Affiliation: University of New Mexico
- Hydroxylase enzymes of the vitamin D pathway: expression, function, and regulationJohn L Omdahl
Department of Biochemistry and Molecular Biology, University of New Mexico, Albuquerque, New Mexico 87131 5221, USA
Annu Rev Nutr 22:139-66. 2002..The regulatory complex is assembled on vitamin D response elements in the proximal promoter of the P450C24 gene and functions to increase the transcription rate...
- Expression, structure-function, and molecular modeling of vitamin D P450sJ L Omdahl
Department of Biochemistry and Molecular Biology, University of New Mexico School of Medicine, Albuquerque, New Mexico 87131 5221, USA
J Cell Biochem 88:356-62. 2003..Expression and characterization of purified recombinant rat CYP24 is discussed in light of mutations directed at the enzyme's active site...
- Hybrid homology modeling and mutational analysis of cytochrome P450C24A1 (CYP24A1) of the Vitamin D pathway: insights into substrate specificity and membrane bound structure-functionAndrew J Annalora
Department of Biochemistry and Molecular Biology, University of New Mexico School of Medicine, Albuquerque, NM 87131 5331, USA
Arch Biochem Biophys 460:262-73. 2007..We hypothesize that CYP24A1 has evolved a unique amino-terminal membrane-binding motif that contributes to substrate specificity and docking through coordinated interactions with the vitamin D A-ring...
- Basal and parathyroid hormone induced expression of the human 25-hydroxyvitamin D 1alpha-hydroxylase gene promoter in kidney AOK-B50 cells: role of Sp1, Ets and CCAAT box protein binding sitesXiu Hui Gao
Department of Molecular Biosciences, University of Adelaide, SA, Adelaide, Australia
Int J Biochem Cell Biol 34:921-30. 2002....
- Role of MAP kinases in the 1,25-dihydroxyvitamin D3-induced transactivation of the rat cytochrome P450C24 (CYP24) promoter. Specific functions for ERK1/ERK2 and ERK5Prem P Dwivedi
Department of Molecular Biosciences Biochemistry, University of Adelaide, Adelaide, Australia 5005
J Biol Chem 277:29643-53. 2002..The ERK1/ERK2 and ERK5 modules provide a novel mechanism for linking the rapid signal transduction and slower transcription actions of 1,25D to induce CYP24 gene expression...
- Rat cytochrome P450C24 (CYP24A1) and the role of F249 in substrate binding and catalytic activityAndrew Annalora
Department of Biochemistry and Molecular Biology, University of New Mexico School of Medicine, Albuquerque, NM 87131-5221, USA
Arch Biochem Biophys 425:133-46. 2004..Therefore, Phe-249 within the F-helix was demonstrated to have an important role in properly binding and aligning substrate in the CYP24A1 active site for C(23) and C(24) oxidation reactions...
- Molecular action of 1,25-dihydroxyvitamin D3 and phorbol ester on the activation of the rat cytochrome P450C24 (CYP24) promoter: role of MAP kinase activities and identification of an important transcription factor binding siteBarbara K Nutchey
School of Molecular and Biomedical Science, University of Adelaide, Adelaide, SA 5000, Australia
Biochem J 389:753-62. 2005..This is the first report to identify the DNA binding sequences required for the synergy between PMA and 1,25D and a role for JNK on the CYP24 gene promoter...
- Identification of growth factor independent-1 (GFI1) as a repressor of 25-hydroxyvitamin D 1-alpha hydroxylase (CYP27B1) gene expression in human prostate cancer cellsPrem P Dwivedi
School of Molecular and Biomedical Science, University of Adelaide, Adelaide, South Australia, 5005, Australia
Endocr Relat Cancer 12:351-65. 2005..These studies provide the basis for a more detailed understanding of CYP27B1 repression in prostate cancer cells and could provide a novel insight in future diagnosis and treatment...
- UNM Human Subjects Research Enhancement ProgramJohn Omdahl; Fiscal Year: 2002..The UNMHSC Human Research Review Committee Administrative Office has been allocated additional space for its staff. Funds to support the costs of renovation of this space are requested. ..
- VITAMIN D P450 FUNCTION--NATURAL & DIRECTED MUTAGENESISJohn Omdahl; Fiscal Year: 2002....