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Lipid-deprived diet perturbs O-glycosylation of secretory proteins in rat mammary epithelial cells

Published online by Cambridge University Press:  01 April 2008

F. Lavialle  and
E. Chanat
F. Lavialle
Affiliation:
INRA, U1196 Génomique et Physiologie de la Lactation, Domaine de Vilvert, F-78352 Jouy-en-Josas Cedex, France
E. Chanat*
Affiliation:
INRA, U1196 Génomique et Physiologie de la Lactation, Domaine de Vilvert, F-78352 Jouy-en-Josas Cedex, France
*
E-mail: [email protected]
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Abstract

Nutrition modulates both production and composition of milk. Milk composition was studied in rats chronically fed a diet without additional lipids, and therefore eating only traces of the recommended supply of essential polyunsaturated fatty acid. Despite a large decrease in milk-protein synthesis, only protein composition, but not protein concentration, was found to change in the milk of rats following a lipid-deprived diet. Correlatively, we observed a substantial increase in the lactose concentration of milk. Analysis of milk proteins by two-dimensional electrophoresis demonstrated that the relative proportion of the various molecular forms of κ-casein, an O-glycosylated protein, was modified in the milk of rats receiving the lipid-deprived diet. In tissues, differences in the two-dimensional pattern of κ-casein between control and lipid-deprived rats were similar, if not identical. In contrast to κ-casein, the molecular forms of α-lactalbumin, an N-glycosylated protein, were not affected by the diet. These data provide evidence that O-glycosylation of milk proteins in the secretory pathway of mammary epithelial cells is modulated by the lipid content of experimental diets.

Keywords

epithelial cellslipidsmilk proteinnutritionprotein glycosylation
Type
Full Paper
Information
animal , Volume 2 , Issue 4 , April 2008 , pp. 491 - 499
Copyright
Copyright © The Animal Consortium 2008

