Hostname: page-component-84b7d79bbc-lrf7s Total loading time: 0 Render date: 2024-07-25T07:38:26.034Z Has data issue: false hasContentIssue false
  • English
  • Français

Milk whey proteins in plasma of sows: variation with physiological state

Published online by Cambridge University Press:  01 June 2009

Susan C. Dodd ,
Isabel A. Forsyth ,
Hugh L. Buttle ,
Michael I. Gurr  and
Raymond R. Dils
Susan C. Dodd
Affiliation:
Endocrinology and Animal Physiology Department, Institute for Grassland and Animal Production, Hurley, Maidenhead SL6 5LR, UK Department of Nutrition, Institute of Food Research, Reading Laboratory, Shinfield, Reading RG2 9AT, UK
Isabel A. Forsyth
Affiliation:
Department of Cellular Physiology, AFRO Babraham Institute, Babraham Hall, Cambridge CB2 4AT, UK
Hugh L. Buttle
Affiliation:
Endocrinology and Animal Physiology Department, Institute for Grassland and Animal Production, Hurley, Maidenhead SL6 5LR, UK
Michael I. Gurr
Affiliation:
Department of Nutrition, Institute of Food Research, Reading Laboratory, Shinfield, Reading RG2 9AT, UK
Raymond R. Dils
Affiliation:
Department of Biochemistry and Physiology, School of Animal and Microbial Sciences, University of Reading, Whiteknights, PO Box 228, Reading RG6 2AJ, UK
Get access Rights & Permissions [Opens in a new window]

Summary

The whey proteins α-lactalbumin and βMactoglobulin have been investigated as potential markers of mammary development in sows by measuring their concentrations in plasma. The whey proteins were isolated from porcine milk by gel filtration, ion-exchange and hydrophobic interaction chromatography, characterized by several criteria and used to raise antibodies. Specific radioimmuno-assays were set up for porcine α-lactalbumin and β-lactoglobulin and validated for use in porcine blood and milk. Plasma levels of the whey proteins were measured in sows that were pregnant, suckling litters post partum, weaned abruptly at birth or were pregnant but mastectomized. Both whey proteins showed similar patterns in plasma post partum, falling from a maximum 1 d after parturition to values < 0·02% those in milk by day 4–5 post partum in suckling sows and showing a transient peak associated with early involution before declining to very low concentrations in non-suckling sows. α-Lactalbumin was first detected in the last week prepartum, rising markedly in the 3 d before parturition, correlated with rising prolactin (r = 0·986) and falling progesterone (r = –0·998). β-Lactoglobulin rose much earlier from 5 weeks prepartum, at the time when lobulo-alveolar mammary development is occurring, and correlated (r = 0·929) with oestradiol-17β. In mastectomized sows, concentrations of whey proteins in plasma were reduced by 90% or more when compared with intact animals, though following a similar pattern. This study shows that whey protein concentrations in plasma vary with physiological state and reflect aspects of the development of the mammary gland. The very different profiles for α-lactalbumin and β lactoglobulin prepartum indicate that they are differently controlled.

Type
Original Articles
Information
Journal of Dairy Research , Volume 61 , Issue 1 , February 1994 , pp. 21 - 34
Copyright
Copyright © Proprietors of Journal of Dairy Research 1994

