scholarly journals SEC23A rescues SEC23B-deficient congenital dyserythropoietic anemia type II

2021 ◽  
Vol 7 (48) ◽  
Author(s):  
Richard King ◽  
Zesen Lin ◽  
Ginette Balbin-Cuesta ◽  
Gregg Myers ◽  
Ann Friedman ◽  
...  
Keyword(s):  
Type Ii ◽  
Congenital Dyserythropoietic Anemia

scholarly journals GATA1 erythroid-specific regulation of SEC23B expression and its implication in the pathogenesis of congenital dyserythropoietic anemia type II

Haematologica ◽  
2017 ◽  
Vol 102 (9) ◽  
pp. e371-e374 ◽  
Author(s):  
Roberta Russo ◽  
Immacolata Andolfo ◽  
Antonella Gambale ◽  
Gianluca De Rosa ◽  
Francesco Manna ◽  
...  
Keyword(s):  
Type Ii ◽  
Congenital Dyserythropoietic Anemia ◽  
Specific Regulation

Congenital Dyserythropoietic Anemia

PEDIATRICS ◽  
1973 ◽  
Vol 51 (5) ◽  
pp. 957-958
Author(s):  
G. Bennett Humphrey ◽  
Bahaod-Din Mojab ◽  
Ingomar Mutz
Keyword(s):  
Carbohydrate Metabolism ◽  
Morphological Characteristics ◽  
Type I ◽  
Type Ii ◽  
Congenital Dyserythropoietic Anemia ◽  
The 1950S ◽  
Deja Vu ◽  
Déjà Vu ◽  
Excellent Article

Reading the excellent article by Drs. Murphy and Oski, "Congenital Dyserythropoietic Anemia (CDA)",1 which further defines type II, produced a sense of deja vu. In the 1950s, nonspherocytic, hemolytic anemias (HNHA) were categorized as type I and II based on the in vitro autohemolysis test.2 This group of anemias has subsequently been demonstrated to be due to a series of enzymatic abnormalities in carbohydrate metabolism.3 In CDA, the morphological characteristics which define types I, II, and III probably reflect nuclear rather than cytoplasmic abnormalities.

A novel variant mutation for congenital dyserythropoietic anemia, type II

2014 ◽  
Vol 53 (4) ◽  
pp. 272-273 ◽  
Author(s):  
Joo Y. Song ◽  
Anjali Pawar ◽  
Christin Collins
Keyword(s):  
Type Ii ◽  
Congenital Dyserythropoietic Anemia ◽  
Novel Variant

scholarly journals Successful Treatment of Iron Overload by Phlebotomies in a Patient With Severe Congenital Dyserythropoietic Anemia Type II

Blood ◽  
1997 ◽  
Vol 89 (8) ◽  
pp. 3068-3068 ◽  
Author(s):  
W.K. Hofmann ◽  
J.P. Kaltwasser ◽  
D. Hoelzer ◽  
P. Nielsen ◽  
E.E. Gabbe
Keyword(s):  
Iron Overload ◽  
Successful Treatment ◽  
Type Ii ◽  
Congenital Dyserythropoietic Anemia

scholarly journals Anomalous clustering of underglycosylated band 3 in erythrocytes and their precursor cells in congenital dyserythropoietic anemia type II

Blood ◽  
1986 ◽  
Vol 68 (2) ◽  
pp. 521-529 ◽  
Author(s):  
MN Fukuda ◽  
G Klier ◽  
J Yu ◽  
P Scartezzini
Keyword(s):  
Electron Microscopy ◽  
Freeze Fracture ◽  
Band 3 ◽  
Precursor Cells ◽  
Erythrocyte Membranes ◽  
Immunogold Electron Microscopy ◽  
Glycophorin A ◽  
Type Ii ◽  
Congenital Dyserythropoietic Anemia ◽  
Cytoplasmic Area

Congenital dyserythropoietic anemia type II (CDA II or HEMPAS) is a genetic anemia caused by membrane abnormality. Our previous studies indicated that in HEMPAS, erythrocytes band 3 and band 4.5 are not glycosylated by polylactosaminoglycans. The present study was aimed at determining how such underglycosylated band 3 behaves in erythrocyte membranes. By using anti-band 3 antibodies, immunogold electron microscopy revealed that band 3s are clustered in HEMPAS erythrocyte membranes. By freeze-fracture electron microscopy, band 3s were also seen as lightly clumped intramembrane particles on a protoplasmic fracture face. Erythrocyte precursor cells stained by anti-band 3 antibodies showed that band 3s are present in the cytoplasmic area of the reticulocytes as scattered single particles. However, in young erythrocytes in which intracellular membranes are almost degenerated, band 3s were clustered in the cytoplasmic area of the cell. These observations suggest that band 3s cluster before they are incorporated into the plasma membranes of HEMPAS erythrocytes. In contrast to band 3, glycophorin A detected by anti-glycophorin A antibodies did not show a noticeable difference between normal and HEMPAS. Such a clustering of band 3 may cause abnormal localization of band 3-associated proteins and may thus result in the macroscopic membrane abnormality seen in HEMPAS erythrocytes.

