Summary
Previousin situ hybridization studies from our laboratory have shown that expression of certain milk protein genes, e.g. α-lactalbumin, is very high in most parts of the mammary glands of sheep and cattle, while in other areas containing an abundance of fat globules it is virtually zero (Molenaaret al., 1992). One possible explanation is that some areas of the mammary gland are dedicated to protein synthesis and some to fat synthesis. To check this possibility, the cRNA for butyrophilin, a milk-fat globule membrane protein, and hence a putative marker of milk fat synthesis, was used as a probe inin situ hybridization studies. The results show quite clearly that the patterns of expression for this gene are similar, cell type for cell type, as those for milk protein genes such as α-lactalbumin and αs1casein. In addition, we found that butyrophilin gene expression more closely matches that of αS1casein than that of α-lactalbumin. If it is shown in the future that butyrophilin is indeed a marker for milk fat synthesis, then these results support the current assumption that fat and protein synthesis do occur in the same cell.
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References
Bargmann,W. &Knoop,A. (1959) Über die Morphologie der Milchsekretion, licht und elektronenrnikroskopische Studien an der Milchdrüse der Ratte.Z. Zellforsch. 49, 344–88.
Bargmann,W.,FleischhauerK. &Knoop,A. (1961) Über die Morphologie der Milchsekretion II. Zugleich eine Kritik amSchema der Sekretionsmorphologie.Z. Zellforsch. 53, 545–68.
Clermont,Y.,Xia,L.,Rambourg,A.,Turner,J. D. &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.Anat Rec. 235, 363–73.
Cowie,A. T. &Tindal,J. S. (eds) (1971)The Physiology of Lactation, 1st edn. London: Edward Arnold.
Erickson,J. M.,Rushford,C. L.,Dorney,D. J.,WilsonG.N. &Schmickel,R. D. (1981) Structure and variation of human ribosomal DNA: molecular analysis of cloned fragments.Gene 16, 1–9.
Franke,W. W.,Heid,H. W.,Grund,C.,Winter,S.,Freudenstein,C.,Schmid,E.,Jarasch,E. D. &Keenan,T. W. (1981) Antibodies to the major insoluble milk fat globule membrane-associated protein: specific location in apical regions of lactating epithelial cells.J. Cell Biol. 89, 485–94.
Gardinier,M. V.,Amiguet,P.,Linington,C. &Matthieu,J. M. (1992) Myelin/oligodendrocyte glycoprotein is a unique member of the immunoglobulin superfamily.J. Neurosci. Res. 33, 177–87.
Gibson,J. P. (1991) The potential for genetic change in milk fat composition.J. Dairy Sci. 74, 3258–66.
Hasan,R.,White,D. A. &Mayer,R. J. (1982) Extensive destruction of newly synthesized casein in mammary expiants in organ culture.Biochem. J. 202, 133–8.
Hurley,W. L. &Schuler,L. A. (1987) Molecular cloning and nucleotide sequence of a bovine α-lactalbumin cDNA.Gene 61, 119–22.
Jack,L. J. W. &Mather,I. H. (1990) Cloning and analysis of cDNA encoding bovine butyrophilin, an apical glycoprotein expressed in mammary tissue and secreted with the milk-fat globule membrane during lactation.J. Biol Chem. 265, 14 481–6.
Jenness,R. &Sloan,R. E. (1970) The composition of milks of various species: a review.Dairy Sci. Abstr. 32, 599–612.
Johnson,V. G. &Mather,I. H. (1985) Monoclonal antibodies prepared against PAS-1 butyrophilin and GP-55 from guinea-pig milk-fat-globule membrane bind specifically to the apical pole of secretory-epithelial cells in lactating mammary tissue.Exp. Cell. Res. 158, 144–58.
Kanno,C. (1990) Secretory membranes of the lactating mammary gland.Protoplasma 159, 184–208.
Keenan,T. W. &Dylewski,D. P. (1985) Aspects of intracellular transit of serum and lipid phases of milk.J. Dairy Sci. 68, 1025–40.
