The Interaction of Follitropin (FSH) with Membrane-Bound and Solubilized Gonadal Receptors and Adenylate Cyclase

  • L. E. ReichertJr.
  • H. Abou-Issa
Part of the Biochemical Endocrinology book series (BIOEND)


The interaction of follitropin (FSH, follicle-stimulating hormone) with testicular receptors has been studied most extensively in the rat model. Means and Vaitukaitis (1972) studied the binding of tritiated human FSH (hFSH) to receptors in immature rat testis. We have studied the interaction of biologically active, radioiodinated hFSH [125I]-hFSH with receptors in homogenates (Bhalla and Reichert, 1974a,b) and purified membranes from testes tubules of mature rats (Abou-Issa and Reichert, 1976). Desjardins et al. (1977) utilized radioiodinated human and rat FSH to study binding of the hormone to testis during maturation in the rat. It was found that the amount of labeled hormone bound to testis receptor increased slightly (P< 0.01) between 5 and 15 days and then remained relatively constant from 30 to 90 days. No apparent differences were noted in binding parameters between rat FSH and hFSH, although this was not rigorously examined. Considerable information is now available on the characteristics of the follitropin—receptor interaction in rat testes. A summary of reported values for K d and binding capacity is given in Table I. An outline of different conditions utilized to achieve maximum specific binding is also given in Table I. Binding of radiolabeled hFSH to rat testicular receptor is hormone- and tissue-specific and temperature- and pH-dependent, and apparently requires divalent cations for maximum binding, with no apparent specificity shown among Mg2+, Mn2+, and Ca2+ (Abou-Issa and Reichert, 1976).


Granulosa Cell Adenylate Cyclase Follicular Fluid Testicular Receptor Bovine Testis 
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Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • L. E. ReichertJr.
    • 1
  • H. Abou-Issa
    • 1
  1. 1.Department of BiochemistryEmory University School of MedicineAtlantaUSA

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