The Follicle Stimulating Hormone Receptor
Regulation and maintenance of Sertoli cell functions essential for spermatogenesis are primarily dependent on follitropin (FSH), a glycoprotein hormone that is elaborated by the anterior pituitary gland. The initial event in follitropin action is the specific binding of the hormone by high affinity follitropin receptors present on the Sertoli cell plasma membrane. We have studied this process extensively using membrane preparations of variable degrees of purity from rat and bovine calf testis (Bhalla and Reichert, 1974; Abou-Issa and Reichert, 1976,1977). Such studies have proven useful in understanding the functional requirements for specific interactions of follitropin to hormone-specific membrane receptors, and these have been reviewed previously (Reichert et al., 1983,1984; Reichert and Dattatreyamurty, 1989). A soluble follitropin binding component derived from bovine calf testis in the absence of detergent has also been identified (Dias and Reichert, 1982) and the modulation of follitropin binding to receptors by monovalent salts and divalent cations has been reported (Andersen and Reichert, 1982). We also established that the hydrophobic effect is the most important force participating in the interaction of follitropin with its receptor in the membrane and after solubilization (Andersen et al., 1983; Sanborn et al., 1987).
KeywordsCellulose Fluoride Fractionation Disulfide Estradiol
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