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Akers, R. M. & Heald, C. W. 1978 Stimulatory effect of prepartum milk removal on secretory cell differentiation in the bovine mammary gland. Journal of Ultrastructure Research 63 316–322CrossRefGoogle ScholarPubMed
Bell, K., McKenzie, H. A. & Shaw, D. C. 1981 a Porcine β-lactoglobulin A and C. Occurrence, isolation and chemical properties. Molecular and Cellular Biochemistry 35 103–111CrossRefGoogle Scholar
Bell, K., McKenzie, H. A. & Shaw, D. C. 1981 b Porcine α-lactalbumin A and B. Molecular and Cellular Biochemistry 35 113–119CrossRefGoogle ScholarPubMed
Braude, R. & Mitchell, K. G. 1950 ‘Let-down’ of milk in the sow. Nature 165 937CrossRefGoogle ScholarPubMed
Buttle, H. L. 1987 Some effects of total mastectomy upon subsequent reproductive performance in sows. British Veterinary Journal 143 318–327CrossRefGoogle ScholarPubMed
Buttle, H. L. 1988 Role of the ovaries in inducing mammogenesis in pregnant pigs. Journal of Endocrinology 118 41–45CrossRefGoogle ScholarPubMed
Collet, C., Joseph, R. & Nicholas, K. 1991 A marsupial β-lactoglobulin gene: characterisation and prolactin-dependent expression. Journal of Molecular Endocrinology 6 9–16CrossRefGoogle ScholarPubMed
Conti, A., Godovac-Zimmerman, J., Pirchner, F., Liberatori, J. & Braunitzer, G. 1986 a Pig β-lactoglobulin I (Sus scrofa domestica, Artiodactyla). The primary structure of the major component. Biological Chemistry Hoppe-Seyler 367 871–878CrossRefGoogle ScholarPubMed
Conti, A., Napolitano, L., Godovac-Zimmerman, J., Liberatori, J. & Braunitzer, G. 1986 b Preparative separation of pig polymorphic beta-lactoglobulins by IPG and non-IPG. Protides of the Biological Fluids 34 907–910Google Scholar
Cross, B. A., Goodwin, R. F. W. & Silver, I. A. 1958 A histological and functional study of the mammary gland in normal and agalactie sows. Journal of Endocrinology 17 63–74CrossRefGoogle Scholar
Davies, D. T., Holt, C. & Christie, W. W. 1983 The composition of milk. In Biochemistry of Lactation, pp. 71–117 (Ed. Mepham, T. B.). Amsterdam: ElsevierGoogle Scholar
Dodd, S. C., Buttle, H. L., Forsyth, I. A. & Dils, R. R. 1989 Milk whey proteins as markers of mammary gland activity in the plasma of intact and mastectomised pregnant sows. Journal of Endocrinology 121 Supplement, Abstract 312Google Scholar
Dodd, S. C., Forsyth, I. A., Buttle, H. L., Gurr, M. I. & Dils, R. R. 1994 Hormonal induction of α-lactalbumin and β-lactoglobulin in cultured mammary expiants from pregnant pigs. Journal of Dairy Research 61 35–45CrossRefGoogle Scholar
Fleet, I. R., Goode, J. A., Hamon, M. H., Laurie, M. S., Linzell, J. L. & Peaker, M. 1975 Secretory activity of goat mammary glands during pregnancy and the onset of lactation. Journal of Physiology 251 763–773CrossRefGoogle ScholarPubMed
Forsyth, I. A., Byatt, J. C. & Iley, S. 1985 Hormone concentrations, mammary development and milk yield in goats given long-term bromocriptine treatment in pregnancy. Journal of Endocrinology 104 77–85CrossRefGoogle ScholarPubMed
Godovac-Zimmerman, J. & Braunitzer, G. 1987 Modern aspects of the primary structure and function of β-lactoglobulins. Milchwissenschaft 42 294–297Google Scholar
Hartmann, P. E. 1973 Changes in the composition and yield of the mammary secretion of cows during the initiation of lactation. Journal of Endocrinology 59 231–247CrossRefGoogle ScholarPubMed
Hartmann, P. E., Whitely, J. L. & Willcox, D. L. 1984 Lactose in plasma during lactogenesis, established lactation and weaning in sows. Journal of Physiology 347 453–463CrossRefGoogle ScholarPubMed
Hartree, E. F. 1972 Determination of protein: a modification of the Lowry method that gives a linear photometric response. Analytical Biochemistry 48 422–427CrossRefGoogle ScholarPubMed
Houdebine, L. M. & Gaye, P. 1975 Regulation of casein synthesis in the rabbit mammary gland. Titration of mRNA activity for casein under prolactin and progesterone treatments. Molecular and Cellular Endocrinology 3 37–55CrossRefGoogle ScholarPubMed
Jones, E. A. 1972 Studies on the particulate lactose synthetase of mouse mammary gland and the role of α-lactalbumin in the initiation of lactose synthesis. Biochemical Journal 126 67–78CrossRefGoogle ScholarPubMed
Kensinger, R. S., Collier, R. J., Bazer, F. W., Ducsay, C. A. & Becker, H. N. 1982 Nucleic acid, metabolic and histological changes in gilt mammary tissue during pregnancy and lactogenesis. Journal of Animal Science 54 1297–1308CrossRefGoogle ScholarPubMed
