Characterization of mutant and normal thyroid hormone receptor complexes by electrophoretic mobility shift assay / by Tammy L. Bone.
| Author/creator | Bone, Tammy L. author. |
| Other author | Usala, Stephen J., degree supervisor. |
| Other author | East Carolina University. Department of Biology. |
| Format | Theses and dissertations |
| Production | 1995. |
| Description | vi, 54 leaves, 7 unnumbered leaves of plates : illustrations ; 28 cm |
| Supplemental Content | Access via ScholarShip |
| Subjects |
| Summary | Generalized Resistance to Thyroid Hormone (GRTH), the most common form of thyroid hormone resistance, is caused by a single amino acid mutation within the c-erbA-[beta] thyroid hormone receptor gene that produces dominant negative proteins. Dominant negative receptors partially elicit their effect by dimerizing with normal receptors and decreasing the total concentration of functional complexes available for binding to the DNA in promoter regions of thyroid hormone responsive genes. These functional DNA-binding complexes are referred to as monomers, homodimers, and heterodimers, and can be visualized by using the Electrophoretic Mobility Shift Assay (Gel-Shift). The DNA-binding properties of a panel of mutant thyroid hormone receptors with various phenotypes revealed that homodimers were mediators of dominant negative activity when their binding was studied on model DNA sequences. Similar dimerization properties were reported for the two mildly dominant negative receptors, GH and CL, when studied on model thyroid hormone response elements (TREs), Both of these receptors had an arginine residue replaced by histidine. Different results were observed when DNA-binding properties of mutant and normal receptors were studied on mutational variants of the native promoter, [alpha]Myosin Heavy Chain. This is suggestive that other receptor properties may be determining differential binding patterns to the [alpha]MHC Also, this study used gel-shift analysis to characterize the WT-[beta]1 thyroid hormone receptor monoclonal antibody. The antibody demonstrated a preference for binding and supershifting homodimer versus heterodimer complexes. |
| General note | Submitted to the faculty of the Department of Biology. |
| General note | Advisor: Stephen J. Usala |
| Dissertation note | M.S. East Carolina University 1995 |
| Bibliography note | Includes bibliographical references (leaves 51-54). |
| Genre/form | Academic theses. |
| Genre/form | Academic theses. |
| Genre/form | Thèses et écrits académiques. |
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|---|---|---|---|---|
| Joyner | University Archives | ASK AT SPECIAL COLLECTIONS DESK | ✔ Available | Request Material |
| Electronic Resources | Access Content Online | ✔ Available |