AnatomyDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and Processes
Anemia, Dyserythropoietic, CongenitalAnemia, Hemolytic, CongenitalAnemiaErythroblastsAnemia, MacrocyticErythrocytes, AbnormalErythropoiesisSplenectomyIron OverloadAnion Exchange Protein 1, ErythrocyteVesicular Transport ProteinsPedigreeErythrocyte MembraneAnemia, AplasticAnemia, HemolyticBone MarrowErythrocytes

Mutational spectrum in congenital dyserythropoietic anemia type II: identification of 19 novel variants in SEC23B gene. (41/81)

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A dominant mutation in the gene encoding the erythroid transcription factor KLF1 causes a congenital dyserythropoietic anemia. (42/81)

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E109K is a SEC23B founder mutation among Israeli Moroccan Jewish patients with congenital dyserythropoietic anemia type II. (43/81)

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Codanin-1 mutations in congenital dyserythropoietic anemia type 1 affect HP1{alpha} localization in erythroblasts. (44/81)

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Two founder mutations in the SEC23B gene account for the relatively high frequency of CDA II in the Italian population. (45/81)

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Incomplete synthesis of N-glycans in congenital dyserythropoietic anemia type II caused by a defect in the gene encoding alpha-mannosidase II. (46/81)

Congenital dyserythropoietic anemia type II, or hereditary erythroblastic multinuclearity with a positive acidified-serum-lysis test (HEMPAS), is a genetic anemia in humans inherited by an autosomally recessive mode. The enzyme defect in most HEMPAS patients has previously been proposed as a lowered activity of N-acetylglucosaminyltransferase II, resulting in a lack of polylactosamine on proteins and leading to the accumulation of polylactosaminyl lipids. A recent HEMPAS case, G.C., has now been analyzed by cell-surface labeling, fast-atom-bombardment mass spectrometry of glycopeptides, and activity assay of glycosylation enzymes. Significantly decreased glycosylation of polylactosaminoglycan proteins and incompletely processed asparagine-linked oligosaccharides were detected in the erythrocyte membranes of G.C. In contrast to the earlier studied HEMPAS cases, G.C. cells are normal in N-acetylglucosaminyltransferase II activity but are low in alpha-mannosidase II (alpha-ManII) activity. Northern (RNA) analysis of poly(A)+ mRNA from normal, G.C., and other unrelated HEMPAS cells all showed double bands at the 7.6-kilobase position, detected by an alpha-ManII cDNA probe, but expression of these bands in G.C. cells was substantially reduced (less than 10% of normal). In Southern analysis of G.C. and normal genomic DNA, the restriction fragment patterns detected by the alpha-ManII cDNA probe were indistinguishable. These results suggest that G.C. cells contain a mutation in alpha-ManII-encoding gene that results in inefficient expression of alpha-ManII mRNA, either through reduced transcription or message instability. This report demonstrates that HEMPAS is caused by a defective gene encoding an enzyme necessary for the synthesis of asparagine-linked oligosaccharides.  (+info)

Congenital dyserythropoietic anemia type II: molecular analysis and expression of the SEC23B gene. (47/81)

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Codanin-1, mutated in the anaemic disease CDAI, regulates Asf1 function in S-phase histone supply. (48/81)

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