Advertisement

Differentiation and Polarized Function of Sertoli Cells In Vitro

  • M. Dym
  • M. A. Hadley
  • D. Djakiew
  • S. W. Byers
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 219)

Abstract

The seminiferous epithelium is composed of two populations of cell types, supportive epithelial elements, the highly polarized Sertoli cells and differentiating elements, the germ cells. The Sertoli cell is a tall, narrow, columnar cell that extends from the basal lamina of the seminiferous epithelium to the tubule lumen. It possesses numerous lateral branches which surround the developing germ cells and it appears to provide support for their differentiation. The basal aspects of the Sertoli cells are linked by specialized tight junctional complexes and these junctions subdivide the seminiferous epithelium into two compartments, basal and apical (Dym and Fawcett, 1970). The tight junctions form the morphological basis of the blood-testis barrier. The basal domain of the cell, in contact with extracellular matrix molecules, possesses receptors for circulating plasma constituents (e.g., FSH receptors — Orth and Christensen, 1977). The apical surface of the cell, in contact with the tubule lumen, is undoubtedly involved in sperm release (Fawcett, 1975). An examination of the ultrastructure of the Sertoli cell reveals a highly polar organization of the organelles (Fawcett, 1975).

Keywords

Tight Junction Sertoli Cell Culture Chamber Seminiferous Epithelium Pachytene Spermatocyte 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Aisen P, Listowsky I, 1980. Iron transport and storage protein. Ann Rev Biochem 49:357–393PubMedCrossRefGoogle Scholar
  2. Blaschuk O, Burdzy K, Fritz IB, 1983. Purification and characterization of a cell-aggregating factor (clusterin), the major glycoprotein in ram rete testis fluid. J Biol Chem 258:7714–7720PubMedGoogle Scholar
  3. Borland K, Muffly KE, Hall PF, 1986. Production of components of extracellular matrix by cultured rat Sertoli cells. Biol Reprod 35:997–1008PubMedCrossRefGoogle Scholar
  4. Byers SW, Hadley MA, Dym M, 1985. Growth of polarized monolayers of epithelial cells from the male reproductive tract on permeable extracellular (ECM) matrix supports. Third Int Cong Androl, BostonGoogle Scholar
  5. Byers SW, Hadley MA, Djakiew D, Dym M, 1986. Growth and characterization of polarized monolayers of epididymal epithelial cells and Sertoli cells in dual environment culture chambers. J Androl 7:59–69PubMedGoogle Scholar
  6. Caplan MJ, Anderson HC, 1986. Intracellular sorting and polarized cell surface delivery of(Na+, K+)ATPase, and endogenous component of MDCK cell basolateral plasma membranes. Cell 46:623–631PubMedCrossRefGoogle Scholar
  7. Cheng YC, Mather JP, Byer AL, Bardin WC, 1986. Identification of hormonally responsive proteins in primary Sertoli cell culture medium by anion-exchange high performance liquid chromatography. Endocrinology 118:480–488PubMedCrossRefGoogle Scholar
  8. Cheng YC, Bardin WC, 1986. Rat testicular testibumin is a protein responsive to follicle stimulating hormone and testosterone that shares immunodeterminants with albumin. Biochemistry 25:5276–5288PubMedCrossRefGoogle Scholar
  9. Conner JR, Fine RE, 1986. The distribution of transferrin immunoreactivity in the rat central nervous system. Brain Res 368:319–328CrossRefGoogle Scholar
  10. Djakiew D, Hadley MA, Byers SW, Dym M, 1986. Transferrin-mediated trans-cellular transport of 59Fe across confluent epithelial sheets of Sertoli cells grown in bicameral cell culture chambers. J Androl 7:355–366PubMedGoogle Scholar
  11. Dorrington JH, Roller NF, Fritz IB, 1975. Effects of follicle-stimulating hormone on cultures of Sertoli cell preparations. Mol Cell Endocrinol 3:57–70PubMedCrossRefGoogle Scholar
  12. Dym M, Fawcett DW, 1970. The blood-testis barrier in the rat and the physiological compartmentation of the seminiferous epithelium. Biol Reprod 3:308–326PubMedGoogle Scholar
  13. Fawcett DW, 1975. Ultrastructure and function of the Sertoli cell. In: Handbook of Physiology, Section 7, Vol 5. Washington, Am Physiol SocGoogle Scholar
  14. Frazier JL, Caskey JH, Yoffe M, Seligman PA, 1982. Studies of the transferrin receptor on both human reticulocytes and nucleated human cells in culture. Comparisons of factors regulating receptor density. J Clin Invest 69:853–865PubMedCrossRefGoogle Scholar
  15. Fritz IB, Griswold MD, Louis BG, Dorrington JH, 1976. Similarity of responses of cultured Sertoli cells to cholera toxin and FSH. Mol Cell Endocrinol 5:289–294PubMedCrossRefGoogle Scholar
  16. Gunsalus GL, Musto NA, Bardin CW, 1980. Bidirectional release of a Sertoli cell product, androgen binding protein, into the blood and seminiferous tubule. In: Steinberger A and Steinberger E (eds.), Testicular Development, Structure and Function. New York, Raven Press, pp. 291–298Google Scholar