Kessler, E. & Brew, K. 1970 The whey proteins of pig's milk: isolation and characterization of a β-lactoglobulin. Biochimica et Biophysica Acta 200 449–458CrossRefGoogle ScholarPubMed
Kuhn, N. J. 1983 The biochemistry of lactogenesis. In Biochemistry of Lactation, pp. 351–379 (Ed. Mepham, T. B.). Amsterdam: ElsevierGoogle Scholar
Lindahl, L. & Vogel, H. J. 1984 Metal-ion-dependent hydrophobic-interaction chromatography of α-lactalbumins. Analytical Biochemistry 140 394–402CrossRefGoogle ScholarPubMed
Linzell, J. L. & Peaker, M. 1971 Mechanism of milk secretion. Physiological Reviews 51 564–597CrossRefGoogle ScholarPubMed
McFadden, T. B., Akers, R. M. & Kazmer, G. W. 1987 Alpha-lactalbumin in bovine serum: relationships with udder development and function. Journal of Dairy Science 70 259–264CrossRefGoogle Scholar
Mao, F. C., Bremel, R. D. & Dentine, M. R. 1991 Serum concentrations of the milk proteins α-lactalbumin and β-lactoglobulin in pregnancy and lactation: correlations with milk and fat yields in dairy cattle. Journal of Dairy Science 74 2952–2958CrossRefGoogle ScholarPubMed
Martin, R. H., Glass, M. R., Chapman, C., Wilson, G. D. & Woods, K. L. 1980 Human α-lactalbumin and hormonal factors in pregnancy and lactation. Clinical Endocrinology 13 223–230CrossRefGoogle ScholarPubMed
Martin, R. H., Glass, M. R., Chapman, C., Wilson, G. D. & Woods, K. L. 1981 Suppression by bromocriptine of the serum α-lactalbumin peak associated with human lactogencsis. Clinical Endocrinology 14 363–366CrossRefGoogle Scholar
Peaker, M. 1978 Ion and water transport in the mammary gland. In Lactation, vol. 4, The Mammary Gland, Human Lactation, Milk Synthesis, pp. 437–462 (Ed. Larson, B. L.). New York: Academic PressGoogle Scholar
Pitelka, D. R., Hamamoto, S. T., Duafala, J. G. & Nemanic, M. K. 1973 Cell contacts in the mouse mammary gland. I. Normal gland in postnatal development and the secretory cycle. Journal of Cell Biology 56 797–818CrossRefGoogle ScholarPubMed
Plaut, K. I., Kensinger, R. S., Griel, L. C. & Kavanaugh, J. F. 1989 Relationships amongst prolactin binding, prolactin concentrations in plasma and metabolic activity of the porcine mammary gland. Journal of Animal Science 67 1509–1519CrossRefGoogle Scholar
Quarfoth, G. J. & Jenness, R. 1975 isolation, composition and functional properties of α-lactalbumins from several species. Biochimica et Biophysica Acta 379 476–487CrossRefGoogle ScholarPubMed
Salacinski, P. R. P., McLean, C., Sykes, J. E. C., Clement-Jones, V. V. & Lowry, P. J. 1981 lodination of proteins, glycoproteins, and peptides using a solid-phase oxidizing agent 1,3,4,6-tetrachloro-3α,6α- diphenylglycoluril (lodogen). Analytical Biochemistry 117 136–146CrossRefGoogle Scholar
Shamay, A., Solinas, S., Pursel, V. G., Mcknight, R. A., Alexander, L., Beattie, C., Hennighausen, L. & Wall, R. J. 1991 Production of the mouse whey acidic protein in transgenic pigs during lactation. Journal of Animal Science 69 4552–4562CrossRefGoogle ScholarPubMed
Taverne, M., Bevers, M., Bradshaw, J. M. C., Dieleman, S. J., Willemse, A. H. & Porter, D. G. 1982 Plasma concentrations of prolactin, progesterone, relaxin and oestradiol-17β in sows treated with progesterone, bromocriptine or indomethacin during late pregnancy. Journal of Reproduction and Fertility 65 85–96CrossRefGoogle ScholarPubMed
Thompson, M. P., Groves, M. L., Brower, D. P., Farrell, H. M., Jenness, R. & Kotts, C. E. 1988 The calcium-dependent electrophoretic shift of α-lactalbumin, the modifier protein of galactosyl transferase. Biochemical and Biophysical Research Communications 157 944–948CrossRefGoogle ScholarPubMed
Whitacre, M. D. & Threlfall, W. R. 1981 Effects of ergocryptine on plasma prolactin, luteinizing hormone, and progesterone in the periparturient sow. American Journal of Veterinary Research 42 1538–1541Google ScholarPubMed
Wilde, C. J., Addey, C. V. P., Casey, M. J., Blatchford, D. R. & Peaker, M. 1988 Feed-back inhibition of milk secretion: the effect of a fraction of goat milk on milk yield and composition. Quarterly Journal of Experimental Physiology 73 391–397CrossRefGoogle ScholarPubMed
Willcox, D. L., Arthur, P. G., Hartmann, P. E. & Whitely, J. L. 1983 Perinatal changes in plasma oestradiol-17β, cortisol and progesterone and the initiation of lactation in sows. Australian Journal of Biological Sciences 36 173–181CrossRefGoogle ScholarPubMed