Congenital dyserythropoietic anemia type II in human patients is not due to mutations in the erythroid anion exchanger 1

Blood ◽  
2003 ◽  
Vol 102 (7) ◽  
pp. 2704-2705 ◽  
Author(s):  
Silverio Perrotta ◽  
Lucio Luzzatto ◽  
Massimo Carella ◽  
Achille Iolascon
Keyword(s):  
Anion Exchanger ◽  
Type Ii ◽  
Anion Exchanger 1 ◽  
Congenital Dyserythropoietic Anemia

scholarly journals Congenital Dyserythropoietic Anemia Type II: Ultrastructural and Radioautographic Studies of Blood and Bone Marrow

Blood ◽  
1972 ◽  
Vol 39 (1) ◽  
pp. 23-30 ◽  
Author(s):  
Kwan Yuen Wong ◽  
George Hug ◽  
Beatrice C. Lampkin
Keyword(s):  
Bone Marrow ◽  
Dna Synthesis ◽  
Marked Decrease ◽  
Tritiated Thymidine ◽  
Red Cells ◽  
Type Ii ◽  
White Girl ◽  
Congenital Dyserythropoietic Anemia ◽  
Cytoplasmic Membranes

Abstract A 12-yr-old white girl with congenital dyserythropoietic anemia (CDA) type II was studied. Excessive cytoplasmic membranes (appearing like "double membranes") were found in the majority of the normoblasts. There was marked decrease in the uptake of tritiated thymidine in the binucleated normoblasts as demonstrated by radioautography. The results suggest that the cells with more severe structural cytoplasmic abnormalities and/or decreased DNA synthesis are destroyed within the bone marrow, and the circulating red cells are derived from a less abnormal population of precursors.

scholarly journals Defective glycosylation of erythrocyte membrane glycoconjugates in a variant of congenital dyserythropoietic anemia type II: association of low level of membrane-bound form of galactosyltransferase

Blood ◽  
1989 ◽  
Vol 73 (5) ◽  
pp. 1331-1339 ◽  
Author(s):  
MN Fukuda ◽  
KA Masri ◽  
A Dell ◽  
EJ Thonar ◽  
G Klier ◽  
...  
Keyword(s):  
Genetic Disease ◽  
Fast Atom Bombardment ◽  
Mass Spectrometry Analysis ◽  
Type Ii ◽  
Congenital Dyserythropoietic Anemia ◽  
Spectrometry Analysis ◽  
Microsomal Membranes ◽  
Cda Ii ◽  
Membrane Bound ◽  
High Mannose

Abstract Congenital dyserythropoietic anemia type II (CDA II) or HEMPAS is a genetic disease caused by plasma membrane abnormality. The enzymic defect of HEMPAS has been suggested to be the lowered activity of N- acetylglucosaminyltransferase II, resulting in lack of polylactosamine formation on proteins and leading to accumulation of polylactosaminyl lipids. In contrast to typical HEMPAS cases, cell-surface labeling of the erythrocytes of a HEMPAS variant G.K. showed an absence of polylactosamines either on proteins or on lipids. Fast-atom bombardment mass spectrometry analysis of G.K.'s erythrocyte glycopeptides detected a series of high mannose-type oligosaccharides, which were not detected in erythrocyte N-glycans of normal cells or of other HEMPAS cases: The former contains polylactosaminoglycans and the latter contains hybrid- type oligosaccharides. Keratansulfate (sulfated polylactosamines) in this patient's serum was abnormally low. The galactosyltransferase activity in microsomal membranes prepared from G.K.'s mononucleated cells was 24% of the normal level, whereas this enzyme activity in G.K.'s serum was comparatively higher than normal. Western blotting of G.K.'s membranes using antigalactosyltransferase antibodies showed that G.K. has reduced amounts of this enzyme present. The results collectively suggest that variant G.K. is defective in polylactosamine synthesis owing to the decreased quantity of the membrane-bound form of galactosyltransferase.

Isolation and characterization of poly-N-acetyllactosaminylceramides accumulated in the erythrocytes of congenital dyserythropoietic anemia type II patients

1986 ◽  
Vol 42 (1-3) ◽  
pp. 185-197 ◽  
Author(s):  
Michiko N. Fukuda ◽  
Brian Bothner ◽  
Paolo Scartezzini ◽  
Anne Dell
Keyword(s):  
Type Ii ◽  
Congenital Dyserythropoietic Anemia ◽  
Isolation And Characterization
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