Proteolytic cleavage of CR1 on human erythrocytes in vivo: evidence for enhanced cleavage in AIDS

Détails

ID Serval
serval:BIB_22402BD90726
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Proteolytic cleavage of CR1 on human erythrocytes in vivo: evidence for enhanced cleavage in AIDS
Périodique
European Journal of Immunology
Auteur(s)
Pascual  M., Danielsson  C., Steiger  G., Schifferli  J. A.
ISSN
0014-2980
Statut éditorial
Publié
Date de publication
03/1994
Peer-reviewed
Oui
Volume
24
Numéro
3
Pages
702-8
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Mar
Résumé
The number of complement receptor type 1 (CR1; CD35) on human erythrocytes (E) decreases during normal in vivo aging. Patients with acquired immunodeficiency syndrome (AIDS) have an acquired deficiency of CR1 on E. The possible mechanisms responsible for the loss of CR1 from E include the release of small vesicles from the E membrane and proteolytic cleavage of CR1. When compared to E of normal donors and of asymptomatic human immunodeficiency virus HIV+ subjects, E of patients with AIDS had fewer CR1/E (p < 0.001), but had the same number of two glycosylphosphatidylinositol-anchored proteins, decay-accelerating-factor (DAF) and CD59. When compared to young E, old E separated by density gradients on Percoll had fewer CR1 [six normal subjects, mean loss: 50.4 +/- 4.9 (SEM) %], DAF (34.4 +/- 1.2%) and CD59 (34.5 +/- 2.7%). The loss of CR1 was significantly higher than the loss of DAF and CD59 (p < 0.02). In vitro, ATP depletion of E is responsible for the release of vesicles from the E surface, a reaction that has been called in vitro aging. CR1, DAF and CD59 were lost on ATP-depleted E; however, the loss of CR1 and DAF were identical (six experiments, mean loss of CR1: 28.7 +/- 2.7%, DAF: 26.3 +/- 4.6% and CD59: 20.5 +/- 4%). Thus, the release of vesicles from E cannot explain the specific loss of CR1 in patients with AIDS and would explain only incompletely the loss of CR1 during in vivo aging. In vitro experiments indicated that CR1 was more sensitive to trypsin and papain cleavage than DAF and CD59. Enhanced chemiluminescence Western blotting, using a monoclonal antibody (E11) recognizing fragments of CR1 down to 43 kDa on E exposed to trypsin or papain, indicated that normal E bear fragments of CR1, which are not found on polymorphonuclear leukocytes or on CR1-bearing vesicles in urine. The relative amount of these fragments was increased in patients with AIDS. Taken together these data suggest that the specific loss of CR1 on E in AIDS is due to proteolytic cleavage. The loss of CR1 during in vivo aging also involves proteolytic cleavage, although part of the loss might be explained by other mechanisms including the release of vesicles by E.
Mots-clé
Acquired Immunodeficiency Syndrome/*blood Antigens, CD/chemistry/metabolism Antigens, CD55 Antigens, CD59 Cell Separation Erythrocyte Aging Erythrocyte Membrane/*metabolism Humans Membrane Glycoproteins/chemistry/metabolism Papain/pharmacology Peptide Mapping Receptors, Complement 3b/chemistry/*metabolism Trypsin/pharmacology
Pubmed
Web of science
Création de la notice
29/01/2008 13:53
Dernière modification de la notice
20/08/2019 12:59
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