Abstract
Lactose plays a crucial role in controlling milk volume by inducing water toward into the mammary secretory vesicles from the mammary epithelial cell cytoplasm, thereby maintaining osmolality. In current study, we determined the expression of several lactose synthesis related genes, including glucose transporters (glucose transporter 1, glucose transporter 8, sodium-glucose cotransporter 1, sodium-glucose cotransporter 3, and sodium-glucose cotransporter 5), lactose synthases (α-lactalbumin and β1,4-galactosyltransferase), and hexokinases (hexokinase-1 and hexokinase-2) in sow mammary gland tissue at day 17 before delivery, on the 1st day of lactation and at peak lactation. The data showed that glucose transporter 1 was the dominant glucose transporter within sow mammary gland and that expression of each glucose transporter 1, sodium-glucose cotransporter 1, hexokinase-1, hexokinase-2, α-lactalbumin, and β1,4-galactosyltransferase were increased (p < 0.05) when the sows transited from late pregnancy to peak lactation. AKT1 over-expressed mammary epithelial cells were then constructed, and the results indicated that AKT1 increases (p < 0.01) the expression of hexokinase-1 and glucose transporter 1. In summary, lactose synthesis was significantly elevated with the increase of milk production and AKT1 could positively regulate lactose synthesis.
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Adam, A. C., Rubio-Texeira, M., & Polaina, J. (2004). Lactose: The milk sugar from a biotechnological perspective. Critical Reviews in Food Science and Nutrition, 44, 553–557.
Rigout, S., Lemosquet, S., van Eys, J. E., Blum, J. W., & Rulquin, H. (2002). Duodenal glucose increases glucose fluxes and lactose synthesis in grass silage-fed dairy cows. Journal of Dairy Science, 85, 595–606.
Liu, H., Zhao, K., & Liu, J. (2013). Effects of glucose availability on expression of the key genes involved in synthesis of milk fat, lactose and glucose metabolism in bovine mammary epithelial cells. PLoS One, 8, e66092.
Hansen, A. V., Strathe, A. B., Kebreab, E., France, J., & Theil, P. K. (2012). Predicting milk yield and composition in lactating sows: A Bayesian approach. Journal of Animal Science, 90, 2285–2298.
Shu, D. P., Chen, B. L., Hong, J., Liu, P. P., Hou, D. X., & Huang, X., et al. (2012). Global transcriptional profiling in porcine mammary glands from late pregnancy to peak lactation. Omics: A Journal of Integrative Biology, 16, 123–137.
Chen, F., Hao, Y., Piao, X. S., Ma, X., Wu, G. Y., & Qiao, S. Y., et al. (2011). Soybean-derived beta-conglycinin affects proteome expression in pig intestinal cells in vivo and in vitro. Journal of Animal Science, 89, 743–753.
Li, C. M., Yan, H. C., Fu, H. L., Xu, G. F., & Wang, X. Q. (2014). Molecular cloning, sequence analysis, and function of the intestinal epithelial stem cell marker Bmi1 in pig intestinal epithelial cells. Journal of Animal Science, 92, 85–94.
Threadgold, L. C., & Kuhn, N. J. (1979). Glucose-6-phosphate hydrolysis by lactating rat mammary gland. The International Journal of Biochemistry, 10, 683–685.
Kronfeld, D. S. (1982). Major metabolic determinants of milk volume, mammary efficiency, and spontaneous ketosis in dairy cows. Journal of Dairy Science, 65, 2204–2212.
Davis, S. R., & Collier, R. J. (1985). Mammary blood flow and regulation of substrate supply for milk synthesis. Journal of Dairy Science, 68, 1041–1058.
Scheepers, A., Joost, H. G., & Schurmann, A. (2004). The glucose transporter families SGLT and GLUT: Molecular basis of normal and aberrant function. Jpen-Journal of Parenteral and Enteral Nutrition, 28, 364–371.
Zhao, F. Q. (2014). Biology of glucose transport in the mammary gland. Journal of Mammary Gland Biology and Neoplasia, 19, 3–17.
