Skip to main content
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1985 Jun 1;100(6):1941–1947. doi: 10.1083/jcb.100.6.1941

Cooperativity between Sertoli cells and testicular peritubular cells in the production and deposition of extracellular matrix components

PMCID: PMC2113598  PMID: 3889013

Abstract

We examined the synthesis and deposition of extracellular matrix (ECM) components in cultures of Sertoli cells and testicular peritubular cells maintained alone or in contact with each other. Levels of soluble ECM components produced by populations of isolated Sertoli cells and testicular peritubular cells were determined quantitatively by competitive enzyme-linked immunoabsorbent assays, using antibodies shown to react specifically with Type I collagen, Type IV collagen, laminin, or fibronectin. Peritubular cells in monoculture released into the medium fibronectin (432 to 560 ng/microgram cell DNA per 48 h), Type I collagen (223 to 276 ng/microgram cell DNA per 48 h), and Type IV collagen (350 to 436 ng/microgram cell DNA per 48 h) during the initial six days of culture in serum-free medium. In contrast, Sertoli cells in monoculture released into the medium Type IV collagen (322 to 419 ng/microgram cell DNA per 48 h) but did not form detectable amounts of Type I collagen or fibronectin during the initial six days of culture. Neither cell type produced detectable quantities of soluble laminin. Immunocytochemical localization investigations demonstrated that peritubular cells in monoculture were positive for fibronectin, Type I collagen, and Type IV collagen but negative for laminin. In all monocultures most of the ECM components were intracellular, with scant deposition as extracellular fibrils. Sertoli cells were positive immunocytochemically for Type IV collagen and laminin but negative for fibronectin and Type I collagen. Co-cultures of peritubular cells and Sertoli cells resulted in interactions that quantitatively altered levels of soluble ECM components present in the medium. This was correlated with an increased deposition of ECM components in extracellular fibrils. The data correlated with an increased deposition of ECM components in extracellular fibrils. The data presented here we interpret to indicate that the two cell types in co-culture act cooperatively in the formation and deposition of ECM components. Results are discussed with respect to the nature of interactions between mesenchymal peritubular cell precursors and adjacent epithelial Sertoli cell precursors in the formation of the basal lamina of the seminiferous tubule.

