Caron, A., Richard, D., and Laplante, M.: The roles of mTOR complexes in lipid metabolism, Annu. Rev. Nutr., 35, 321–348, https://doi.org/10.1146/annurev-nutr-071714-034355, 2015.
Carreño, D., Hervás, G., Toral, P. G., Castro-Carrera, T., and Frutos, P.: Fish oil-induced milk fat depression and associated downregulation of mammary lipogenic genes in dairy ewes, J. Dairy Sci., 99, 7971–7981, https://doi.org/10.3168/jds.2016-11019, 2016.
Chatchatee, P., Järvinen, K. M., Bardina, L., Vila, L., Beyer, K., and Sampson, H. A.: Identification of IgE and IgG binding epitopes on
β-and
κ-casein in cow's milk allergic patients, Clin. Exp. Allergy, 31, 1256–1262, https://doi.org/10.1046/j.1365-2222.2001.01167.x, 2001.
Fan, X., Qiu, L., Teng, X., Zhang, Y., and Miao, Y.: Effect of INSIG1 on the milk fat synthesis of buffalo mammary epithelial cells, J. Dairy Res., 87, 349–355, https://doi.org/10.1017/S0022029920000710, 2020.
Gang, X., Yang, Y., Zhong, J., Jiang, K., Pan, Y., Karnes, R. J., Zhang, J., Xu, W., Wang, G., and Huang, H.: P300 acetyltransferase regulates fatty acid synthase expression, lipid metabolism and prostate cancer growth, Oncotarget, 7, 15135–15149, https://doi.org/10.18632/oncotarget.7715, 2016.
Ghosh, A., Stewart, D., and Matlashewski, G.: Regulation of human p53 activity and cell localization by alternative splicing, Mol. Cell. Biol., 24, 7987–7997, https://doi.org/10.1128/MCB.24.18.7987-7997.2004, 2004.
Ghosh, H. S., McBurney, M., and Robbins, P. D.: SIRT1 negatively regulates the mammalian target of rapamycin, PLOS One, 5, 9199–9206, https://doi.org/10.1371/journal.pone.0009199, 2010.
Goldstein, I. and Rotter, V.: Regulation of lipid metabolism by p53-fighting two villains with one sword, Trends Endocrin. Met., 23, 567–575, https://doi.org/10.1016/j.tem.2012.06.007, 2012.
Hall, T. A.: BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT, Nucl. Acid. S., 41, 95–98, 1999.
Hallenborg, P., Feddersen, S., Francoz, S., Murano, I., Sundekilde, U., Petersen, R. K., Akimov, V., Olson, M. V., Lozano, G., Cinti, S., Gjertsen, B. T., Madsen, L., Marine, J. C., Blagoev, B., and Kristiansen, K.: Mdm2 controls CREB-dependent transactivation and initiation of adipocyte differentiation, Cell Death Differ., 19, 1381–1389, https://doi.org/10.1038/cdd.2012.15, 2012.
Hayashi, A. A., Nones, K., Roy, N. C., McNabb, W. C., Mackenzie, D. S., Pacheco, D., and McCoard, S.: Initiation and elongation steps of mRNA translation are involved in the increase in milk protein yield caused by growth hormone administration during lactation, J. Dairy Sci., 92, 1889–1899, https://doi.org/10.3168/jds.2008-1334, 2009.
Huang, J., Guesthier, M. A., and Burgos, S. A.: AMP-activated protein kinase controls lipid and lactose synthesis in bovine mammary epithelial cells, J. Dairy Sci., 103, 340–351, https://doi.org/10.3168/jds.2019-16343, 2020.
Horton, L. E., Bushell, M., Barth-Baus, D., Tilleray, V. J., Clemens, M. J., and Hensold, J.: p53 activation results in rapid dephosphorylation of the eIF4E-binding protein 4E-BP1, inhibition of ribosomal protein S6 kinase and inhibition of translation initiation, Oncogene, 21, 5325–5334, https://doi.org/10.1038/sj.onc.1205662, 2002.
Jerry, D. J., Kuperwasser, C., Downing, S. R., Pinkas, J., He, C., Dickinson, E., Marconi S, and Naber, S. P.: Delayed involution of the mammary epithelium in BALB/c-p53null mice, Oncogene, 17, 2305–2312, https://doi.org/10.1038/sj.onc.1202157, 1998.
Kaelin, W. G.: The p53 gene family, Oncogene, 18, 7701–7705, https://doi.org/10.1038/sj.onc.1202955, 1999.
