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Quinoid dihydropteridine reductase

dihydropteridine reductase, DHPR
This gene encodes the enzyme dihydropteridine reductase, which catalyzes the NADH-mediated reduction of quinonoid dihydrobiopterin. This enzyme is an essential component of the pterin-dependent aromatic amino acid hydroxylating systems. Mutations in this gene resulting in QDPR deficiency include aberrant splicing, amino acid substitutions, insertions, or premature terminations. Dihydropteridine reductase deficiency presents as atypical phenylketonuria due to insufficient production of biopterin, a cofactor for phenylalanine hydroxylase. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, ACID, HAD, AGE, V1a
Papers on dihydropteridine reductase
In situ visualizing T-Tubule/SR junction reveals the ultra-structures of calcium storage and release machinery.
Yang et al., Shanghai, China. In Int J Biol Macromol, Jan 2016
The T-Tubule/SR junction comprises two membrane systems: the integral proteins DHPR and RyR1 and the Ca(2+)-buffering apparatus within the SR lumen.
Effect of sophoridine on Ca(2+) induced Ca(2+) release during heart failure.
Yang et al., Yinchuan, China. In Physiol Res, Dec 2015
We investigated the Ca(2+) induced Ca(2+) transients and assessed the expression of ryanodine receptor (RyR2) and L-type Ca(2+) channel (dihydropyridine receptor, DHPR).
[A genome-wide association study on body weight traits of Jinghai yellow chicken].
Gu et al., Yangzhou, China. In Yi Chuan, Aug 2015
Finally, nine candidate genes were obtained, among which four genes of FAM124A (Family with sequence similarity 124A), QDPR (Quinoid dihydropteridine reductase), WDR1 (WD repeat domain 1) and SLC2A9 (Solute carrier family 2 (facilitated glucose transporter), member 9) might be important candidate genes influencing body weight traits of Jinghai yellow chicken.
The disorders of the calcium release unit of skeletal muscles: what have we learned from mouse models?
Cancellara et al., Padova, Italy. In J Muscle Res Cell Motil, Feb 2015
The release from the Sarcoplasmic Reticulum stores (SR) is handled by a multiprotein complex called Calcium Release Unit and composed of DiHydroPyridine Receptor or DHPR, Ryanodine Receptor or RYR, Calsequestrin or CASQ, junctin, Triadin, Junctophilin and Mitsugumin 29.
Eps 15 Homology Domain (EHD)-1 Remodels Transverse Tubules in Skeletal Muscle.
McNally et al., Omaha, United States. In Plos One, 2014
The disorganized T-tubule structures in Ehd1-heterozygous muscle were accompanied by marked elevation of the T-tubule-associated protein DHPR and reduction of the triad linker protein junctophilin 2, reflecting defective triads.
Localized nuclear and perinuclear Ca(2+) signals in intact mouse skeletal muscle fibers.
Fink et al., Heidelberg, Germany. In Front Physiol, 2014
To investigate which type of Ca(2+) channels contribute to the Ca(2+) signals associated with nuclei in skeletal muscle fibers, we performed measurements with the RyR blocker dantrolene, the DHPR blocker nifedipine or the IP3R blocker Xestospongin C. We observed Ca(2+) signals associated with nuclei in the presence of each blocker.
Skeletal muscle excitation-contraction coupling: who are the dancing partners?
Dulhunty et al., Canberra, Australia. In Int J Biochem Cell Biol, 2014
This role of beta subunit remains to be fully investigated as well as the degree to which it may complement any other direct or indirect voltage-dependent coupling interactions between the DHPR alpha II-III loop and the ryanodine receptor.
Monoamine neurotransmitter deficiencies.
Pearl, Washington, D.C., United States. In Handb Clin Neurol, 2012
Disorders detectable by elevated serum phenylalanine are deficiencies of GTP cyclohydrolase (homozygous), pterin-carbinolamine dehydratase, dihydropteridine reductase, and pyruvoyl-tetrahydropterin synthase.
Junctophilin 1 and 2 proteins interact with the L-type Ca2+ channel dihydropyridine receptors (DHPRs) in skeletal muscle.
