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gamma-butyrobetaine dioxygenase, as a gamma-butyrobetaine hydroxylase, B-box-1
Top mentioned proteins: PPAR, V1a, ACID, HAD, STEP
Papers on gamma-butyrobetaine dioxygenase
Expression and purification of active, stabilized trimethyllysine hydroxylase.
Tars et al., Rīga, Latvia. In Protein Expr Purif, 2014
Previous efforts have been devoted towards the inhibition of gamma-butyrobetaine dioxygenase, which catalyses the last step in carnitine biosynthesis.
Selective inhibition of OCTN2 is more effective than inhibition of gamma-butyrobetaine dioxygenase to decrease the availability of l-carnitine and to reduce myocardial infarct size.
Dambrova et al., Rīga, Latvia. In Pharmacol Res, 2014
l-Carnitine is a cofactor in the energy metabolism pathways where it drives the uptake and oxidation of long chain fatty acids (LCFA) by mitochondria.
Mouse γ-butyrobetaine dioxygenase is regulated by peroxisome proliferator-activated receptor α through a PPRE located in the proximal promoter.
Eder et al., Gießen, Germany. In Biochem Pharmacol, 2011
study clearly shows that mouse gamma-butyrobetaine dioxygenase is a direct PPARalpha target gene
Carnitine synthesis and uptake into cells are stimulated by fasting in pigs as a model of nonproliferating species.
Eder et al., Halle, Germany. In J Nutr Biochem, 2009
Fasted pigs had a higher activity of gamma-butyrobetaine dioxygenase (BBD), enzyme that catalyses the last step of carnitine biosynthesis in liver and kidney, and higher relative mRNA concentrations of OCTN2, the most important carnitine transporter, in liver, kidney, skeletal muscle, and small intestinal mucosa than control pigs (P<.05).
Hepatic uptake of gamma-butyrobetaine, a precursor of carnitine biosynthesis, in rats.
Tamai et al., Kanazawa, Japan. In Am J Physiol Gastrointest Liver Physiol, 2009
Gamma-butyrobetaine (GBB) is a precursor in the biosynthesis of carnitine, which plays an important role in the beta-oxidation of fatty acids, and is converted to carnitine by gamma-butyrobetaine dioxygenase (BBD) predominantly in liver.
Determination of carnitine, its short chain acyl esters and metabolic precursors trimethyllysine and gamma-butyrobetaine by quasi-solid phase extraction and MS/MS detection.
Eder et al., Halle, Germany. In J Chromatogr B Analyt Technol Biomed Life Sci, 2009
Quantifying the formation of deuterated carnitine from deuterated gamma-butyrobetaine, this method is also suitable for the determination of the activity of gamma-butyrobetaine dioxygenase in tissues.
Activities of gamma-butyrobetaine dioxygenase and concentrations of carnitine in tissues of pigs.
Eder et al., Halle, Germany. In Comp Biochem Physiol A Mol Integr Physiol, 2009
We found that among several pig tissues, a considerable activity of gamma-butyrobetaine dioxygenase (BBD), the last enzyme of carnitine synthesis, exists, like in humans and several other species, only in liver and kidney.
Peroxisome proliferator-activated receptor alpha and enzymes of carnitine biosynthesis in the liver are down-regulated during lactation in rats.
Eder et al., Halle, Germany. In Metabolism, 2009
Dams suckling their litters, irrespective of litter size, had lower relative messenger RNA concentrations of PPARalpha, various classic PPARalpha target genes involved in fatty acid catabolism, as well as enzymes involved in carnitine synthesis (trimethyllysine dioxygenase, 4-N-trimethylaminobutyraldehyde dehydrogenase, gamma-butyrobetaine dioxygenase) and OCTN1 in the liver than dams whose litters were removed (P < .05).
Vitamin C is not essential for carnitine biosynthesis in vivo: verification in vitamin C-depleted senescence marker protein-30/gluconolactonase knockout mice.
Ishigami et al., Chiba, Japan. In Biol Pharm Bull, 2008
Vitamin C (VC) has long been considered a requirement for the activities of two enzymes in the carnitine biosynthetic pathway, i.e., 6-N-trimethyllysine dioxygenase and gamma-butyrobetaine dioxygenase.
Clofibrate treatment up-regulates novel organic cation transporter (OCTN)-2 in tissues of pigs as a model of non-proliferating species.
Eder et al., Halle, Germany. In Eur J Pharmacol, 2008
Concentrations of gamma-butyrobetaine, the precursor of endogenous formation of carnitine, in liver, muscle and plasma did not differ between both groups; the activity of gamma-butyrobetaine dioxygenase, the rate limiting enzyme of carnitine synthesis, in the liver was lower in pigs treated with clofibrate than in control pigs (P<0.05).
PPAR alpha mediates transcriptional upregulation of novel organic cation transporters-2 and -3 and enzymes involved in hepatic carnitine synthesis.
Eder et al., Halle, Germany. In Exp Biol Med (maywood), 2008
Moreover, wild-type mice treated with WY 14,643 had greater mRNA abundances of enzymes involved in hepatic carnitine synthesis (4-N-trimethylaminobutyraldehyde dehydrogenase, gamma-butyrobetaine dioxygenase) and increased carnitine concentrations in liver and muscle than did untreated wild-type mice (P < 0.05).
PPAR alpha-activation results in enhanced carnitine biosynthesis and OCTN2-mediated hepatic carnitine accumulation.
Vaz et al., Amsterdam, Netherlands. In Biochim Biophys Acta, 2007
Here we show that both enhancement of carnitine biosynthesis (due to increased gamma-butyrobetaine dioxygenase activity), extra-hepatic gamma-butyrobetaine synthesis and increased hepatic carnitine import (OCTN2 expression) contributes to the increased hepatic carnitine levels after fasting and that these processes are PPAR alpha-dependent.
L-carnitine is synthesized in the human fetal-placental unit: potential roles in placental and fetal metabolism.
Vaz et al., Amsterdam, Netherlands. In Placenta, 2006
Placenta contained low but detectable activity of gamma-butyrobetaine dioxygenase.
Carnitine transport into muscular cells. Inhibition of transport and cell growth by mildronate.
Demarquoy et al., Dijon, France. In Biochem Pharmacol, 2000
Among these inhibitors, the most potent was mildronate (3-(2,2,2-trimethylhydrazinium)propionate), known as a gamma-butyrobetaine hydroxylase inhibitor.
Analysis of the growth and transformation suppressor domains of promyelocytic leukemia gene, PML.
Chang et al., Houston, United States. In J Biol Chem, 1996
To elucidate the functional domains of PML, several mutants lacking the nuclear localization signal (PMLnls-), the dimerization domain (PMLdim-), the proline-rich domain at the N-terminal (PMLpro-), the proline-rich RING finger motif (PMLpr-), the proline-rich RING finger B-box-1 (PML-prb-), the serine-proline-rich domain at the C-terminal (PMLsp-), and the double mutant (PMLprb-nls-) have been constructed.
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