Kamada, R., Toguchi, Y., Nomura, T., Imagawa, T., and Sakaguchi, K.: Tetramer formation of tumor suppressor protein p53: structure, function, and applications, Biopolymers, 106, 598–612, https://doi.org/10.1002/bip.22772, 2016.
Khalil, H. S., Tummala, H., Chakarov, S., Zhelev, N., and Lane, D. P.: Targeting ATM pathway for therapeutic intervention in cancer, Biodiscovery, 1, 185–208, https://doi.org/10.7750/Biodiscovery.2012.1.3, 2012.
Kruse, J. P. and Gu, W.: SnapShot: p53 posttranslational modifications, Cell, 133, 930–930, https://doi.org/10.1016/j.cell.2008.05.020, 2008.
Kumar, S., Stecher, G., and Tamura, K.: MEGA7: molecular evolutionary genetics analysis version 7.0 for bigger datasets, Mol. Biol. Evol., 33, 1870–1874, https://doi.org/10.1093/molbev/msw054, 2016.
Lane, D. P.: p53, guardian of the genome, Nature, 362, 15–16, https://doi.org/10.1038/358015a0, 1992.
Larkin, M. A., Blackshields, G., Brown, N. P., Chenna, R., McGettigan, P. A., McWilliam, H., Valentin, F., Wallace, I. M., Wilm, A., Lopez, R., Thompson, J. D., Gibson, T. J., and Higgins, D. G.: Clustal W and Clustal X version 2.0, Bioinformatics, 23, 2947–2948, https://doi.org/10.1093/bioinformatics/btm404, 2007.
Leblanc, V. and May, P.: Activation and post-translational modifications of p53 following DNA damage, Med. Sci., 18, 577–584, https://doi.org/10.1051/medsci/2002185577, 2002.
Levine, A. J. and Oren, M.: The first 30 years of p53: growing ever more complex, 9, 49–758, Nat. Rev. Cancer, 9, 49–758, https://doi.org/10.1038/nrc2723, 2009.
Li, B., Greenberg, N., Stephens, L. C., Meyn, R., Medina, D., and Rosen, J. M.: Preferential overexpression of a 172 Arg
→Leu mutant p53 in the mammary gland of transgenic mice results in altered lobuloalveolar development, Cell Growth Differ., 5, 711–721, 1994.
Li, H., Liu, X., Wang, Z., Lin, X., Yan, Z., Cao, Q., Zhao, M., and Shi, K.: MEN1/Menin regulates milk protein synthesis through mTOR signaling in mammary epithelial cells, Sci. Rep., 7, 5479–5487, https://doi.org/10.1038/s41598-017-06054-w, 2017.
Liu, L., Lin, Y., Liu, L., Wang, L., Bian, Y., Gao, X., and Li, Q.: Regulation of peroxisome proliferator-activated receptor gamma on milk fat synthesis in dairy cow mammar
y epithelial cells, In. Vitro. Cell. Dev.-An., 52, 1044–1059, https://doi.org/10.1007/s11626-016-0059-4, 2016.
Marijn, T. V., Jaarsveld, D., Deng, E. A., and Wiemer, Z. Z.: Tissue-specific chk1 activation determines apoptosis by regulating the balance of p53 and p21, Iscience, 12, 27–40, https://doi.org/10.1016/j.isci.2019.01.001, 2019.
Nasr, M., Awad, A., and El Araby, I. E.: Associations of leptin and pituitary-specific transcription factor genes' polymorphisms with reproduction and production traits in dairy buffalo, Reprod. Domest. Anim., 51, 597–603, https://doi.org/10.1111/rda.12726, 2016.
Nguyen, T. A., Menendez, D., Resnick, M. A., and Anderson, C. W.: Mutant TP53 posttranslational modifications: challenges and opportunities, Hum. Mutat., 35, 738–755, https://doi.org/10.1002/humu.22506, 2014.
Okita, N., Ishikawa, N., Mizunoe, Y., Oku, M., Nagai, W., Suzuki, Y., Matsushima, S., Mikami, K., Okado, H., Sasaki, T., and Higami, Y.: Inhibitory effect of p53 on mitochondrial content and function during adipogenesis, Biochem. Bioph. Res. Co., 446, 91–97, https://doi.org/10.1016/j.bbrc.2014.02.059, 2014.
Purushotham, A., Schug, T. T., Xu, Q., Surapureddi, S., Guo, X., and Li, X.: Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation, Cell Metab., 9, 327–338, https://doi.org/10.1016/j.cmet.2009.02.006, 2009.
