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Heparin-Binding Proteins in Purified Plasma Membranes of Bovine Granulosa Cells

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Growth Factors and the Ovary
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Abstract

During follicular development, granulosa cells produce glycosaminoglycans (GAGs) as constituents which are secreted into follicular fluid (1). GAGs stimulate appearance of gonadotropin receptors on granulosa cells cultured in vitro (2). Conversely, follicular GAGs inhibit gonadotropin binding to cell surface receptors (2,3). They inhibit progesterone secretion (4,5) and may inhibit steroidogenesis indirectly by altering the binding and degradation of lipoproteins (4).

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References

  1. Ax RL, Bellin ME, Grimek HJ. Properties and synthesis of glycosaminoglycans by the ovary. In: Toft DO, Ryan RJ, eds. Proceedings of the 5th Ovarian Workshop, Champaign, IL, 1985:451–80.

    Google Scholar 

  2. Nimrod A, Lindner HR. Heparin facilitates the induction of LH receptors by FSH in granulosa cells cultured in serum-enriched medium. FEBS Lett 1980; 119:155–7.

    Article  PubMed  CAS  Google Scholar 

  3. Amsterdam A, Riesel R, Mintz Y, Shemesh M, Salomon Y. Inhibition of gonadotropin sensitive adenylate cyclase by ovarian follicular fluid. Biochem Biophys Res Commun 1979;87:505–12.

    Article  PubMed  CAS  Google Scholar 

  4. Bellin ME, Veldhuis JD, Ax RL. Follicular fluid glycosaminoglycans inhibit degradation of low density lipoproteins and progesterone production by porcine granulosa cells. Biol Reprod 1987; 37:1179–84.

    Article  PubMed  CAS  Google Scholar 

  5. Ledwitz-Rigby F, Gross TM, Schjeide OA, Rigby BW. The glycosaminoglycan chondroitin-4-sulfate alters progesterone secretion by porcine granulosa cells. Biol Reprod 1987; 36:320–7.

    Article  PubMed  CAS  Google Scholar 

  6. Bushmeyer SM, Bellin ME, Ax RL. Specific binding of [H]heparin to bovine granulosa cell membranes. Mol Cell Endocrinol 1985; 42:135–44.

    Article  PubMed  CAS  Google Scholar 

  7. Ax RL, Bushmeyer SM, Boehm SK, Bellin ME. Binding of the glycosaminoglycan [3H]heparin to bovine granulosa cells varies with size and estrogen content of ovarian follicles. Endocr Res 1984; 10:63–72.

    PubMed  CAS  Google Scholar 

  8. Bellin ME, Wentworth BC, Ax RL. Comparisons of the ability of follicular fluid glycosaminoglycans and chemically desulfated heparin to compete for heparin binding sites on granulosa cells. Biol Reprod 1987; 37:293–300.

    Article  PubMed  CAS  Google Scholar 

  9. Ax RL, Stodd CM, Boehm SK, Bellin ME. Removal of glycosaminoglycans from bovine granulosa cells contributes to increased binding of hydrogen-3 heparin. J Dairy Sci 1986; 69:531–4.

    Article  PubMed  CAS  Google Scholar 

  10. Hunter MJ, Commerford SL. Pressure homogenization of mammalian tissues. Biochim Biophys Acta 1961; 47:580–6.

    Article  PubMed  CAS  Google Scholar 

  11. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 277:680–5.

    Article  Google Scholar 

  12. Wray W, Boulikas T, Wray VP, Hancock R. Silver staining of proteins in Polyacrylamide gels. Anal Biochem 1981; 118:197–203.

    Article  PubMed  CAS  Google Scholar 

  13. Burnette WN. “Western blotting:” electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal Biochem 1981; 112:195–203.

    Article  PubMed  CAS  Google Scholar 

  14. Bolton AE, Hunter WM. The labelling of proteins to high specific radioactivities by conjugation to a I-containing acylating agent. Biochem J 1973; 133:529–39.

    PubMed  CAS  Google Scholar 

  15. Cardin AD, Witt KR, Jackson RL. Visualization of heparin-binding proteins by ligand blotting with 125I-heparin. Anal Biochem 1984; 137:368–73.

    Article  PubMed  CAS  Google Scholar 

  16. Smith JW, Knauer DJ. Ligand blotting with I-fluoresceinamine-heparin. Anal Biochem 1987; 160:105–14.

    Article  PubMed  CAS  Google Scholar 

  17. Kraemer PM, Tobey RA. Cell-cycle dependent desquamation of heparan sulfate from the cell surface. J Cell Biol 1972; 55:713–7.

    Article  PubMed  CAS  Google Scholar 

  18. Priedkalns J, Weber AF, Zemjanis R. Qualitative and quantitative morphological studies of the cells of the membrana granulosa, theca interna and corpus luteum of the bovine ovary. Z Mikrosk Anat Forsch 1968; 85:501–20.

    Article  CAS  Google Scholar 

  19. Lobb RR, Harper JW, Fett JW. Purification of heparin-binding growth factors. Anal Biochem 1986; 154:1–14.

    Article  PubMed  CAS  Google Scholar 

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© 1989 Plenum Press, New York

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Winer, M.A., Ax, R.L. (1989). Heparin-Binding Proteins in Purified Plasma Membranes of Bovine Granulosa Cells. In: Hirshfield, A.N. (eds) Growth Factors and the Ovary. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5688-2_37

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  • DOI: https://doi.org/10.1007/978-1-4684-5688-2_37

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-5690-5

  • Online ISBN: 978-1-4684-5688-2

  • eBook Packages: Springer Book Archive

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