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Gonadotropins and Their Subunits: Basic and Clinical Studies

1976; Elsevier BV; Linguagem: Inglês

10.1016/b978-0-12-571132-6.50019-1

J. L. VAITUKAITIS, Griff T. Ross, Glenn D. Braunstein, Phillip L. Rayford,

Glycosylation and Glycoproteins Research

This chapter presents some basic and clinical studies to discuss gonadotropins and their subunits. These studies conclude that specific alterations of the carbohydrate portion of the glycoprotein hormones result in both immunologic and biologic alterations, depending on the hormone in question. The immunologic behavior of human chorionic gonadotropin (hCG) is least affected by desialylation as compared to lutenizing hormone (LH) and follicle stimulating hormone (FSH). The glycoprotein hormones—LH, FSH, hCG, and thyroid-stimulating hormone (TSH)—share a common quaternary structure composed of essentially identical α-subunits. Both the placenta and pituitary contain an excess of free α-subunits, that implies that the mechanism of synthesis and secretion of the glycoprotein hormones from those organs can be similar. Significant clinical applications have resulted from the basic immunologic and biologic studies of the subunits of the glycoprotein hormones. Specifically, antisera to the subunits of the glycoprotein hormones are used as probes for studying the synthesis and secretion of free subunits from both the pituitary and placenta. The specific antisera to the β-subunit of hCG are used to screen a wide variety of patients with tumors ectopically secreting hCG. These reagents should prove useful for further delineation of control of synthesis and secretion of the gonadotropins for future investigators.