A novel mutation of CYP27B1 in two siblings with vitamin D-dependent rickets type 1A

2017 ◽  
Author(s):  
Zerrin Orbak
Keyword(s):  
Vitamin D ◽  
Novel Mutation

A Case of Hereditary Vitamin D-Resistant Rickets (HVDRR) without Alopecia: A Novel Mutation

2011 ◽  
pp. P2-116-P2-116
Author(s):  
Karen Eileen Huang ◽  
Peter J Malloy ◽  
Debra Jeandron ◽  
David Feldman ◽  
Pisit Pitukcheewanont
Keyword(s):  
Vitamin D ◽  
Novel Mutation ◽  
Vitamin D Resistant Rickets ◽  
Resistant Rickets

scholarly journals Hereditary 1,25-Dihydroxyvitamin D Resistant Rickets due to a Mutation Causing Multiple Defects in Vitamin D Receptor Function

Endocrinology ◽  
2004 ◽  
Vol 145 (11) ◽  
pp. 5106-5114 ◽  
Author(s):  
Peter J. Malloy ◽  
Rong Xu ◽  
Lihong Peng ◽  
Sara Peleg ◽  
Abdullah Al-Ashwal ◽  
...  
Keyword(s):  
Vitamin D ◽  
Ligand Binding ◽  
Vitamin D Receptor ◽  
Novel Mutation ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Retinoid X Receptor ◽  
Vdr Gene ◽  
Dihydroxyvitamin D3 ◽  
Resistant Rickets

Abstract Hereditary vitamin D-resistant rickets (HVDRR) is an autosomal recessive disease caused by mutations in the vitamin D receptor (VDR). We studied a young Saudi Arabian girl who exhibited the typical clinical features of HVDRR, but without alopecia. Analysis of her VDR gene revealed a homozygous T to C mutation in exon 7 that changed isoleucine to threonine at amino acid 268 (I268T). From crystallographic studies of the VDR ligand-binding domain, I268 directly interacts with 1,25-dihydroxyvitamin D3 [1,25(OH)2D3] and is involved in the hydrophobic stabilization of helix H12. We recreated the I268T mutation and analyzed its effects on VDR function. In ligand binding assays, the I268T mutant VDR exhibited an approximately 5- to 10-fold lower affinity for [3H]1,25(OH)2D3 compared with the wild-type (WT) VDR. The I268T mutant required approximately a 65-fold higher concentration of 1,25(OH)2D3 to be equipotent in gene transactivation. Both retinoid X receptor heterodimerization and coactivator binding were reduced in the I268T mutant. Analogs of 1,25(OH)2D3 have been proposed as potential therapeutics for patients with HVDRR. Interestingly, in protease sensitivity assays, treatment with the potent vitamin D analog, 20-epi-1,25(OH)2D3, stabilized I268T mutant proteolytic fragments better than 1,25(OH)2D3. Moreover, 20-epi-1,25(OH)2D3 restored transactivation of the I268T mutant to levels exhibited by WT VDR treated with 1,25(OH)2D3. In conclusion, we describe a novel mutation, I268T, in the VDR ligand-binding domain that alters ligand binding, retinoid X receptor heterodimerization, and coactivator binding. These combined defects in VDR function cause resistance to 1,25(OH)2D3 action and result in the syndrome of HVDRR.

Vitamin D-dependent rickets type 1 due to a novel mutation in CYP27B1

2017 ◽  
Author(s):  
Yael Levy-Shraga ◽  
Ben Pode-Shakked ◽  
Naomi Pode-Shakked ◽  
Ortal Barel ◽  
Jeffrey Jacobson ◽  
...  
Keyword(s):  
Vitamin D ◽  
Novel Mutation

Lightwood Syndrome Revisited with a Novel Mutation in CYP24 and Vitamin D Supplement Recommendations

2013 ◽  
Vol 163 (4) ◽  
pp. 1208-1210 ◽  
Author(s):  
Mireille Castanet ◽  
Eric Mallet ◽  
Marie-Laure Kottler
Keyword(s):  
Vitamin D ◽  
Novel Mutation ◽  
Vitamin D Supplement

Identification of a novel mutation in hereditary vitamin D resistant rickets causing exon skipping

1996 ◽  
Vol 45 (1) ◽  
pp. 85-92 ◽  
Author(s):  
N. S. Hawa ◽  
F. J. Cockerill ◽  
S. Vadher ◽  
M. Hewison ◽  
A. R. Rut ◽  
...  
Keyword(s):  
Vitamin D ◽  
Novel Mutation ◽  
Exon Skipping ◽  
Vitamin D Resistant Rickets ◽  
Resistant Rickets

scholarly journals A Case of Vitamin D-Dependent Rickets Type 1A with a Novel Mutation in the Uzbek Population

2016 ◽  
Vol 8 (4) ◽  
pp. 484-489 ◽  
Author(s):  
Bahar Özcabı ◽  
Feride Tahmiscioğlu Bucak ◽  
Sevinç Jaferova ◽  
Çiğdem Oruç ◽  
Amra Adrovic ◽  
...  
Keyword(s):  
Vitamin D ◽  
Novel Mutation
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