Typescript (photocopy)

Graduation date: 1994

The 1£\, 25-dihydroxyvitamin D3 (1,25(OH)2D3) is involved in various physiological processes, including calcium/phosphorous homeostasis, cell growth, differentiation and apoptosis. 1,25(OH)2D3 induces the formation of VDR/RXR complex to up-regulate or down-regulate target gene expression. Recent studies find that VDR undergoes several post-translational modifications, such as phosphorylation and ubiquitination, which may regulate its transcriptional activity and/or stability. In this study, we identified VDR as a new target for small ubiquitin-related modifier (SUMO)-2 modification in vitro. In E. coli. SUMO-conjugation system, VDR is mainly sumoylated at Lys-103. SUMOylation of VDR enhanced VDR/RXR-mediated transcriptional activation as determined by promoter activity assay. In addition, 1,25(OH)2D3-induced expression of osteopontin was attenuated after mutation of VDR SUMOylation site. However, chromatin immunoprecipitation assay indicated that wild type and K103A mutant of VDR bound to the osteopontin promoter with similar affinity. Collectivity, our results suggest that SUMOylation of VDR may affect its transcriptional activity by modulating the interaction between VDR and co-activators.

Thesis (M.S.)--University of Alabama at Birmingham, 2007. / Title from PDF title page (viewed Feb. 1, 2010). Includes bibliographical references (p. 19-24).

Thesis (Ph. D.)--Ohio State University, 1970. / Includes vita. Includes bibliographical references (leaves 67-77). Available online via OhioLINK's ETD Center.

Thesis (Ph. D.)--Ohio State University, 2004. / Title from first page of PDF file. Document formatted into pages; contains xii, 153 p.; also includes graphics. Includes abstract and vita. Advisor: Richard P. Swenson, Dept. of Biochemistry. Includes bibliographical references (p. 144-153).

Thesis (Ph. D.)--University of Texas at Austin, 2003. / Vita. Includes bibliographical references. Available from UMI Company.

Pyridoxal-5-phosphate (PLP), the active form of vitamin B6 (B6), is a co-factor for enzymes in macronutrient metabolism. Increasing protein intake may affect B6 by increasing PLP-dependent enzymes in amino acid metabolism, which may be more pronounced during moderate B6 deficiency. Decreased B6 status decreases PLP-dependent enzyme activity possibly altering macronutrient metabolism. We examined changing dietary carbohydrate: protein ratios in rats consuming recommended vs. moderately deficient intakes of pyridoxine (PN)-HCl, on plasma markers of B6 status and enzymes in intermediary metabolism. Marginal B6 deficiency decreased all plasma B6 vitamers except for pyridoxic acid. Protein intake (40% energy) significantly reduced plasma PN and tended to decrease plasma pyridoxal with no significant alterations in plasma homocysteine or cysteine. Hepatic cystathionine-γ-lyase, glycogen phosphorylase, plasma aspartate and alanine aminotransferase significantly decreased with marginal B6 deficiency and cystathionine-γ-lyase decreased with increasing protein intake. Marginal B6 deficiency significantly increased hepatic glycogen with no changes in plasma haptoglobin. / October 2015

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