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Functional analysis of Drosophila and human follistatin domains and their role in growth inhibition
- Date Issued:
- 2005
- Summary:
- 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.
Title: | Functional analysis of Drosophila and human follistatin domains and their role in growth inhibition. |
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Name(s): |
Shah, Ripal. Florida Atlantic University, Degree grantor Haerry, Theodor E., Thesis advisor |
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Type of Resource: | text | |
Genre: | Electronic Thesis Or Dissertation | |
Issuance: | monographic | |
Date Issued: | 2005 | |
Publisher: | Florida Atlantic University | |
Place of Publication: | Boca Raton, Fla. | |
Physical Form: | application/pdf | |
Extent: | 50 p. | |
Language(s): | English | |
Summary: | 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. | |
Identifier: | 9780542386756 (isbn), 13282 (digitool), FADT13282 (IID), fau:10134 (fedora) | |
Note(s): |
Charles E. Schmidt College of Science Thesis (M.S.)--Florida Atlantic University, 2005. |
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Subject(s): |
Cell differentiation Drosophila--Cytology Molecular genetics Reproduction--Physiological aspects Glycoproteins |
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Held by: | Florida Atlantic University Libraries | |
Persistent Link to This Record: | http://purl.flvc.org/fcla/dt/13282 | |
Sublocation: | Digital Library | |
Use and Reproduction: | Copyright © is held by the author with permission granted to Florida Atlantic University to digitize, archive and distribute this item for non-profit research and educational purposes. Any reuse of this item in excess of fair use or other copyright exemptions requires permission of the copyright holder. | |
Use and Reproduction: | http://rightsstatements.org/vocab/InC/1.0/ | |
Host Institution: | FAU | |
Is Part of Series: | Florida Atlantic University Digital Library Collections. |