Function of Vitamin D Metabolites and Bone Disease

Haussler, Mark R.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS)
• Type: Research Project (R01)
• Project #: 3R01AR015781-16S1
• Application #: 3154841
• Study Section: Physiology Study Section (PHY)
• Project Start: 1975-01-01
• Project End: 1989-12-31
• Budget Start: 1987-01-01
• Budget End: 1987-12-31
• Support Year: 16
• Fiscal Year: 1987

Institution

• Name: University of Arizona
• Type: Schools of Medicine
• City: Tucson
• State: AZ
• Country: United States
• Zip Code: 85722

Publications

Jurutka, P W; Remus, L S; Whitfield, G K et al. (2000) The polymorphic N terminus in human vitamin D receptor isoforms influences transcriptional activity by modulating interaction with transcription factor IIB. Mol Endocrinol 14:401-20

Thompson, P D; Jurutka, P W; Haussler, C A et al. (1998) Heterodimeric DNA binding by the vitamin D receptor and retinoid X receptors is enhanced by 1,25-dihydroxyvitamin D3 and inhibited by 9-cis-retinoic acid. Evidence for allosteric receptor interactions. J Biol Chem 273:8483-91

Haussler, M R; Haussler, C A; Jurutka, P W et al. (1997) The vitamin D hormone and its nuclear receptor: molecular actions and disease states. J Endocrinol 154 Suppl:S57-73

Jurutka, P W; Hsieh, J C; Remus, L S et al. (1997) Mutations in the 1,25-dihydroxyvitamin D3 receptor identifying C-terminal amino acids required for transcriptional activation that are functionally dissociated from hormone binding, heterodimeric DNA binding, and interaction with basal transcription facto J Biol Chem 272:14592-9

Whitfield, G K; Selznick, S H; Haussler, C A et al. (1996) Vitamin D receptors from patients with resistance to 1,25-dihydroxyvitamin D3: point mutations confer reduced transactivation in response to ligand and impaired interaction with the retinoid X receptor heterodimeric partner. Mol Endocrinol 10:1617-31

Jurutka, P W; Hsieh, J C; Nakajima, S et al. (1996) Human vitamin D receptor phosphorylation by casein kinase II at Ser-208 potentiates transcriptional activation. Proc Natl Acad Sci U S A 93:3519-24

Nakajima, S; Hsieh, J C; Jurutka, P et al. (1996) Examination of the potential functional role of conserved cysteine residues in the hormone binding domain of the human 1,25-dihydroxyvitamin D3 receptor. J Biol Chem 271:5143-9

Ray, R; Swamy, N; MacDonald, P N et al. (1996) Affinity labeling of the 1 alpha,25-dihydroxyvitamin D3 receptor. J Biol Chem 271:2012-7

Hsieh, J C; Nakajima, S; Galligan, M A et al. (1995) Receptor mediated genomic action of the 1,25(OH)2D3 hormone: expression of the human vitamin D receptor in E. coli. J Steroid Biochem Mol Biol 53:583-94

Whitfield, G K; Hsieh, J C; Jurutka, P W et al. (1995) Genomic actions of 1,25-dihydroxyvitamin D3. J Nutr 125:1690S-1694S