gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

ALAS2 aminolevulinate, delta-, synthase 2

delta Aminolevulinate synthase
Top mentioned proteins: 5-aminolevulinate synthase, ACID, HAD, CAN, STEP
Papers on delta Aminolevulinate synthase
[Peculiarities of the Structural-Functional State of the Cytochrome Part of Liver Mitochondrial Respiratory Chain under Conditions of Acetaminophen-induced Hepatitis against the Background of Alimentary Deprivation of Protein].
Kopylchuk et al., In Biofizika, May 2015
Activity of the key enzyme of the cytochrome part of the respiratory chain--cytochrome oxidase, quantitative redistribution of mitochondrial cytochromes b, c1, c and aa3, activity of the key enzymes of cytochromes' heme metabolism--delta-aminolevulinate synthase and heme oxygenase under conditions of acetaminophen-induced hepatitis against the background of alimentary deprivation of protein were studied.
Octabromodiphenyl ether - porphyrogenicity after repeated administration to rats.
Szymańska et al., Łódź, Poland. In Int J Occup Med Environ Health, 2012
The following measures of heme synthesis disturbance were used: urinary excretion of porphyrins, liver concentration of porphyrins, the activity of delta-aminolevulinate synthase (ALA-S) and delta-aminolevulinate dehydratase (ALA-D) in the liver.
Evaluation of mRNA marker specificity for the identification of five human body fluids by capillary electrophoresis.
Donfack et al., United States. In Forensic Sci Int Genet, 2012
Seven markers for the following genes were selected for evaluation in this study: histatin 3 (HTN3) and statherin (STATH) for saliva, mucin 4 (MUC4) for vaginal secretions, matrix metalloproteinase 7 (MMP7) for menstrual blood, delta-aminolevulinate synthase 2 (ALAS2) for peripheral blood, and protamine 2 (PRM2) and transglutaminase 4 (TGM4) for semen.
[Recent progress in iron metabolism and iron-related anemia].
Harigae, Sendai, Japan. In Rinsho Byori, 2010
The most common inherited sideroblastic anemia is X-linked sideroblastic anemia (XLSA) caused by mutations of the erythroid-specific delta-aminolevulinate synthase gene (ALAS2), which is the first enzyme involved in heme biosynthesis in erythroid cells.
New mutation in erythroid-specific delta-aminolevulinate synthase as the cause of X-linked sideroblastic anemia responsive to pyridoxine.
Divoky et al., Olomouc, Czech Republic. In Acta Haematol, 2010
The most common form is X-linked SA, which results from mutations in erythroid-specific δ-aminolevulinate synthase (ALAS2), the first enzyme in heme biosynthesis.
Light pulse induces ALA-S gene expression in the rat Harderian gland.
Touitou et al., Paris, France. In J Physiol Pharmacol, 2010
We have previously shown that continuous light exposure abolished the day/night variations of the delta-aminolevulinate synthase (ALA-S; the rate-limiting enzyme for porphyrin biosynthesis) gene expression observed under standard light: dark cycles (LD 12:12) in the rat HGs.
PBRL, a putative peripheral benzodiazepine receptor, in primitive erythropoiesis.
Sheng et al., Kōbe, Japan. In Gene Expr Patterns, 2009
Five of them, delta-aminolevulinate synthase, delta-aminolevulinic acid dehydrogenase, porphobilinogen deaminase, coproporphyrinogen decarboxylase and ferrochelatase, show stage-specific increase in gene expression correlated with primitive hematopoiesis, but not with primitive erythrocyte differentiation.
Melatonin and environmental lighting regulate ALA-S gene expression and So porphyrin biosynthesis in the rat harderian gland.
Djeridane et al., Paris, France. In Chronobiol Int, 2008
The aim of this study was to determine day-night PPIX levels as well as day-night activity and mode of expression of the porphyrinogenic enzymes delta-aminolevulinate synthase (ALA-S) and ferrochelatase (Fech) in the rat HG.
Potential role of lipin-1 in exercise-induced mitochondrial biogenesis.
Terada et al., Tokorozawa, Japan. In Biochem Biophys Res Commun, 2008
Second, ectopic expression of lipin-1 in L6 myotube increased carnitine palmitoyltransferase-1 and delta-aminolevulinate synthase gene expression.
B6-responsive disorders: a model of vitamin dependency.
Clayton, London, United Kingdom. In J Inherit Metab Dis, 2006
The last show a very variable degree of pyridoxine responsiveness, from 90% in X-linked sideroblastic anaemia (delta-aminolevulinate synthase deficiency) through 50% in homocystinuria (cystathionine beta-synthase deficiency) to 5% in ornithinaemia with gyrate atrophy (ornithine delta-aminotransferase deficiency).
[Progress of study on sideroblastic anemia and its possible gene therapy--review].
Zhu et al., Beijing, China. In Zhongguo Shi Yan Xue Ye Xue Za Zhi, 2005
Actually there are two isozymes of ALAS and ALAS2 (erythroid delta-aminolevulinate synthase), they play the leading role in the hemoglobin biosynthetic pathway.
Multiple mechanisms for hereditary sideroblastic anemia.
Sassa et al., Sendai, Japan. In Cell Mol Biol Incl Cyto Enzymol, 2002
It has been shown that a deficiency of the erythroid-specific delta-aminolevulinate synthase (ALAS-E) activity is responsible for pyridoxine-responsive HSA in many patients, however, the pathogenesis of other types of HSA remains still unknown.
[Heme metabolism and oxidative stress].
Barannik et al., Kharkiv, Ukraine. In Ukr Biokhim Zh (1999), 2001
The main attention is focused to the prooxidant action of heme, the interaction of heme transport and lipid exchange, and to the heme metabolism key enzymes (delta-aminolevulinate synthase and heme oxygenase), serum heme-binding protein hemopexin and intracellular heme-binding proteins participating in metabolism adaptation under the action of factors, which cause oxidative stress.
Positional cloning of the zebrafish sauternes gene: a model for congenital sideroblastic anaemia.
Zon et al., Boston, United States. In Nat Genet, 1998
Using positional cloning techniques, we show that sau encodes the erythroid-specific isoform of delta-aminolevulinate synthase (ALAS2; also known as ALAS-E), the enzyme required for the first step in haem biosynthesis.
Regulation by heme of mitochondrial protein transport through a conserved amino acid motif.
Timko et al., Charlottesville, United States. In Science, 1993
A conserved motif, termed the heme regulatory motif (HRM), was identified in the presequences of the erythroid delta-aminolevulinate synthase precursors and was shown to be involved in hemin inhibition of transport of these proteins into mouse mitochondria in vitro.
share on facebooktweetadd +1mail to friends