Zhao, F. Q., Glimm, D. R., & Kennelly, J. J. (1993). Distribution of mammalian facilitative glucose transporter messenger RNA in bovine tissues. The International Journal of Biochemistry, 25, 1897–1903.
Alo, P. L., Visca, P., Botti, C., Galati, G. M., Sebastiani, V., & Andreano, T., et al. (2001). Immunohistochemical expression of human erythrocyte glucose transporter and fatty acid synthase in infiltrating breast carcinomas and adjacent typical/atypical hyperplastic or normal breast tissue. American Journal of Clinical Pathology, 116, 129–134.
Macheda, M. L., Williams, E. D., Best, J. D., Wlodek, M. E., & Rogers, S. (2003). Expression and localisation of GLUT1 and GLUT12 glucose transporters in the pregnant and lactating rat mammary gland. Cell and Tissue Research, 311, 91–97.
Davis, A. J., Fleet, I. R., Goode, J. A., Hamon, M. H., Walker, F. M., & Peaker, M. (1979). Changes in mammary function at the onset of lactation in the goat: Correlation with hormonal changes. The Journal of Physiology, 288, 33–44.
Nielsen, M. O., Madsen, T. G., & Hedeboe, A. M. (2001). Regulation of mammary glucose uptake in goats: Role of mammary gland supply, insulin, IGF-1 and synthetic capacity. The Journal of Dairy Research, 68, 337–349.
Ramakrishnan, B., & Qasba, P. K. (2001). Crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the beta1,4-galactosyltransferase-I. Journal of Molecular Biology, 310, 205–218.
Ramakrishnan, B., Shah, P. S., & Qasba, P. K. (2001). Alpha-Lactalbumin (LA) stimulates milk beta-1,4-galactosyltransferase I (beta 4Gal-T1) to transfer glucose from UDP-glucose to N-acetylglucosamine. Crystal structure of beta 4Gal-T1 x LA complex with UDP-Glc. The Journal of Biological Chemistry, 276, 37665–37671.
Zhao, K., Liu, H. Y., Wang, H. F., Zhou, M. M., & Liu, J. X. (2012). Effect of glucose availability on glucose transport in bovine mammary epithelial cells. Animal, 6, 488–493.
Vilotte, J. L., & Laude, H. (2002). Transgenesis applied to transmissible spongiform encephalopathies. Transgenic Research, 11, 547–564.
Maroulakou, I. G., Oemler, W., Naber, S. P., Klebba, I., Kuperwasser, C., & Tsichlis, P. N. (2008). Distinct roles of the three Akt isoforms in lactogenic differentiation and involution. Journal of Cellular Physiology, 217, 468–477.
Dillon, R. L., & Muller, W. J. (2010). Distinct biological roles for the akt family in mammary tumor progression. Cancer Research, 70, 4260–4264.
Boxer, R. B., Stairs, D. B., Dugan, K. D., Notarfrancesco, K. L., Portocarrero, C. P., & Keister, B. A., et al. (2006). Isoform-specific requirement for Akt1 in the developmental regulation of cellular metabolism during lactation. Cell Metabolism, 4, 475–490.
Chen, C. C., Boxer, R. B., Stairs, D. B., Portocarrero, C. P., Horton, R. H., & Alvarez, J. V., et al. (2010). Akt is required for Stat5 activation and mammary differentiation. Breast Cancer Research: BCR, 12, R72.
Strange, R., Metcalfe, T., Thackray, L., & Dang, M. (2001). Apoptosis in normal and neoplastic mammary gland development. Microscopy Research and Technique, 52, 171–181.
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This work was supported by the Natural Science Foundation of China (no. 31402082).
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Chen, F., Chen, B., Guan, W. et al. Metabolic Transition of Milk Lactose Synthesis and Up-regulation by AKT1 in Sows from Late Pregnancy to Lactation. Cell Biochem Biophys 75, 131–138 (2017). https://doi.org/10.1007/s12013-016-0778-x
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DOI: https://doi.org/10.1007/s12013-016-0778-x