  17. Gunsalus GL, Musto NA, Bardin CW, Kunz HW, Gill TJ, 1985. Rats homozygous for the grc complex have defective transport of androgen-binding protein to the epididymis, but normal secretion into the blood. Biol Reprod 33:1057–1063PubMedCrossRefGoogle Scholar
  18. Hadley MA, Byers SW, Suarez-Quian CA, Kleinman HK, Dym M, 1985. Extracellular matrix regulates Sertoli cell differentiation, testicular cord formation, and germ cell development in vitro. J Cell Biol 101:1511–1522PubMedCrossRefGoogle Scholar
  19. Hadley MA, Dym D, 1987. Electron microscopic immunocytochemical localization of the extracellular matrix in the lamina propria of the rat testis. Biol ReprodGoogle Scholar
  20. Hadley MA, Djakiew D, Byers SW, Dym M, 1987. Polarized secretion of androgen binding protein and transferrin by Sertoli cells grown in a bicameral culture system. Endocrinology 120:000–000CrossRefGoogle Scholar
  21. Hay ED, 1984. Cell-matrix interaction in the embryo: cell shape, cell surface, cell skeletons, and their role in differentiation. In: Trelstad RL (ed.), The Role of the Extracellular Matrix in Development. New York: Alan R. Liss, Inc., pp. 1–31Google Scholar
  22. Huggenvik J, Sylvester SR, Griswold MD, 1984. Control of transferrin RNA synthesis in Sertoli cells. Ann NY Acad Sci 438:1–7PubMedCrossRefGoogle Scholar
  23. Janecki A, Steinberger A, 1987. Bipolar secretion of androgen-binding protein and transferrin by Sertoli cells cultured in a two compartment culture chamber. Endocrinology 120:291–298PubMedCrossRefGoogle Scholar
  24. Kleinman HK, Klebe RJ, Martin GR, 1981. Role of collagenous matrices in the adhesion and growth of cells. J Cell Biol 88:473–485PubMedCrossRefGoogle Scholar
  25. Lacroix M, Smith FE, Fritz IB, 1977. Secretion of plasminogen activator by Sertoli cell enriched cultures. Mol Cell Endocrinol 9:227–236PubMedCrossRefGoogle Scholar
  26. Misfeldt DS, Hamamoto ST, Pitelka DR, 1976. Transepithelial transport in cell culture. PNAS 73:1212–1216PubMedCrossRefGoogle Scholar
  27. Orth J, Christensen AK, 1977. Localization of 125I-labeled FSH in the testes of hypophysectomized rats by autoradiography at the light and electron microscopic levels. Endocrinology 101:262–278PubMedCrossRefGoogle Scholar
  28. Simmons NL, Brown CDA, Rugg EL, 1984. The action of epinephrine on Madin-Darby canine kidney cells. Fed Proc 43:2225–2229PubMedGoogle Scholar
  29. Skinner MK, Griswold MD, 1980. Sertoli cells synthesize and secrete transferrin-like protein. J Biol Chem 255:9523–9525PubMedGoogle Scholar
  30. Skinner MK, Griswold MD, 1983. Sertoli cells synthesize and secrete a ceruloplasmin-like protein. Biol Reprod 28:1225–1229PubMedCrossRefGoogle Scholar
  31. Skinner MK, Tung PS, Fritz IB, 1985. Cooperativity between Sertoli cells and testicular peritubular cells in the production and disposition of extracellular matrix components. J Cell Biol 100:1941–1947PubMedCrossRefGoogle Scholar
  32. Spitz IM, Gunsalus GL, Mather JP, Thau P, Bardin WC, 1985. The effects of the indazole carboxylic acid derivative, tolnidamine, on testicular function: 1. Early changes in androgen binding protein secretion in the rat. J Androl 6:171–178PubMedGoogle Scholar
  33. Steinberger A, Steinberger E, 1976. Secretion of an FSH-inhibiting factor by cultured Sertoli cells. Endocrinology 99:918–921PubMedCrossRefGoogle Scholar
  34. Steinberger A, Heindel JJ, Lindsay JN, Elkington JS, Sandborn BM, Steinberger E, 1975. Isolation and culture of FSH responsive Sertoli cells. Endocrinol Res Comm 2:261–272CrossRefGoogle Scholar
  35. Sternberger LA, 1979. Immunocytochemistry. NY: John Wiley and Sons.Google Scholar
  36. Suarez-Quian CA, Hadley MA, Dym M, 1984. Effect of substrate on the shape of Sertoli cells “in vitro”. Ann NY Acad Sci 438:417–434PubMedCrossRefGoogle Scholar
  37. Tung PS, Skinner MK, Fritz IB, 1984. Fibronectin synthesis is a marker for peritubular cell contaminants in Sertoli cell-enriched cultures. Biol Reprod 30:199–211PubMedCrossRefGoogle Scholar
  38. Van Renswoude J, Bridges KR, Harford JB, Klausner RD, 1982. Receptor-mediated endocytosis of transferrin and the uptake of Fe in K 562 cells: identification of a nonlysosomal acidic compartment. PNAS 79:6186–6190PubMedCrossRefGoogle Scholar
  39. Wright WW, Musto NA, Mather JP, Bardin CW, 1981. Sertoli cells secrete both testis specific and serum proteins. PNAS (USA) 78:7565–7569CrossRefGoogle Scholar
  40. Welsh MJ, Weibe JP, 1975. Rat Sertoli cells: a rapid method for obtaining viable cells. Endocrinology 96:618–624PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • M. Dym
    • 1
  • M. A. Hadley
    • 1
  • D. Djakiew
    • 1
  • S. W. Byers
    • 1
  1. 1.Department of Anatomy and Cell Biology, School of Medicine - School of DentistryGeorgetown UniversityUSA

Personalised recommendations