Stage-Dependent Differences in FSH Binding and Cyclic Nucleotide Secretion and Metabolism during the Cycle of the Rat Seminiferous Tubule

  • K. Purvis
  • M. Parvinen
  • K. Gautvik
  • V. Hansson
Part of the Biochemical Endocrinology book series (BIOEND, volume 1)


In living, freshly isolated rat seminiferous tubules, cyclic changes in FSH binding, cAMP secretion (basal and FSH stimulated) and the activities of cAMP and cGMP phosphodiesterases could be detected which were related to specific stages of spermatogenesis. FSH binding (per cm stage) increased gradually between stages VII and IX and then, after remaining relatively constant, was elevated further in stages XIV-I. Thereafter, binding fell to a nadir stage VIIa-b. FSH stimulated cAMP secretion was at its lowest in stage VIIa-b and maximal between stages XIV-V. The greatest specific activities of the cAMP and cGMP phosphodiesterases were detected in stages VII-VIII which are associated with spermiation in the rat. A degree of dissociation was found to exist in the cAMP and cGMP hydrolysing capacities at certain stages (IX-XII), suggesting the existence of different isoforms of the enzyme which may be differentially controlled. Exposure of the various stages to FSH or dibutyryl cAMP for 4 hr in vitro did not alter the profiles of phosphodiesterase activity.

The phosphodiesterase profiles were inversely related to the quantity of cAMP produced by the tubular segments after stimulation with FSH, both in the presence and absence of the phosphodiesterase inhibitor, methyl isobutyl xanthine (MIX). However, MIX elicited the greatest effect from the tubular segments, in terms of FSH stimulated cAMP production, in stages XIV-V, where direct measurements of phosphodiesterase indicate the enzyme activity is relatively low. The reasons for this apparent contradiction are discussed in relation to previous findings on stage-dependent alterations in various aspects of tubular function.


Sertoli Cell Adenylyl Cyclase Seminiferous Tubule Methyl Isobutyl Xanthine Phosphodiesterase Activity 
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  1. Cusan, L., Gordeladze, J. O., Parvinen, M., Clausen, 0. P. F., and Hansson, V., 1981, Protein carboxyl-methylase and germ cell adenylyl cyclase at specific stages of the spermatogenic cycle of the rat, Biol. Reprod., 25:915.PubMedCrossRefGoogle Scholar
  2. Gardner, E. A., Thompson, W. J., and Stancel, G. M., 1976, Characterization of uterine phosphodiesterase and effects of estrogen on enzyme activity, Fed. Proc., 35 Abstr. 2224.Google Scholar
  3. Gordeladze, J. O., Parvinen, M., Clausen, O. P. F., and Hansson, V., 1981, Stage-dependent variation in Mn2 -sensitive adenylyl cyclase (AC) activity in spermatids and FSH-sensitive AC in Sertoli cells, Arch. Andrology, 8:43.CrossRefGoogle Scholar
  4. Garvis, C. J., 1978, Inhibition of spermiation in the Syrian hamster using debutyryl cyclic-AMP, Cell. Tiss. Res., 192: 241.Google Scholar
  5. Hansson, V., Purvis, K., Attramadal, A., Torjesen, P., Andersen, D., and Ritzen, E. M., 1978, Sertoli cell function in the androgen insensitive (Tfm) rat, Int. J. Androl., 1:96.CrossRefGoogle Scholar
  6. Lacroix, M., Parvinen, M., and Fritz, I. B., 1981, Localization of testicular plasminogen activator in discrete portions (stages VII and VIII) of the seminiferous tubule, Biol. Reprod., 25:143.PubMedCrossRefGoogle Scholar
  7. Loten, E. G., and Sneyd, J. G. T., 1973, Evidence for separate sites of action for the antilipolytic effects of insulin and prostaglandin E1, Endocrinology, 93:1315.PubMedCrossRefGoogle Scholar
  8. Means, A. R., Dedman, J. R., Fakunding, J. L., and Tindall, D. J., 1978, Mechanism of action of FSH in the male rat, in: “Receptors and Hormone Action,” Vol. Ill, pp. 363–392, L. Birnbaumer, B. W. O’Malley, eds., Academic Press, New York.Google Scholar
  9. Parvinen, M., Marana, R., Robertson, D. M., Hansson, V., and Ritzén, E. M., 1980, Functional cycle of the rat Sertoli cells: Differential binding and action of follicle-stimulating hormone at various stages of the spermatogenic cycle, in: “Testicular Development, Structure, and Function,” pp. 425–432, A. Steinberger, E. Steinberger, eds., Raven Press, New York.Google Scholar
  10. Parvinen, M., and Ruokonen, A., 1982, Endogenous steroids in rat seminiferous tubules. Comparison of different spermatogenic stages isolated by transillumination-assisted microdissection, J. Androl., in press.Google Scholar
  11. Purvis, K., Olsen, A., Barry, M., and Hansson, V., 1981, Testicular cyclic nucleotide phosphodiesterase in the rat. Kinetic properties and changes with age, Arch. Andrology, 6:327.CrossRefGoogle Scholar
  12. Ritzen, E. M., Parvinen, M., Hansson, V., French, F. S., and Feldman, M., 1980, Role of Sertoli cell in spermatogenesis, in: “Proc. VI Int. Congr. Endocrinol.,” pp. 159–161, Australian Academy of Science, Canberra.Google Scholar
  13. Stephens, D. T., Wang, J. -L., and Hoskins, D. D., 1979, The cyclic AMP phosphodiesterase of bovine spermatozoa: Multiple forms, kinetic properties and changes during development, Biol. Reprod., 20:483.PubMedCrossRefGoogle Scholar
  14. Thompson, W. J., and Williams, R. H., 1974, Effect of adrenalectomy on cyclic 3’,5’-guanosine monophosphate metabolism of rat liver and other tissues, Arch. Biochem. Biophys., 165:468.PubMedCrossRefGoogle Scholar
  15. Tovey, K. C., Oldham, K. G., and Whelan, J. A. M., 1974, A simple direct assay for cyclic AMP in plasma and other biological samples using an improved competitive protein binding technique, Clin. Chim. Acta 56:221.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • K. Purvis
    • 1
  • M. Parvinen
    • 2
  • K. Gautvik
    • 3
  • V. Hansson
    • 1
  1. 1.Institute of PathologyRikshospitaletOsloNorway
  2. 2.Institute of Biomedicine, Department of AnatomyUniversity of TurkuTurku 52Finland
  3. 3.Institute of PhysiologyUniversity of OsloOsloNorway

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