Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Escherichia coli biotin ligase can attach biotin molecules to a lysine residue of biotin acceptor peptide (BAP), and biotinylation of particular BAP-fused proteins in cells was carried out by coexpression of E. coli biotin ligase (in vivo biotinylation). This in vivo biotinylation technology has been applied for protein purification, analysis of protein localization, and protein-protein interaction in eukaryotic cells, while such studies have not been reported in bacterial cells. In this study, in vivo biotinylation of bacterial magnetic particles (BacMPs) synthesized by Magnetospirillum magneticum AMB-1 was attempted by heterologous expression of E. coli biotin ligase. To biotinylate BacMPs in vivo, BAP was fused to a BacMP surface protein, Mms13, and E. coli biotin ligase was simultaneously expressed in the truncated form lacking the DNA-binding domain. This truncation-based approach permitted the growth of AMB-1 transformants when biotin ligase was heterologously expressed. In vivo biotinylation of BAP on BacMPs was confirmed using an alkaline phosphatase-conjugated antibiotin antibody. The biotinylated BAP-displaying BacMPs were then exposed to streptavidin by simple mixing. The streptavidin-binding capacity of BacMPs biotinylated in vivo was 35-fold greater than that of BacMPs biotinylated in vitro, where BAP-displaying BacMPs purified from bacterial cells were biotinylated by being mixed with E. coli biotin ligase. This study describes not only a simple method to produce biotinylated nanomagnetic particles but also a possible expansion of in vivo biotinylation technology for bacterial investigation.
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PMID:In vivo biotinylation of bacterial magnetic particles by a truncated form of Escherichia coli biotin ligase and biotin acceptor peptide. 2062 27

Hereditary vitamin D-resistant rickets (HVDRR) is a rare autosomal recessive disorder characterized by severe rickets, hypocalcemia, hypophosphatemia, secondary hyperparathyroidism, and elevated alkaline phosphatase. This disorder is caused by homogeneous or heterogeneous mutations affecting the function of the vitamin D receptor (VDR), which lead to complete or partial target organ resistance to the action of 1,25-dihydroxy vitamin D. A non-consanguineous family of Chinese Han origin with one affected individual demonstrating HVDRR was recruited, with the proband evaluated clinically, biochemically and radiographically. To identify the presence of mutations in the VDR gene, all the exons and exon-intron junctions of the VDR gene from all family members were amplified using PCR and sequenced. The proband showed rickets, progressive alopecia, hypocalcemia, hypophosphatemia, secondary hyperparathyroidism, and elevated alkaline phosphatase. She also suffered from epilepsy, which is rarely seen in patients with HVDRR. Direct sequencing analysis revealed a homozygous missense mutation c.122G>A (p.C41Y) in the VDR gene of the proband, which is located in the first zinc finger of the DNA-binding domain. Both parents had a normal phenotype and were found to be heterozygous for this mutation. We report a Chinese Han family with one individual affected with HVDRR. A homozygous missense mutation c.122G>A (p.C41Y) in the VDR gene was found to be responsible for the patient's syndrome. In contrast to the results of treatment of HVDRR in other patients, our patient responded well to a supplement of oral calcium and a low dose of calcitriol.
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PMID:Clinical and genetic findings in a Chinese family with VDR-associated hereditary vitamin D-resistant rickets. 2740 66

Background Hereditary vitamin D resistant rickets (HVDRR) is a bone disorder characterized by a phenotype of rickets with onset at early stage of life with elevated alkaline phosphatase, hypocalcemia, hypophosphatemia, hyperparathyroidism and elevated levels of 1,25-dihydroxyvitamin D (calcitriol) as a consequence of the resistance of the vitamin D receptor (VDR). Mutations in the DNA-binding domain of the VDR of the vitamin D receptor have been characterized by a lack of response to traditional treatment with calcium and calcitriol. Secondary hyperparathyroidism and hypophosphatemia are the main factors in its pathogenesis. Cinacalcet is a calciomimetic drug that reproduces the action of calcium by increasing the sensitivity of the calcium-sensitive receptors (CASR) of the parathyroid glands that regulate the secretion of the parathyroid hormone (PTH). Case presentation We describe its effectiveness and safety in a patient with HVDRR and review other published report cases in the literature. According to published experience, cinacalcet could be used as an adjunctive treatment for the HVDRR with mutations in the DNA-binding domain of the VDR refractory to traditional treatment. Due to lack of knowledge of possible effects of cinacalcet on CASR in the skeleton, long-term use should be avoided. Conclusions The optimal dose of cinacalcet for treatment of HVDRR ranges between 0.25 and 0.5 mg/kg/day. Serious side effects of cinacalcet have not been published in this type of patient, although we considered that a close monitoring is necessary in order to detect hypocalcemia.
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PMID:Cinacalcet treatment experience in hereditary vitamin D resistant rickets. 3192 93


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