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References

Bergmeyer, HU 1984. Lactose and D-galactose. In Methods of enzymatic analysis (ed. HO, Beutler), pp. 104–112. Verlag Chemie, Weinheim, Deerfield beach/Florida, Basel.Google Scholar
Boisgard, R, Chanat, E 2000. Phospholipase D-dependent and -independent mechanisms are involved in milk protein secretion in rabbit mammary epithelial cells. Biochimica et Biophysica Acta 1495, 281–296.Google Scholar
Boisgard, R, Chanat, E, Lavialle, F, Pauloin, A, Ollivier-Bousquet, M 2000. Roads taken by milk proteins in mammary epithelial cells. Livestock Production Science 70, 49–61.Google Scholar
Bouguyon, E, Beauvallet, C, Huet, JC, Chanat, E 2006. Disulphide bonds in casein micelle from milk. Biochemical and Biophysical Research Communications 343, 450–458.Google Scholar
Brew, K, Hill, RL 1975. Lactose biosynthesis. Reviews of Physiology, Biochemistry and Pharmacology 72, 105–158.Google Scholar
Burgoyne, RD, Duncan, JS 1998. Secretion of milk proteins. Journal of Mammary Gland Biology and Neoplasia 3, 275–286.Google Scholar
Chanat, E 2006. Sulphated proteins secreted by rat mammary epithelial cells. Reproduction Nutrition Development 46, 557–566.Google Scholar
Clermont, Y, Xia, L, Rambourg, A, Turner, JD, Hermo, L 1993. Transport of casein submicelles and formation of secretion granules in the Golgi apparatus of epithelial cells of the lactating mammary gland of the rat. The Anatomical Record 235, 363–373.Google Scholar
De Matteis, MA, Godi, A 2004. PI-loting membrane traffic. Nature Cell Biology 6, 487–492.Google Scholar
Farsad, K, De Camilli, P 2003. Mechanisms of membrane deformation. Current Opinion in Cell Biology 15, 372–381.Google Scholar
Gazdag, AC, Wetter, TJ, Davidson, RT, Robinson, KA, Buse, MG, Yee, AJ, Turcotte, LP, Cartee, GD 2000. Lower calorie intake enhances muscle insulin action and reduces hexosamine levels. American Journal of Physiology, Regulatory, Integrative and Comparative Physiology 278, R504–R512.Google Scholar
Holland, JW, Deeth, HC, Alewood, PF 2005. Analysis of O-glycosylation site occupancy in bovine kappa-casein glycoforms separated by two-dimensional gel electrophoresis. Proteomics 5, 990–1002.Google Scholar
Holt, C 1983. Swelling of Golgi vesicles in mammary secretory cells and its relation to the yield and quantitative composition of milk. Journal of Theoretical Biology 101, 247–261.Google Scholar
Jost, B, Vilotte, JL, Duluc, I, Rodeau, JL, Freund, JN 1999. Production of low-lactose milk by ectopic expression of intestinal lactase in the mouse mammary gland. Nature Biotechnology 17, 160–164.CrossRefGoogle ScholarPubMed
Kuhn, NJ, Carrick, DT, Wilde, CJ 1980. Lactose synthesis: the possibilities of regulation. Journal of Dairy Science 63, 328–336.Google Scholar
Lkhider, M, Petridou, B, Aubourg, A, Ollivier-Bousquet, M 2001. Prolactin signalling to milk protein secretion but not to gene expression depends on the integrity of the Golgi region. Journal of Cell Science 114, 1883–1891.Google Scholar
Mamone, G, Caira, S, Garro, G, Nicolai, A, Ferranti, P, Picariello, G, Malorni, A, Chianese, L, Addeo, F 2003. Casein phosphoproteome: identification of phosphoproteins by combined mass spectrometry and two-dimensional gel electrophoresis. Electrophoresis 24, 2824–2837.CrossRefGoogle ScholarPubMed
Ollivier-Bousquet, M, Kann, G, Durand, G 1993. Prolactin transit through mammary epithelial cells and appearance in milk. Endocrine Regulations 27, 115–124.Google ScholarPubMed
Ollivier-Bousquet, M, Lavialle, F, Guesnet, P, Rainteau, D, Durand, G 1997. Lipid-depleted diet perturbs membrane composition and intracellular transport in lactating mammary cells. Journal of Lipid Research 38, 913–925.Google Scholar
Pechoux, C, Boisgard, R, Chanat, E, Lavialle, F 2005. Ca(2+)-independent phospholipase A2 participates in the vesicular transport of milk proteins. Biochimica et Biophysica Acta 1743, 317–329.Google Scholar
Rudolph, MC, McManaman, JL, Phang, T, Russell, T, Kominsky, DJ, Serkova, NJ, Stein, T, Anderson, SM, Neville, MC 2007. Metabolic regulation in the lactating mammary gland: a lipid synthesizing machine. Physiological Genomics 28, 323–336.Google Scholar
Sasaki, M, Eigel, WN, Keenan, TW 1978. Lactose and major milk proteins are present in secretory vesicle-rich fractions from lactating mammary gland. Proceedings of the National Academy of Sciences at the United States of America 75, 5020–5024.Google Scholar
Seddiki, T, Delpal, S, Aubourg, A, Durand, G, Ollivier-Bousquet, M 2002. Endocytic prolactin routes to the secretory pathway in lactating mammary epithelial cells. Biology of Cell 94, 173–185.Google Scholar
Stinnakre, M-G, Vilotte, JL, Soulier, S, Mercier, J-C 1994. Creation and phenotypic analysis of α-lactalbumin-deficient mice. Proceedings of the National Academy of Sciences of the United States of America 91, 6544–6548.Google Scholar
Swaisgood, HE 2003. Chemistry of the caseins. In Advanced dairy chemistry (ed. PF, FoxPLH, McSweeney), pp. 139–201. Kluwer Academic/Plenum Publishesrs.Google Scholar
Turner, MD, Handel, SE, Wilde, CJ, Burgoyne, RD 1993. Differential effect of brefeldin A on phosphorylation of the caseins in lactating mouse mammary epithelial cells. Journal of Cell Science 106, 1221–1226.Google Scholar
Van Meer, G, Sprong, H 2004. Membrane lipids and vesicular traffic. Current Opinion in Cell Biology 16, 373–378.Google Scholar
Wells, L, Vosseller, K, Hart, GW 2003. A role for N-acetylglucosamine as a nutrient sensor and mediator of insulin resistance. Cell and Molecular Life Sciences 60, 222–228.Google Scholar
Wetter, TJ, Gazdag, AC, Dean, DJ, Cartee, GD 1999. Effect of calorie restriction on in vivo glucose metabolism by individual tissues in rats. The American Journal of Physiology 276, E728–E738.Google Scholar
Zachara, NE, Hart, GW 2004. O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress. Biochimica et Biophysica Acta 1673, 13–28.Google Scholar