Date of Award


Document Type

Union College Only

Degree Name

Bachelor of Science



First Advisor

Brian Cohen




hormone, receptor, Sertoli cells, pahtways, kinase, activation


Human follicle stimulating hormone (hFSH) is a glycoprotein hormone that acts through a cell surface G protein-coupled receptor. Receptor activation stimulates cAMP production to promote normal gamete formation in both males and females. In men, FSH is responsible for stimulating spermatogenesis by stimulating the proliferation of Sertoli cells. In women, FSH functions with luteinizing hormone (LH) to regulate the menstrual cycle and to promote oocyte maturation in the ovary. Understanding and developing techniques to control the signal transduction pathway of the follicle stimulating hormone receptor (hFSHR) may lead to novel in vitro fertilization and contraceptive techniques. We hypothesize that the hFSHR signaling complex is compartmentalized within plasma membrane microdomains known as lipid rafts. The goal of this study was to investigate the role of lipid rafts in the function of hFSHR. A cholesterol-withdrawing agent called methyl-b-cyclodextrin was used to disrupt lipid rafts. Then, western blotting techniques were then used to analyze the activation of hFSHR downstream pathways, p38-MAP kinase and p44/42-MAP kinase. Cholesterol depletion resulted in the maintenance of p44/42 activity but interfered with activation of the p38 pathway. This suggests that these pathways have different mechanisms of activation and may represent a potential opportunity for therapeutic intervention.