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a case of X-linked sideroblastic anemia caused by a novel homozygous deletional mutation in exon 10 of ALAS2 gene is presented
int-1 (show WNT1 Proteins)-GATA (show QRSL1 Proteins) site should be examined in patients with XLSA in clinical settings when no known mutation is found in ALAS2 exons.
From pH jump experiments, comparable rates for the denaturation of the tertiary structure and PLP (show PLP1 Proteins)-microenvironment were discerned, indicating that the catalytic active site geometry strongly depends on the stable tertiary structural organization. Lastly, we demonstrate that partially folded ALAS tends to self-associate into higher oligomeric species at moderate GuHCl concentrations.
data indicate that the X-linked protoporphyria (show FECH Proteins) variants possess enhanced ALAS activity and ALA dissociation rates, as well as distinct structural properties from those of wild-type hALAS
In this article we add a novel mutation to the previously described 61 different ALAS2 mutations identified in X-linked sideroblastic anaemia patients.
the primary deficiency in ferrochelatase (show FECH Proteins) leads to a secondary increase in ALAS2 expression.
The ALAS2 Y365C mutation impairs pyridoxal 5'-phosphate binding to ALAS2, destabilizing the enzyme. X inactivation was not highly skewed in WBC from affected women. This X-linked dominant mutation perturbs erythropoiesis via cell-nonautonomous effects.
the 130-base pair enhancer region located in the first intron of the ALAS2 gene should be examined in patients with congenital sideroblastic anemia in whom the gene responsible is unknown.
5 families with X-linked sideroblastic anemia had mutations in a GATA (show QRSL1 Proteins) transcription factor binding site located in a transcriptional enhancer element in intron 1 of the ALAS2 gene.
Loss-of-function FECH (show FECH Proteins) and gain-of-function erythroid-specific ALAS2 mutations causing erythropoietic protoporphyria (show FECH Proteins) and x-linked protoporphyria (show FECH Proteins) in North American patients reveal novel mutations and a high prevalence of X-linked protoporphyria (show FECH Proteins).
Xalas2 might be able to synthesize hemoglobin (show HBB Proteins) during hematopoiesis and mediate erythrocyte differentiation by regulating hba3 expression in Xenopus laevis
We propose that the N-terminal truncation offers a cell-specific ALAS2 regulatory mechanism without hindering heme synthesis
Light treatments revealed that ALAS2 expression results in an increase in cell death in comparison to aminolevulinic acid (ALA) treatment producing a similar amount of protoprophyrin IX.
The rate of ALA release is also controlled by a hysteretic kinetic mechanism (observed as a lag (show STMN1 Proteins) in the ALA external aldimine formation progress curve), consistent with conformational changes governing the dissociation of ALA from ALAS.
impaired mitochondrial [Fe-S] cluster biogenesis in Mfrn1 (show SLC25A37 Proteins)(gt/gt (show FABP6 Proteins)) cells results in elevated IRP1 (show ACO1 Proteins) RNA-binding that attenuates ALAS2 mRNA translation and protoporphyrin accumulation
Aberrant iron accumulation and peroxidized state of (ALAS2)-deficient definitive erythroblasts
Gene expression and enzymatic assays indicate that erythroid 5-aminolevulinic acid synthase (show ALAS1 Proteins) (Alas2) is decreased in hem6 animals, suggesting a mechanism that could account for the anemia.
The product of this gene specifies an erythroid-specific mitochondrially located enzyme. The encoded protein catalyzes the first step in the heme biosynthetic pathway. Defects in this gene cause X-linked pyridoxine-responsive sideroblastic anemia. Alternatively spliced transcript variants encoding different isoforms have been identified.
5-aminolevulinate synthase 2
, aminolevulinate, delta-, synthase 2 (sideroblastic/hypochromic anemia)
, 5-aminolevulinate synthase, erythroid-specific, mitochondrial
, aminolevulinate, delta-, synthase 2
, delta-ALA synthase 2
, 5-aminolevulinic acid synthase 2
, delta-aminolevulinate synthase 2
, 5-aminolevulinate synthase, erythroid-specific, mitochondrial-like
, delta-ALA synthetase
, delta-ALA synthetase 2
, Aminolevulinate synthase 2, delta
, aminolevulinic acid synthase 2, erythroid
, erythroid-specific delta-aminolevulinate synthase ALAS-E
, erythroid aminolevulinate synthase
, erythroid-specific ALAS