Date of Award
2005
Document Type
Thesis
Publication Status
Version of Record
Submission Date
October 2026
Thesis/Dissertation Advisor [Chair]
Haerry, Theodor E.
Abstract
Follistatin (FS) proteins are highly conserved inhibitors of Activins, members of the Transforming Growth Factor beta (TGF-beta) family, which play prominent roles in patterning and cell proliferation, and can contribute to tumor formation. Comparison of FS from Drosophila (dFS) and humans (hFS) in flies shows that hFS is less active. The goal of this thesis is to test three possible mechanisms: dFS might be more stable and turn over at a lower rate, exhibit a stronger affinity for ligands, or diffuse less because of stronger interaction with the extracellular matrix. We generated chimeric proteins of dFS and hFS by exchanging individual protein domains. Our results suggest that the increased activity is likely due to ligand binding. Based on the recent structure of the hFS-Activin complex, we speculate that stronger interactions with heparin sulfate in the extracellular matrix may also contribute to the increased activity of dFS.
Extent
50 p.
Recommended Citation
Shah, Ripal., "Functional analysis of Drosophila and human follistatin domains and their role in growth inhibition" (2005). Electronic Theses and Dissertations 2000 - 2009. 870.
https://digitalcommons.fau.edu/etd_general_5/870
Identifier
FADT13282
Comments
Charles E. Schmidt College of Science|Thesis (M.S.)--Florida Atlantic University, 2005.|Charles E. Schmidt College of Science