The Mechanism of Loss of CR1 during Maturation of Erythrocytes Is Different between Factor I Deficient Patients and Healthy Donors

ABSTRACT During the in vivo maturation of erythrocytes, the number of CR1 per cell decreases by approximately two-thirds in 30 days. The CR1 loss is enhanced in several diseases such as SLE, AIDS, and particularly in factor I deficiency. Microvesicles enriched in CR1 and DAF are released from erythr...

Full description

Saved in:
Bibliographic Details
Published in:Blood cells, molecules, & diseases molecules, & diseases, 2002-09, Vol.29 (2), p.200-212
Main Authors: Miot, Sylvie, Marfurt, Jutta, Lach-Trifilieff, Estelle, González-Rubio, Carolina, López-Trascasa, Margarita, Sadallah, Salima, Schifferli, Jürg-Alfred
Format: Article
Language:English
Subjects:
Afibrinogenemia - blood
Antibodies
Case-Control Studies
CD55 Antigens - analysis
CD55 Antigens - metabolism
complement
Erythrocyte Aging
erythrocytes
Erythrocytes - physiology
Exocytosis
factor I deficiency
Fibrinogen
human
Humans
Immunoblotting
in vivo maturation
Receptors, Complement 3b - analysis
Receptors, Complement 3b - immunology
Receptors, Complement 3b - metabolism
Reticulocytes
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:ABSTRACT During the in vivo maturation of erythrocytes, the number of CR1 per cell decreases by approximately two-thirds in 30 days. The CR1 loss is enhanced in several diseases such as SLE, AIDS, and particularly in factor I deficiency. Microvesicles enriched in CR1 and DAF are released from erythrocytes matured in vitro, leading to the same loss of both molecules. When comparing reticulocytes and erythrocytes, CR1 and DAF were lost similarly in 15 normal individuals, suggesting that vesiculation may be at the origin of CR1 loss in vivo. However, the enhanced loss of CR1 in 3 patients with factor I deficiency was contrasted with a normal loss of DAF, raising the possibility that, in this pathological condition, CR1 might be proteolytically cleaved, leaving small CR1 fragments on the erythrocytes. To answer this question, a rabbit polyclonal antibody was raised against the cytoplasmic (tail) domain of CR1, which recognised specifically CR1 of erythrocytes and urinary vesicles on Western blots. However, no CR1 fragments could be detected on erythrocytes of the factor I deficient patients although this antibody was able to recognise CR1 fragments after treatment of normal erythrocytes or urinary vesicles with elastase. These data suggest that cell surface domains rich in CR1, but not in DAF, are specifically lost in factor I deficiency.
ISSN:1079-9796
1096-0961
DOI:10.1006/bcmd.2002.0559