Keenan,T. W.,Saacke,R. G. &Patton,S. (1970) Prolactin, the Golgi apparatus, and milk secretion: a brief interpretive review.J Dairy Sci. 53, 1349–52.
Kuhn,N. J. (1983) The biosynthesis of lactose. InBiochemistry of Lactation (edited byMepham,T. B.), pp. 1159–76. Amsterdam: Elsevier.
Kurosumi,K.,Kobayashi,Y. &Baba,N. (1968) The fine structure of mammary glands of lactating rats, with special reference to the apocrine secretion.Exp. Cell. Res. 50, 177.
Linzell,J. L. &Peaker,M. (1971) Mechanism of milk secretion.Phys. Rev. 51, 564–97.
Mather,I. H. &Jack,L. J. W. (1993) A review of the molecular and cellular biology of butryophilin, the major protein of bovine milk fat glubule membrane.J. Dairy Sci. 76, 3832–50.
Mather,I. H. &Keenan,T. W. (1983) Functions of endomembranes and the cell surface in the secretion of organic milk constituents. InBiochemistry of Lactation (edited byMepham,T. B.), p. 231. Amsterdam: Elsevier.
Mepham,T. B. (1987)Physiolog of Lactation, pp. 82 and 155. Milton Keynes: Open University Press.
Molenaar,A. J.,Davis,S. R. &Wilkins,R. J. (1992) Expression of a-lactalbumin, aS1casein and lactoferrin genes is heterogeneous in sheep and cattle mammary tissue.J. Histochem. Cytochem. 40, 611–8.
Neville,M. C. (1990) The physiological basis of milk secretion.Annals NY Acad. Sci. 586, 1–11.
Nickerson,S. C. (1992) Anatomy and physiology of the udder. InMachine Milking and Lactation (edited byBramley,A. J. et al.), pp. 37–68. Newbury: Insight.
Nickerson,S. C. &Akers,R. M. (1984) Biochemical and ultrastructural aspects of milk synthesis and secretion.Int. J. Biochem. 16, 855–65.
Ponte,P.,Ng,S. Y.,Engel,J.,Gunning,P. &Kedes,L. (1984) Evolutionary conservation in the untranslated regions of actin mRNAs: DNA sequence of a human beta-actin cDNA.Nucl. Acids Res. 12, 1687–96.
Richardson,K. C. (1947) Some structural features of mammary tissues.Br. Med. Bull. 5, 123–9.
Saacke,R. G. &Heald,C. W. (1974) Cytological aspects of milk formation and secretion. InLactation: a Comprehensive Treatise, vol 2. (edited byLarson,B. L. &Smith,V. R.), pp. 147–89. New York: Academic Press.
Stelwagen,K.,Davis,S. R.,Farr,V. C.,Eichler,S. J. &Politis,I. (1994) Effect of once daily milking and concurrent somatotrophin on mammary tight junction permeability and yield in cows.J. Dairy Sci. 77, 2994–3001.
Stewart,A. F.,Willis,I. M. &Mackinlay,A. G. (1984) Nucleotide sequences of bovine aS1casein andk-casein cDNAs.Nucl. Acids Res. 12, 3895–907.
Wilde,C. J.,Kerr,M. A. &Calvert,D. T. (1991) Intracellular degradation of newly synthesized casein in perfused rat mammary gland.Exp. Physiol. 76, 533–7.
Witkiewicz,H.,Bolander,M. E. &Edwards,D. R. (1993) Improved design of riboprobes from pBluescript and related vectors for in situ hybridization.Biotechniques 14, 458–62.
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Molenaar, A.J., Davis, S.R., Wilkins, R.J. et al. Expression of the butyrophilin gene, a milk fat globule membrane protein, is associated with the expression of the αS1casein gene. Histochem J 27, 388–394 (1995). https://doi.org/10.1007/BF02389025
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DOI: https://doi.org/10.1007/BF02389025