Results 11 to 20 of about 1,366 (166)

Anemia sideroblástica por una variante en el gen ALAS2

Revista Hematología
Las anemias sideroblásticas (AS) son un grupo heterogéneo de patologías raras en las que se ve afectada la biosíntesis del hemo y la utilización del hierro durante la síntesis de la hemoglobina.
F. Aguirre, A. Albero, C. Pepe, V. Avalos, A. Chaves, D. Fernandez, M. González, L. Nieto, B. Milanesio, E. Rossetti, E. Masegosa, R. Escobar, S. E. Eberle   +12 more
exaly   +4 more sources

A case report of congenital sideroblastic anemia caused by a novel ALAS2 mutation in conjunction with thalassemia

Annals of Hematology
Background Congenital sideroblastic anemia (CSA) and thalassemia are both hereditary disorders of erythropoiesis, primarily affecting erythroid cells. Their typical manifestations include anemia and iron overload. In this study, we conducted clinical and
Zhi-Xiao Chen, Li-Ye Yang, Liang-Tuo Wang, Bao-Ying Chen, Jian-Lian Liang, Li-Li Liu, Xiao-Hua Yu   +6 more
doaj   +4 more sources

A novel ALAS2 mutation causes congenital sideroblastic anemia

Mediterranean Journal of Hematology and Infectious Diseases, 2023
Kun Yang
doaj   +4 more sources

CLPX and CLPP proteins are required for regulation of ALAS2

, 2021
Heme synthesis consists of a series of eight enzymatic steps that result in the synthesis of porphyrin products, which in turn can be used to generate other tetrapyrrole compounds. In late-stage erythropoiesis, these precursors can be converted into its terminal product, heme.
Carter, Stashauna S.
openaire   +3 more sources

X-linked macrocytic dyserythropoietic anemia in females with an ALAS2 mutation [PDF]

Journal of Clinical Investigation, 2015
Macrocytic anemia with abnormal erythropoiesis is a common feature of megaloblastic anemias, congenital dyserythropoietic anemias, and myelodysplastic syndromes. Here, we characterized a family with multiple female individuals who have macrocytic anemia. The proband was noted to have dyserythropoiesis and iron overload.
Vijay G, Sankaran, Jacob C, Ulirsch, Vassili, Tchaikovskii, Leif S, Ludwig, Aoi, Wakabayashi, Senkottuvelan, Kadirvel, R Coleman, Lindsley, Rafael, Bejar, Jiahai, Shi, Scott B, Lovitch, David F, Bishop, David P, Steensma   +11 more
openaire   +5 more sources

Expression of murine 5-aminolevulinate synthase variants causes protoporphyrin IX accumulation and light-induced mammalian cell death. [PDF]

PLoS ONE, 2014
5-Aminolevulinate synthase (ALAS; EC 2.3.1.37) catalyzes the first committed step of heme biosynthesis in animals. The erythroid-specific ALAS isozyme (ALAS2) is negatively regulated by heme at the level of mitochondrial import and, in its mature form ...
Erica J Fratz, Gregory A Hunter, Gloria C Ferreira   +2 more
doaj   +2 more sources

Severe Microcytic Anemia Caused by Complex Hereditary Spherocytosis and X-Linked Sideroblastic Anemia with Mutations in SPTB and ALAS2 Genes

Journal of Clinical Medicine, 2023
We report a case of severe anemia caused by complex hereditary spherocytosis (HS) and X-linked sideroblastic anemia (XLSA) with two mutations in the spectrin beta (SPTB) and 5-aminolevulinic acid synthase (ALAS2) genes. The proband was a 16-year-old male
Jianying Zhou, Hang Zhang, Yao Qin, Ting Liu   +3 more
semanticscholar   +2 more sources

ALAS2 acts as a modifier gene in patients with congenital erythropoietic porphyria

Blood, 2011
Abstract Mutations in the uroporphyrinogen III synthase (UROS) gene cause congenital erythropoietic porphyria (CEP), an autosomal-recessive inborn error of erythroid heme biosynthesis. Clinical features of CEP include dermatologic and hematologic abnormalities of variable severity. The discovery of a new type of erythroid porphyria, X-
Jordi, To-Figueras, Sarah, Ducamp, Jerome, Clayton, Celia, Badenas, Constance, Delaby, Cecile, Ged, Said, Lyoumi, Laurent, Gouya, Hubert, de Verneuil, Carole, Beaumont, Gloria C, Ferreira, Jean-Charles, Deybach, Carmen, Herrero, Herve, Puy   +13 more
openaire   +3 more sources

Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release [PDF]

Nature Communications, 2020
Mutation of the C-terminal extension of 5′-aminolevulinate synthase 2 (ALAS2) is the molecular cause for X-linked protoporphyria, but the underlying mechanism is unclear.
Henry J. Bailey, Gustavo A. Bezerra, Jason R. Marcero, Siladitya Padhi, William R. Foster, Elzbieta Rembeza, Arijit Roy, David F. Bishop, Robert J. Desnick, Gopalakrishnan Bulusu, Harry A. Dailey, Wyatt W. Yue   +11 more
doaj   +2 more sources

Brain tissue haemoglobin expression in saline-perfused vs non-perfused rodents

Heliyon
Haemoglobin beta (Hbb) and delta-aminolevulinate synthase 2 (Alas2) messenger RNA (mRNA) is mainly found in immature red blood cells, reticulocytes, and not in mature erythrocytes.
Marion Walser, Lars Karlsson, Reza Motalleb, Jörgen Isgaard, H Georg Kuhn, N. David Åberg   +5 more
doaj   +3 more sources