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...

Full description

Saved in:
Bibliographic Details
Published inHaematologica (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
LanguageEnglish
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
Online AccessGet full text

Cover

More Information
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