Full Text

The Full Text of this article is available as a PDF (868.7 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bressler R. S., Ross M. H. Differentiation of peritubular myoid cells of the testis: effects of intratesticular implantation of newborn mouse testes into normal and hypophysectomized adults. Biol Reprod. 1972 Feb;6(1):148–159. doi: 10.1093/biolreprod/6.1.148. [DOI] [PubMed] [Google Scholar]
  2. Dym M., Fawcett D. W. The blood-testis barrier in the rat and the physiological compartmentation of the seminiferous epithelium. Biol Reprod. 1970 Dec;3(3):308–326. doi: 10.1093/biolreprod/3.3.308. [DOI] [PubMed] [Google Scholar]
  3. Elkington J. S., Fritz I. B. Regulation of sulfoprotein synthesis by rat Sertoli cells in culture. Endocrinology. 1980 Oct;107(4):970–976. doi: 10.1210/endo-107-4-970. [DOI] [PubMed] [Google Scholar]
  4. Foidart J. M., Foidart J. B., Mahieu P. R. Synthesis of collagen and fibronectin by glomerular cells in culture. Ren Physiol. 1980;3(1-6):183–192. doi: 10.1159/000172760. [DOI] [PubMed] [Google Scholar]
  5. Fritz I. B., Karmally K. Hormonal influences on formation of plasminogen activator by cultured testis tubule segments at defined stages of the cycle of the seminiferous epithelium. Can J Biochem Cell Biol. 1983 Jul;61(7):553–560. doi: 10.1139/o83-071. [DOI] [PubMed] [Google Scholar]
  6. Gore-Langton R. E., Tung P. S., Fritz I. B. The absence of specific interactions of Sertoli-cell-secreted proteins with antibodies directed against H-Y antigen. Cell. 1983 Jan;32(1):289–301. doi: 10.1016/0092-8674(83)90519-6. [DOI] [PubMed] [Google Scholar]
  7. Hay E. D. Extracellular matrix. J Cell Biol. 1981 Dec;91(3 Pt 2):205s–223s. doi: 10.1083/jcb.91.3.205s. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hutson J. C., Stocco D. M. Peritubular cell influence on the efficiency of androgen-binding protein secretion by Sertoli cells in culture. Endocrinology. 1981 Apr;108(4):1362–1368. doi: 10.1210/endo-108-4-1362. [DOI] [PubMed] [Google Scholar]
  9. Killen P. D., Striker G. E. Human glomerular visceral epithelial cells synthesize a basal lamina collagen in vitro. Proc Natl Acad Sci U S A. 1979 Jul;76(7):3518–3522. doi: 10.1073/pnas.76.7.3518. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Lacroix M., Parvinen M., Fritz I. B. Localization of testicular plasminogen activator in discrete portions (stage VII and VIII) of the seminiferous tubule. Biol Reprod. 1981 Aug;25(1):143–146. doi: 10.1095/biolreprod25.1.143. [DOI] [PubMed] [Google Scholar]
  11. MARTIN G. R., GROSS J., PIEZ K. A., LEWIS M. S. On the intramolecular cross-linking of collagen in lathyritic rats. Biochim Biophys Acta. 1961 Nov 11;53:599–601. doi: 10.1016/0006-3002(61)90227-x. [DOI] [PubMed] [Google Scholar]
  12. McLean I. W., Nakane P. K. Periodate-lysine-paraformaldehyde fixative. A new fixation for immunoelectron microscopy. J Histochem Cytochem. 1974 Dec;22(12):1077–1083. doi: 10.1177/22.12.1077. [DOI] [PubMed] [Google Scholar]
  13. Miller E. J., Martin G. R., Piez K. A., Powers M. J. Characterization of chick bone collagen and compositional changes associated with maturation. J Biol Chem. 1967 Dec 10;242(23):5481–5489. [PubMed] [Google Scholar]
  14. Russell L. D., Tallon-Doran M., Weber J. E., Wong V., Peterson R. N. Three-dimensional reconstruction of a rat stage V Sertoli cell: III. A study of specific cellular relationships. Am J Anat. 1983 Jun;167(2):181–192. doi: 10.1002/aja.1001670204. [DOI] [PubMed] [Google Scholar]
  15. Russell L. Movement of spermatocytes from the basal to the adluminal compartment of the rat testis. Am J Anat. 1977 Mar;148(3):313–328. doi: 10.1002/aja.1001480303. [DOI] [PubMed] [Google Scholar]
  16. Skinner M. K., Fritz I. B. Testicular peritubular cells secrete a protein under androgen control that modulates Sertoli cell functions. Proc Natl Acad Sci U S A. 1985 Jan;82(1):114–118. doi: 10.1073/pnas.82.1.114. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Tung P. S., Dorrington J. H., Fritz I. B. Structural changes inducted by follicle-stimulating hormone or dibutyryl cyclic AMP on presumptive Sertoli cells in culture. Proc Natl Acad Sci U S A. 1975 May;72(5):1838–1842. doi: 10.1073/pnas.72.5.1838. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Tung P. S., Fritz I. B. Extracellular matrix promotes rat Sertoli cell histotypic expression in vitro. Biol Reprod. 1984 Feb;30(1):213–229. doi: 10.1095/biolreprod30.1.213. [DOI] [PubMed] [Google Scholar]
  19. Tung P. S., Fritz I. B. Interactions of sertoli cells with myoid cells in vitro. Biol Reprod. 1980 Aug;23(1):207–217. doi: 10.1093/biolreprod/23.1.207. [DOI] [PubMed] [Google Scholar]
  20. Tung P. S., Fritz I. B. Specific surface antigens on rat pachytene spermatocytes and successive classes of germinal cells. Dev Biol. 1978 Jun;64(2):297–315. doi: 10.1016/0012-1606(78)90080-5. [DOI] [PubMed] [Google Scholar]
  21. Tung P. S., Skinner M. K., Fritz I. B. Fibronectin synthesis is a marker for peritubular cell contaminants in Sertoli cell-enriched cultures. Biol Reprod. 1984 Feb;30(1):199–211. doi: 10.1095/biolreprod30.1.199. [DOI] [PubMed] [Google Scholar]
  22. Wang H. M., Nanda V., Rao L. G., Melcher A. H., Heersche J. N., Sodek J. Specific immunohistochemical localization of type III collagen in porcine periodontal tissues using the peroxidase-antiperoxidase method. J Histochem Cytochem. 1980 Nov;28(11):1215–1223. doi: 10.1177/28.11.7000890. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES