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CYP27B1  -  cytochrome P450, family 27, subfamily B,...

Homo sapiens

 
 
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Disease relevance of CYP27B1

 

Psychiatry related information on CYP27B1

 

High impact information on CYP27B1

 

Chemical compound and disease context of CYP27B1

 

Biological context of CYP27B1

  • Rescue of the pseudo-vitamin D deficiency rickets phenotype of CYP27B1-deficient mice by treatment with 1,25-dihydroxyvitamin D3: biochemical, histomorphometric, and biomechanical analyses [14].
  • The regulation of the gene for renal 25-hydroxyvitamin D 1alpha- hydroxylase (1alpha(OH)ase; CYP27B1) by parathyroid hormone (PTH) under hypocalcemic conditions is fundamentally important for the maintenance of calcium and phosphate homeostasis [15].
  • We propose that the formation of such a repressive complex on the inhibitory domain of the CYP27B1 gene in prostate cancer cells could lead to silencing of either the nearby enhancer or proximal promoter domains and lead to cancer progression by reducing local production of 1,25D [2].
  • First, we identify a repressive region between -997 and -1200 in the human CYP27B1 promoter following transient transfection analysis in the prostate cancer cell lines DU145, PC3 and LNCaP [2].
  • BACKGROUND: CYP27B1 hydroxylase catalyzes the conversion of 25 hydroxyvitamin D(3) (25OHD(3)) to 1,25(OH)(2)D(3), the most active natural vitamin D metabolite, which plays a role in the regulation of immunity and cell proliferation [4].
 

Anatomical context of CYP27B1

  • A cell line was treated with calcitriol to determine the effect on the expression of CYP27B1, 1alpha,25-dihydroxyvitamin D(3)-24-hydroxylase (CYP24), and vitamin D(3) receptor (VDR) [1].
  • Human mammary epithelial cells express CYP27B1 and are growth inhibited by 25-hydroxyvitamin D-3, the major circulating form of vitamin D-3 [3].
  • In contrast, basal 1alpha-hydroxylase CYP27B1 expression levels were found to be 65% higher in the colon than in the small intestine (P < 0.02) [16].
  • Besides the almost universal presence of VDRs, some cell types (e.g. keratinocytes, monocytes, bone, placenta) are capable of metabolizing 25-hydroxyvitamin D to 1,25(OH)(2)D by the enzyme 1alpha-hydroxylase (CYP27B1) [17].
  • The aim of this study was to investigate what factors regulate expression of the CYP27B1 gene in osteoblast cells [18].
 

Associations of CYP27B1 with chemical compounds

 

Physical interactions of CYP27B1

 

Regulatory relationships of CYP27B1

  • 1alpha,25-Dihydroxyvitamin D(3) downregulates CYP27B1 and induces CYP24A1 in colon cells [20].
  • PTH and forskolin stimulated CYP1alpha promoter activity via a cAMP-dependent pathway acting through the phosphorylation of CREB (cAMP-dependent response element-binding protein) [21].
 

Other interactions of CYP27B1

  • Human placenta synthesizes and metabolizes 1,25-dihydroxyvitamin D(3) [1,25(OH)(2)D(3)/calcitriol] through the activity of 25-hydroxyvitamin D(3)-1alpha-hydroxylase (CYP27B1) and 1,25(OH)(2)D(3)-24-hydroxylase (CYP24A1), the two key enzymes for Vitamin D metabolism [22].
  • In contrast, UVB and calcitriol had no effect on gene expression of CYP27A1 and CYP27B1 [23].
  • CYP2R1-, CYP27B1- and CYP24-mRNA expression in German type 1 diabetes patients [24].
  • Our results implicate TOM1L2 and CYP27B1 as having roles as novel targets for the 17p and 12q amplicons, respectively [25].
  • Further subtraction of normal endothelium, bone marrow, white blood cell and other normal tissue transcripts resulted in just three gene transcripts, ANAPC10, PLXDC1(TEM7), and CYP27B1, that are highly specific to GBM-ECs [26].
 

Analytical, diagnostic and therapeutic context of CYP27B1

  • Using Western blot and quantitative real-time PCR, CYP27B1 mRNA and protein were detected in immortalized, nontumorigenic human mammary epithelial cell (HMEC) cultures [3].
  • In the research presented here, we have investigated the influence of UVB-triggered calcitriol production on gene expression of the vitamin D3 hydroxylating enzymes catabolic 25-hydroxyvitamin-D3-24-hydroxylase (CYP24A1), active vitamin-D3-25-hydroxylase (CYP27A1), and 25-hydroxyvitamin-D3-1alpha-hydroxylase (CYP27B1) using real-time PCR [23].
  • As shown by HPLC, CYP27B1 is active only if basal 24-hydroxylation is not maximally functional [20].
  • Although the sequence alignment suggested that Arg107, Gly125, and Pro497 of CYP27B1 might be involved in substrate binding, the experimental data strongly suggested that mutations of these amino-acid residues destroyed the tertiary structure of the substrate-heme pocket [27].
  • We have previously engineered an animal model of PDDR by targeted inactivation of the 1alpha-OHase gene in mice [14].

References

  1. Vitamin D(3) metabolism in human glioblastoma multiforme: functionality of CYP27B1 splice variants, metabolism of calcidiol, and effect of calcitriol. Diesel, B., Radermacher, J., Bureik, M., Bernhardt, R., Seifert, M., Reichrath, J., Fischer, U., Meese, E. Clin. Cancer Res. (2005) [Pubmed]
  2. Identification of growth factor independent-1 (GFI1) as a repressor of 25-hydroxyvitamin D 1-alpha hydroxylase (CYP27B1) gene expression in human prostate cancer cells. Dwivedi, P.P., Anderson, P.H., Omdahl, J.L., Grimes, H.L., Morris, H.A., May, B.K. Endocr. Relat. Cancer (2005) [Pubmed]
  3. Human mammary epithelial cells express CYP27B1 and are growth inhibited by 25-hydroxyvitamin D-3, the major circulating form of vitamin D-3. Kemmis, C.M., Salvador, S.M., Smith, K.M., Welsh, J. J. Nutr. (2006) [Pubmed]
  4. A promoter polymorphism of the CYP27B1 gene is associated with Addison's disease, Hashimoto's thyroiditis, Graves' disease and type 1 diabetes mellitus in Germans. Lopez, E.R., Zwermann, O., Segni, M., Meyer, G., Reincke, M., Seissler, J., Herwig, J., Usadel, K.H., Badenhoop, K. Eur. J. Endocrinol. (2004) [Pubmed]
  5. Is vitamin D hypothesis for schizophrenia valid? Independent segregation of psychosis in a family with vitamin-D-dependent rickets type IIA. Ozer, S., Uluşahin, A., Ulusoy, S., Okur, H., Coşkun, T., Tuncali, T., Göğüş, A., Akarsu, A.N. Prog. Neuropsychopharmacol. Biol. Psychiatry (2004) [Pubmed]
  6. Electroconvulsive therapy (ECT) in a patient with a dual-chamber sensing, VDDR pacemaker. Giltay, E.J., Kho, K.H., Keijzer, L.T., Leijenaar, M., van Schaick, H.W., Blansjaar, B.A. The journal of ECT. (2005) [Pubmed]
  7. A novel protein complex that interacts with the vitamin D3 receptor in a ligand-dependent manner and enhances VDR transactivation in a cell-free system. Rachez, C., Suldan, Z., Ward, J., Chang, C.P., Burakov, D., Erdjument-Bromage, H., Tempst, P., Freedman, L.P. Genes Dev. (1998) [Pubmed]
  8. Vitamin D receptor genotype is associated with radiographic osteoarthritis at the knee. Uitterlinden, A.G., Burger, H., Huang, Q., Odding, E., Duijn, C.M., Hofman, A., Birkenhäger, J.C., van Leeuwen, J.P., Pols, H.A. J. Clin. Invest. (1997) [Pubmed]
  9. Linkage disequilibrium analysis in young populations: pseudo-vitamin D-deficiency rickets and the founder effect in French Canadians. Labuda, M., Labuda, D., Korab-Laskowska, M., Cole, D.E., Zietkiewicz, E., Weissenbach, J., Popowska, E., Pronicka, E., Root, A.W., Glorieux, F.H. Am. J. Hum. Genet. (1996) [Pubmed]
  10. Linkage mapping by simultaneous screening of multiple polymorphic loci using Alu oligonucleotide-directed PCR. Zietkiewicz, E., Labuda, M., Sinnett, D., Glorieux, F.H., Labuda, D. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  11. Genistein inhibits vitamin D hydroxylases CYP24 and CYP27B1 expression in prostate cells. Farhan, H., Wähälä, K., Cross, H.S. J. Steroid Biochem. Mol. Biol. (2003) [Pubmed]
  12. Novel mutations in the 1alpha-hydroxylase (P450c1) gene in three families with pseudovitamin D-deficiency rickets resulting in loss of functional enzyme activity in blood-derived macrophages. Smith, S.J., Rucka, A.K., Berry, J.L., Davies, M., Mylchreest, S., Paterson, C.R., Heath, D.A., Tassabehji, M., Read, A.P., Mee, A.P., Mawer, E.B. J. Bone Miner. Res. (1999) [Pubmed]
  13. Sequence variants in the human 25-hydroxyvitamin D3 1-alpha-hydroxylase (CYP27B1) gene are not associated with prostate cancer risk. Hawkins, G.A., Cramer, S.D., Zheng, S.L., Isaacs, S.D., Wiley, K.E., Chang, B.L., Bleecker, E.R., Walsh, P.C., Meyers, D.A., Isaacs, W.B., Xu, J. Prostate (2002) [Pubmed]
  14. Rescue of the pseudo-vitamin D deficiency rickets phenotype of CYP27B1-deficient mice by treatment with 1,25-dihydroxyvitamin D3: biochemical, histomorphometric, and biomechanical analyses. Dardenne, O., Prudhomme, J., Hacking, S.A., Glorieux, F.H., St-Arnaud, R. J. Bone Miner. Res. (2003) [Pubmed]
  15. 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 sites. Gao, X.H., Dwivedi, P.P., Choe, S., Alba, F., Morris, H.A., Omdahl, J.L., May, B.K. Int. J. Biochem. Cell Biol. (2002) [Pubmed]
  16. Calcitriol regulates the expression of the genes encoding the three key vitamin D3 hydroxylases and the drug-metabolizing enzyme CYP3A4 in the human fetal intestine. Theodoropoulos, C., Demers, C., Delvin, E., Ménard, D., Gascon-Barré, M. Clin. Endocrinol. (Oxf) (2003) [Pubmed]
  17. Vitamin D and cancer. Bouillon, R., Eelen, G., Verlinden, L., Mathieu, C., Carmeliet, G., Verstuyf, A. J. Steroid Biochem. Mol. Biol. (2006) [Pubmed]
  18. Regulation of the CYP27B1 5'-flanking region by transforming growth factor-beta in ROS 17/2.8 osteoblast-like cells. Turner, A.G., Dwivedi, P.P., May, B.K., Morris, H.A. J. Steroid Biochem. Mol. Biol. (2007) [Pubmed]
  19. RNAi-mediated silencing of CYP27B1 abolishes 1,25(OH)(2)D(3) synthesis and reduces osteocalcin and CYP24 mRNA expression in human osteosarcoma (HOS) cells. Anderson, P.H., Atkins, G.J., Findlay, D.M., Oloughlin, P.D., Welldon, K., Vincent, C., Morris, H.A. J. Steroid Biochem. Mol. Biol. (2007) [Pubmed]
  20. 1alpha,25-Dihydroxyvitamin D(3) downregulates CYP27B1 and induces CYP24A1 in colon cells. Lechner, D., K??llay, E., Cross, H.S. Mol. Cell. Endocrinol. (2007) [Pubmed]
  21. Hormonal regulation of 25-hydroxyvitamin D3-1alpha-hydroxylase and 24-hydroxylase gene transcription in opossum kidney cells. Armbrecht, H.J., Hodam, T.L., Boltz, M.A. Arch. Biochem. Biophys. (2003) [Pubmed]
  22. Regulation of Vitamin D hydroxylases gene expression by 1,25-dihydroxyvitamin D(3) and cyclic AMP in cultured human syncytiotrophoblasts. Avila, E., D??az, L., Barrera, D., Halhali, A., M??ndez, I., Gonz??lez, L., Zuegel, U., Steinmeyer, A., Larrea, F. J. Steroid Biochem. Mol. Biol. (2007) [Pubmed]
  23. Wavelength-dependent induction of CYP24A1-mRNA after UVB-triggered calcitriol synthesis in cultured human keratinocytes. B??r, M., Domaschke, D., Meye, A., Lehmann, B., Meurer, M. J. Invest. Dermatol. (2007) [Pubmed]
  24. CYP2R1-, CYP27B1- and CYP24-mRNA expression in German type 1 diabetes patients. Ramos-Lopez, E., Brück, P., Jansen, T., Pfeilschifter, J.M., Radeke, H.H., Badenhoop, K. J. Steroid Biochem. Mol. Biol. (2007) [Pubmed]
  25. Gene amplifications in osteosarcoma-CGH microarray analysis. Atiye, J., Wolf, M., Kaur, S., Monni, O., Böhling, T., Kivioja, A., Tas, E., Serra, M., Tarkkanen, M., Knuutila, S. Genes Chromosomes Cancer (2005) [Pubmed]
  26. PLXDC1 (TEM7) is identified in a genome-wide expression screen of glioblastoma endothelium. Beaty, R.M., Edwards, J.B., Boon, K., Siu, I.M., Conway, J.E., Riggins, G.J. J. Neurooncol. (2007) [Pubmed]
  27. Structure-function analysis of CYP27B1 and CYP27A1. Studies on mutants from patients with vitamin D-dependent rickets type I (VDDR-I) and cerebrotendinous xanthomatosis (CTX). Sawada, N., Sakaki, T., Kitanaka, S., Kato, S., Inouye, K. Eur. J. Biochem. (2001) [Pubmed]
 
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