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Isolation und Charakterisierung differenzierungsspezifischer Antigene der Milchdrüse

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Molekular- und Zellbiologie

Zusammenfassung

In diesem Kapitel stellen wir zwei Membranproteine vor, die für die Drüsenepithelzelle der laktierenden Mamma in allen daraufhin untersuchten Säugetieren charakteristisch und spezifisch sind. Als Ausgangsmaterial zur Isolation dieser Proteine dient das Sekretprodukt der Drüsenepithelzellen, die Milch. Die Hauptbestandteile der Milch — Proteine, Kohlenhydrate und Fette — werden alle von diesen Zellen synthetisiert und sezerniert. Dabei werden zwei ganz verschiedene Sekretionswege eingeschlagen, die in Abb. 1 skizziert sind: Während die typischen Milchproteine (vor allem Caseine und α-Lactalbumin) und Kohlenhydrate (vor allem Lactose) über einen Exocytose-Mechanismus via den Golgi-Apparat und sekretorische Vesikel, deren Membran mit der apikalen Plasmamembran verschmilzt, nach außen abgegeben werden (A), erfolgt die Sekretion des Milchfetts (vor allem Triglyceride) durch Abschnürung von der apikalen Zelloberflache (B). Dieser Prozeß kommt, soweit bekannt, nur bei der laktierenden Mammaepithelzelle vor; er ähnelt dem „budding“ von Viruspartikeln, jedoch ist die von der Zelloberfläche abgeschnürte Plasmamembran bei der Milchfettsekretion etwa 10 000 mal größer.

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Literatur

  • Bernardi G (1971) Chromatography of proteins on hydroxyapatite. Methods Enzymol 22:325–329

    Article  Google Scholar 

  • Bruder G, Heid H, Jarasch E-D, Keenan TW, Mather IH (1982) Characteristics of membrane-bound and soluble forms of xanthine oxidase from milk and endothelial cells of capillaries. Biochim Biophys Acta 701:357–369

    Article  PubMed  CAS  Google Scholar 

  • Bruder G, Heid HW, Jarasch E-D, Mather IH (1983) Immunological identification and determination of xanthine oxidase in cells and tissues. Differentiation 23:218–225

    Article  PubMed  CAS  Google Scholar 

  • Dingwall C, Sharnick SV, Laskey RA (1982) A Polypeptide domain that specifies migration of nucleoplasmin into the nucleus. Cell 30:449–458

    Article  PubMed  CAS  Google Scholar 

  • Fairbanks G, Steck TL, Wallach DFH (1971) Electrophoretic analysis of the major Polypeptides of the human erythrocyte membrane. Biochemistry 10:2606–2617

    Article  PubMed  CAS  Google Scholar 

  • Franke WW, Heid HW, Grund C, Winter S, Freudenstein C, Schmid E, Jarasch E-D, Keenan TW (1981) Antibodies to the major insoluble milk fat globule membrane-associated protein: Specific location in apical regions of lactating epithelial cells. J Cell Biol 89:485–494

    Article  PubMed  CAS  Google Scholar 

  • Heid HW, Winter S, Bruder G, Keenan TW, Jarasch E-D (1983) Butyrophilin, an apical plasma membrane-associated glycoprotein characteristic of lactating mammary glands of diverse species. Biochim Biophys Acta 728:228–238

    Article  PubMed  CAS  Google Scholar 

  • Herbert WJ (1978) Mineral-oil adjuvant and the immunization of laboratory animals. In: Weir DM (ed) Handbook of Experimental Immunology, Vol 3, Application of Immunological Methods. 3rd edition. Blackwell Scientific, Oxford, p A3.1

    Google Scholar 

  • Jarasch E-D, Bruder G, Keenan TW, Franke WW (1977) Redox constituents in milk fat globule membranes and rough endoplasmic reticulum from lactating mammary gland. J Cell Biol 73:223–241

    Article  PubMed  CAS  Google Scholar 

  • Jarasch E-D, Grund C, Bruder G, Heid HW, Keenan TW, Franke WW (1981) Localization of xanthine oxidase in mammary-gland epithelium and capillary endothelium. Cell 25:67–82

    Article  PubMed  CAS  Google Scholar 

  • Johnstone A, Thorpe R (1982) Immunochemistry in Practice, Blackwell Scientific Oxford, p 298

    Google Scholar 

  • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685

    Article  PubMed  CAS  Google Scholar 

  • Mather IH, Jarasch E-D, Bruder G, Heid HW, Mepham TB (1984a) Protein synthesis in lactating guinea-pig mammary tissue perfused in vitro. I. Radiolabelling of membrane and secretory proteins. Exp Cell Res 151:208–223

    Article  PubMed  CAS  Google Scholar 

  • Mather IH, Bruder G, Jarasch E-D, Heid HW, Johnson VC (1984b) Protein synthesis in lactating guinea-pig mammary tissue perfused in vitro. II. Biogenesis of milk-fat-globule membrane proteins. Exp Cell Res 151:277–282

    Article  PubMed  CAS  Google Scholar 

  • O’Farrell PH (1975) High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250:4007–4021

    PubMed  Google Scholar 

  • O’Farrell PZ, Goodman HM, O’Farrell PH (1977) High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell 12:1133–1142

    Article  PubMed  Google Scholar 

  • Roussos GG (1967) Xanthine oxidase from bovine small intestine. Methods Enzymol XII, 5-16

    Google Scholar 

  • Shapiro SZ, Young JR (1981) An immunochemical method for mRNA purification. Application to messenger RNA encoding trypanosome variable surface antigen. J Biol Chem 256:1495–1498

    PubMed  CAS  Google Scholar 

  • Switzer RC, Merril CR, Shifrin S (1979) A highly sensitive silver stain for detecting proteins and peptides in Polyacrylamide gels. Analyt Biochem 98:231–237

    Article  PubMed  CAS  Google Scholar 

  • Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of proteins from Polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci USA 76:4350–4354

    Article  PubMed  CAS  Google Scholar 

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© 1985 Springer-Verlag Berlin Heidelberg

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Jarasch, ED., Bruder, G., Heid, H. (1985). Isolation und Charakterisierung differenzierungsspezifischer Antigene der Milchdrüse. In: Blin, N., Trendelenburg, M.F., Schmidt, E.R. (eds) Molekular- und Zellbiologie. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-70100-9_3

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  • DOI: https://doi.org/10.1007/978-3-642-70100-9_3

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-540-13934-8

  • Online ISBN: 978-3-642-70100-9

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