Date of Award
Bachelor of Science
Brian D. Cohen
The purpose of my research project has been to determine the nature of the binding relationship between caveolin and hFSHR inside sex cells. FSH plays a role in the maturation of these cells, and interfering with the receptor’s interaction with caveolin would prevent cell maturation (down regulating fertility). It is believed the interaction occurs through transmembrane domain IV of the receptor due to its aromatic nature. The treatment of sex cells with synthetic peptides that mimic the hFSHR-caveolin binding sequence should prevent the interaction, shutting down the signaling cascade from hFSHR. This can be tested for by the monitoring of downstream signals given off by hFSHR, including the presence (or absence) of phosphorylated p44, PKA, and CREB. It is hypothesized the wildtype peptide treatment will down regulate all of these signals when compared to the mutant control. Current data points towards this hypothesis holding true, with successful western blots displaying a noted difference in cell signaling between the wildtype and mutant peptide treatments. These results indicate the key interaction between caveolin and hFSHR likely occurs at transmembrane domain IV.
Hagan, Timothy James, "Investigation of the Caveolin-Human Follicle Stimulating Hormone Receptor Interaction through Peptide Treatments" (2016). Honors Theses. 111.