Congenital dyserythropoietic anemia type II: molecular basis and clinical aspects

Dipartimento di Biomedicina dell'Eta Evolutiva, Universita di Bari, Italy. Congenital dyserythropoietic anemia of type II (CDA II) is a rare disorder, usually present in childhood, with a clinical picture of chronic anemia of mild to moderate degree, splenomegaly and intermittent or persistent...

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Bibliographic Details
Published in:	Haematologica (Roma) Vol. 81; no. 6; pp. 543 - 559
Main Authors:	Iolascon, A, D'Agostaro, G, Perrotta, S, Izzo, P, Tavano, R, Miraglia del Giudice, B
Format:	Journal Article
Language:	English
Published:	Pavia Haematologica 01-11-1996
Subjects:	Anemia, Dyserythropoietic, Congenital - blood Anemia, Dyserythropoietic, Congenital - diagnosis Anemia, Dyserythropoietic, Congenital - genetics Anemias. Hemoglobinopathies Biological and medical sciences Carbohydrate Sequence Chromosome Mapping Diseases of red blood cells Genetic Markers Hematologic and hematopoietic diseases Humans Medical sciences Molecular Sequence Data Oligosaccharides - chemistry Human Pathophysiology Dyserythropoietic anemia Clinical form Hemopathy Review Diagnosis Genetic disease
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Summary:	Dipartimento di Biomedicina dell'Eta Evolutiva, Universita di Bari, Italy. Congenital dyserythropoietic anemia of type II (CDA II) is a rare disorder, usually present in childhood, with a clinical picture of chronic anemia of mild to moderate degree, splenomegaly and intermittent or persistent jaundice. It is transmitted by autosomal recessive inheritance and is characterized by the presence of a large number of multinucleate and binucleate erythroblasts in the bone marrow and typical morphological abnormalities of the membrane of circulating erythrocytes. SDS-PAGE of red blood cell membrane proteins shows a narrower aspect and a faster migration of band 3 (anion exchange transporter). This aspect is consistent with decreased glycosylation of this protein. The genetic mutations responsible for the glycosylation defect in CDA II have not yet been identified. Analysis of carbohydrate structures and biochemical data indicate that the activity of either GnT II or alpha-Man II is reduced in different families, suggesting that the disease is genetically heterogeneous. Molecular cloning of the GnT II and alpha-Man II DNA sequences has allowed direct investigation of the genetic mutations underlying the glycosylation defect in CDA II patients to begin.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1
ISSN:	0390-6078 1592-8721