wandersee, G. Hundorfean, C. Günther, Y. Bourjau, S.E. Doyle, B. Frey, A.B. Ekici, C. Büttner, B. Weigmann, R. Atreya, S. Wirtz, C. Becker, J. Siebler, M.F. Neurath, Activation of Epithelial Signal Transducer and Activator of Transcription 1 by Interleukin 28 Controls Mucosal Healing in Mice With Colitis and Is Increased in Mucosa of Patients With Inflammatory Bowel Disease, Gastroenterology. 153 (2017) 123-138.e8. https://doi.org/10.1053/j.gastro.2017.03.015.
[44] C. Andrews, M.H. McLean, S.K. Durum, Cytokine Tuning of Intestinal Epithelial Function., Front. Immunol. 9 (2018) 1270. https://doi.org/10.3389/fimmu.2018.01270.
[45] I.P. Oswald, Role of intestinal epithelial cells in the innate immune defence of the pig intestine, Vet. Res. 37 (2006) 359–368. https://doi.org/10.1051/vetres:2006006.
[46] M. Sinkora, J. Sinkorova, W. Holtmeier, Development of gammadelta thymocyte subsets during prenatal and postnatal ontogeny., Immunology. 115 (2005) 544–55. https://doi.org/10.1111/j.1365-2567.2005.02194.x.
[47] T. Poisot, A. Simková, P. Hyrsl, S. Morand, Interactions between immunocompetence, somatic condition and parasitism in the chub Leuciscus cephalus in early spring., J. Fish Biol. 75 (2009) 1667–82. https://doi.org/10.1111/j.1095-8649.2009.02400.x.
[48] M. Virta, M. Karp, S. Rönnemaa, E.-M. Lilius, Kinetic measurement of the membranolytic activity of serum complement using bioluminescent bacteria, J. Immunol. Methods. 201 (1997) 215–221. https://doi.org/10.1016/S0022-1759(96)00225-6.
[49] S. Nikoskelainen, J. Lehtinen, E.-M. Lilius, Bacteriolytic activity of rainbow trout (Oncorhynchus mykiss) complement, Dev. Comp. Immunol. 26 (2002) 797–804. https://doi.org/10.1016/S0145-305X(02)00032-0.
[50] M.K. Kilpi, J.T. Atosuo, E.-M.E. Lilius, Bacteriolytic activity of the alternative pathway of complement differs kinetically from the classical pathway., Dev. Comp. Immunol. 33 (2009) 1102–10. https://doi.org/10.1016/j.dci.2009.06.007.
[51] J. Atosuo, J. Lehtinen, L. Vojtek, E.-M. Lilius, Escherichia coli K-12 (pEGFPluxABCDEamp): a tool for analysis of bacterial killing by antibacterial agents and human complement activities on a real-time basis., Luminescence. 28 (2013) 771–9. https://doi.org/10.1002/bio.2435.
[52] S. Buchtikova, A. Simkova, K. Rohlenova, M. Flajshans, A. Lojek, E.-M. Lilius, P. Hyrsl, The seasonal changes in innate immunity of the common carp (Cyprinus carpio), Aquaculture. 318 (2011) 169–175. https://doi.org/10.1016/j.aquaculture.2011.05.013.