Sorrentino et al., Siena, Italy. In J Biol Chem, 2012
JP1 and JP2 can facilitate the assembly of DHPR with other proteins of the excitation-contraction coupling machinery
Reciprocal dihydropyridine and ryanodine receptor interactions in skeletal muscle activation.
Fraser et al., Cambridge, United Kingdom. In J Muscle Res Cell Motil, 2011
Dihydropyridine (DHPR) and ryanodine receptors (RyRs) are central to transduction of transverse (T) tubular membrane depolarisation initiated by surface action potentials into release of sarcoplasmic reticular (SR) Ca2+ in skeletal muscle excitation-contraction coupling.
The elusive role of the SPRY2 domain in RyR1.
Dulhunty et al., Australia. In Channels (austin), 2011
the electrostatic regulatory interaction between the SPRY2 F loop residues (that bind to imperatoxin A) and the ASI/basic residues of RyR1 does not influence bi-directional DHPR-RyR1 signaling during skeletal EC coupling
Proteome analysis of the thalamus and cerebrospinal fluid reveals glycolysis dysfunction and potential biomarkers candidates for schizophrenia.
Turck et al., München, Germany. In J Psychiatr Res, 2010
This protein has been found differentially expressed in thalami from patients with schizophrenia.
Diagnosis, classification, and genetics of phenylketonuria and tetrahydrobiopterin (BH4) deficiencies.
Lichter-Konecki et al., Zürich, Switzerland. In Mol Genet Metab, 2010
Dried blood spots are the best sample for the simultaneous measurement of amino acids (phenylalanine and tyrosine), pterins (neopterin and biopterin), and dihydropteridine reductase activity from a single specimen.
Dihydropteridine reductase activity in the brainstem of intrauterine growth-restricted rats.
Hernandez-Rodriguez et al., Mexico. In Int J Dev Neurosci, 2010
Data show that intrauterine growth restriction increases serotonin biosynthesis in the brainstem, which is accompanied by an increase in dihydropteridine reductase activity that may be a compensatory mechanism to maintain sufficient tetrahydrobiopterin.
Diminished expression of dihydropteridine reductase is a potent biomarker for hypertensive vessels.
Kim et al., South Korea. In Proteomics, 2009
results suggest that the deficiency in tetrahydrobiopterin regeneration produced by diminished dihydrobiopterin reductase expression is involved in vascular disorders in hypertensive rats.
Ryanodine receptors of striated muscles: a complex channel capable of multiple interactions.
Protasi et al., Philadelphia, United States. In Physiol Rev, 1997
Skeletal and cardiac muscles contain different RyR and DHPR isoforms and both contribute to the diversity in cardiac and skeletal excitation-contraction coupling mechanisms.
Enhanced dihydropyridine receptor channel activity in the presence of ryanodine receptor.
Allen et al., Kyoto, Japan. In Nature, 1996
The skeletal isoform of the ryanodine receptor (RyR-1) functions as the Ca2+-release channel and the dihydropyridine receptor (DHPR) functions as the voltage sensor and also as an L-type Ca2+ channel.
Disturbance of cerebral function by aluminium in haemodialysis patients without overt aluminium toxicity.
Marsh et al., London, United Kingdom. In Lancet, 1989
The mean activity of erythrocyte dihydropteridine reductase (DHPR), which is inhibited by aluminium, rose during 3 months' desferrioxamine treatment in most of the 15 patients so treated.
Serum aluminum levels and erythrocyte dihydropteridine reductase activity in patients on hemodialysis.
Marsh et al., In N Engl J Med, 1987
The enzyme dihydropteridine reductase (DHPR) is essential for the maintenance of normal brain concentrations of tetrahydrobiopterin, which is itself required for the synthesis of specific neurotransmitters.
Inhibition of dihydropteridine reductase by novel 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine analogs.
Brossi et al., In Science, 1984
Hydroxylated derivatives of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), a nigrostriatal neurotoxin in humans and primates, noncompetitively inhibited dihydropteridine reductase from human liver and rat striatal synaptosomes in vitro at micromolar concentrations.
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