Abnormalities of erythrocyte glycoconjugates are identical in two families with congenital dyserythropoietic anemia type II with different chromosomal localizations of the disease gene

Zdebska, Ewa; Iolascon, Achille; Spychalska, Justyna; Perrotta, Silverio; Lanzara, Carmela; Smoleńska-Sym, Gabriela; Kościelak, Jerzy

doi:10.3324/haematol.10803

Cited by 9 publications

(9 citation statements)

References 9 publications

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“…However, Zdebska et al did not investigate the specific glycosidic linkage of fucose as has been done in this study [26]. The same group could demonstrate, that obligatory heterozygous gene carriers also have a glycosylation phenotype that lies between healthy controls and CDA II patients [28].…”

Section: Discussionmentioning

confidence: 60%

Characterization of the N-glycosylation phenotype of erythrocyte membrane proteins in congenital dyserythropoietic anemia type II (CDA II/HEMPAS)

Denecke

Kranz

Nimtz³

et al. 2007

Glycoconj J

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Section: Discussionmentioning

confidence: 60%

Characterization of the N-glycosylation phenotype of erythrocyte membrane proteins in congenital dyserythropoietic anemia type II (CDA II/HEMPAS)

Denecke

Kranz

Nimtz³

et al. 2007

Glycoconj J

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“…A patient of dyserythropoietic phenotype was recently reported to carry a novel AE1 mutation in association with dehydrated stomatocytosis (De Falco, 2008), but none of the three types of CDA maps to the AE1 locus. Nonetheless, red cell AE1 abundance is reduced in patients with CDAII secondary to mutations in two distinct genes (Zdebska et al, 2007).…”

Section: Kae1 Renal Disease Phenotypesmentioning

confidence: 99%

Molecular physiology and genetics of Na+-independent SLC4 anion exchangers

Alper

2009

Journal of Experimental Biology

193

220

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SUMMARY Plasmalemmal Cl–/HCO3–exchangers are encoded by the SLC4 and SLC26 gene superfamilies, and function to regulate intracellular pH,[Cl–] and cell volume. The Cl–/HCO3– exchangers of polarized epithelial cells also contribute to transepithelial secretion and reabsorption of acid–base equivalents and Cl–. This review focuses on Na+-independent electroneutral Cl–/HCO3– exchangers of the SLC4 family. Human SLC4A1/AE1 mutations cause the familial erythroid disorders of spherocytic anemia, stomatocytic anemia and ovalocytosis. A largely discrete set of AE1 mutations causes familial distal renal tubular acidosis. The Slc4a2/Ae2–/– mouse dies before weaning with achlorhydria and osteopetrosis. A hypomorphic Ae2–/– mouse survives to exhibit male infertility with defective spermatogenesis and a syndrome resembling primary biliary cirrhosis. A human SLC4A3/AE3 polymorphism is associated with seizure disorder, and the Ae3–/– mouse has increased seizure susceptibility. The transport mechanism of mammalian SLC4/AE polypeptides is that of electroneutral Cl–/anion exchange,but trout erythroid Ae1 also mediates Cl– conductance. Erythroid Ae1 may mediate the DIDS-sensitive Cl– conductance of mammalian erythrocytes, and, with a single missense mutation, can mediate electrogenic SO42–/Cl– exchange. AE1 trafficking in polarized cells is regulated by phosphorylation and by interaction with other proteins. AE2 exhibits isoform-specific patterns of acute inhibition by acidic intracellular pH and independently by acidic extracellular pH. In contrast, AE2 is activated by hypertonicity and, in a pH-independent manner, by ammonium and by hypertonicity. A growing body of structure–function and interaction data, together with emerging information about physiological function and structure, is advancing our understanding of SLC4 anion exchangers.

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“…It is a matter of debate if the impaired glycosylation is the primary cause of the disorder or a phenomenon secondary to other pathogenic mechanisms [Zdebska et al, 2001[Zdebska et al, , 2007. Recent studies on N-glycosylation of erythrocyte membrane proteins in CDAII patients indicate that CDAII is not a distinct glycosylation disorder but is caused by a defect disturbing Golgi processing in erythroblasts [Denecke et al, 2008]; however, the biochemical mechanism causing CDAII remains unknown and the aberrant gene has not so far been elucidated.…”

Section: Introductionmentioning

confidence: 99%

Congenital dyserythropoietic anemia type II (CDAII) is caused by mutations in theSEC23Bgene

et al. 2009

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Congenital dyserythropoietic anemia type II (CDAII) is an autosomal recessive disease characterized by ineffective erythropoiesis, hemolysis, erythroblast morphological abnormalities, and hypoglycosylation of some red blood cell (RBC) membrane proteins. Recent studies indicated that CDAII is caused by a defect disturbing Golgi processing in erythroblasts. A linkage analysis located a candidate region on chromosome 20, termed the CDAN2 locus, in the majority of CDAII patients but the aberrant gene has not so far been elucidated. We used a proteomic-genomic approach to identify SEC23B as the candidate gene for CDAII by matching the recently published data on the cytoplasmic proteome of human RBCs with the chromosomic localization of CDAN2 locus. Sequencing analysis of SEC23B gene in 13 CDAII patients from 10 families revealed 12 different mutations: six missense (c.40C>T, c.325G>A, c.1043A>C, c.1489C>T, c.1808C>T, and c.2101C>T), two frameshift (c.428_428delAinsCG and c.1821delT), one splicing (c.689+1G>A), and three nonsense (c.568C>T, c.649C>T, and c.1660C>T). Mutations c.40C>T and c.325G>A were detected in unrelated patients. SEC23B is a member of the Sec23/Sec24 family, a component of the COPII coat protein complex involved in protein transport through membrane vesicles. Abnormalities in this gene are likely to disturb endoplasmic reticulum (ER)-to-Golgi trafficking, affecting different glycosylation pathways and ultimately accounting for the cellular phenotype observed in CDAII.

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Abnormalities of erythrocyte glycoconjugates are identical in two families with congenital dyserythropoietic anemia type II with different chromosomal localizations of the disease gene

Cited by 9 publications

References 9 publications

Characterization of the N-glycosylation phenotype of erythrocyte membrane proteins in congenital dyserythropoietic anemia type II (CDA II/HEMPAS)

Characterization of the N-glycosylation phenotype of erythrocyte membrane proteins in congenital dyserythropoietic anemia type II (CDA II/HEMPAS)

Molecular physiology and genetics of Na+-independent SLC4 anion exchangers

Congenital dyserythropoietic anemia type II (CDAII) is caused by mutations in theSEC23Bgene

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