Raj, N. and Attardi, L. D.: The transactivation domains of the p53 protein, CSH Perspect. Med., 7, 26047–26064, https://doi.org/10.1101/cshperspect.a026047, 2017.
Rius, A. G., Appuhamy, J., Cyriac, J., Kirovski, D., Becvar, O., Escobar, J., McGilliard, M. L., Bequette, B. J., Akers, R. M., and Hanigan, M., D.: Regulation of protein synthesis in mammary glands of lactating dairy cows by starch and amino acids, J. Dairy Sci., 93, 3114–3127, https://doi.org/10.3168/jds.2009-2743, 2010.
Sambrock, J. and Russell, D.: Molecular cloning: A laboratory Manual, 3rd Edn., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 2001.
Schmid, P., Lorenz, A., Hameister, H., and Montenarh, M.: Expression of p53 during mouse embryogenesis, Dev. Brain Res., 113, 857–865, https://doi.org/10.1242/dev.113.3.857, 1991.
Shi, D. S., Wang, J., Yang, Y., Lu F. H., Li, X. P., and Liu, Q. Y.: DGAT1, GH, GHR, PRL and PRLR polymorphism in water buffalo (Bubalus bubalis), Reprod. Domest. Anim., 47, 328–334, https://doi.org/10.1111/j.1439-0531.2011.01876.x, 2012.
Singh, M., Aggarwal, S., Mohanty, A. K., and Mukhopadhyay, T.: Isolation, characterization and functional analysis of full length p53 cDNA from Bubalus bubalis, Gene, 568, 146–154, https://doi.org/10.1016/j.gene.2015.05.047, 2015.
Smith, T. M., Gilliland, K., Clawson, G. A., and Thiboutot, D.: IGF-1 induces SREBP-1 expression and lipogenesis in SEB-1 sebocytes via activation of the phosphoinositide 3-Kinase/Akt pathway, J. Invest. Dermatol., 128, 1286–1293, https://doi.org/10.1038/sj.jid.5701155, 2008.
Takasaki, M., Honma, T., Yanaka, M., Sato, K., Shinohara, N., Ito, J., Tanaka, Y., Tsuduki, T., and Ikeda, I.: Continuous intake of a high-fat diet beyond one generation promotes lipid accumulation in liver and white adipose tissue of female mice, J. Nutr. Biochem., 23, 640–645, https://doi.org/10.1016/j.jnutbio.2011.03.008, 2012.
Tilleray, V., Constantinou, C., and Clemens, M. J.: Regulation of protein synthesis by inducible wild-type p53 in human lung carcinoma cells, FEBS Lett., 580, 1766–1770, https://doi.org/10.1016/j.febslet.2006.02.030, 2006.
Vogelstein, B., Lane, D., and Levine, A. J.: Surfing the p53 network, Nature, 408, 307–310, https://doi.org/10.1038/35042675, 2000.
Wang, H. C., Ko, Y. H., Mersmann, H. J., Chen, C. L., and Ding, S. T.: The expression of genes related to adipocyte differentiation in pigs, J. Anim. Sci., 84, 1059–1066, https://doi.org/10.2527/2006.8451059x, 2006.
Wang, X. and Proud, C. G.: The mTOR pathway in the control of protein synthesis, Physiology, 21, 362–369, https://doi.org/10.1152/physiol.00024.2006, 2006.
Yahagi, N., Shimano, H., Matsuzaka, T., Najima, Y., Sekiya, M., Nakagawa, Y., Ide, T., Tomita, S., Okazaki, H., Tamura, Y., Iizuka, Y., Ohashi, K., Gotoda, T., Nagai, R., Kimura. S., Ishibashi, S., Osuga, J., and Yamada, N.: p53 Activation in adipocytes of obese mice, J. Biol. Chem., 278, 25395–25400, https://doi.org/10.1074/jbc.M302364200, 2003.
Yang, D. Q. and Kastan, M. B.: Participation of ATM in insulin signaling through phosphorylation of eIF-4E-binding protein 1, Nat. Cell Biol., 2, 893–898, https://doi.org/10.1038/35046542, 2000.
Yoshida, K., Liu, H., and Miki, Y.: Protein kinase C
δ regulates Ser46 phosphorylation of p53 tumor suppressor in the apoptotic response to DNA damage, J. Biol. Chem., 281, 5734–5740, https://doi.org/10.1074/jbc.M512074200, 2006.
Zhang, X., Qin, Z., and Wang, J.: The role of p53 in cell metabolism, Acta Pharm. Sinic., 31, 1208–1212, https://doi.org/10.1038/aps.2010.151, 2010.