Document Detail


The role of complement receptor type 1 (CR1, CD35) in determining the cellular distribution of opsonized immune complexes between whole blood cells: kinetic analysis of the buffering capacity of erythrocytes.
MedLine Citation:
PMID:  9038723     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Erythrocytes (E) express complement receptor, type 1 (CR1, CD35), by which they bind opsonized immune complexes (IC) in competition with leucocytes expressing higher numbers of CR1 as well as other complement- and Fc-receptors. This may prevent inappropriate activation of phagocytic cells. We examined the distribution on whole blood cells of preformed tetanus toxoid (TT)/human anti-TT IC, opsonized in situ in 80% autologous serum. Binding to E occurred rapidly and reflected the kinetics of C3-fragment incorporation into the IC. Among eight donors, expressing 180-361 CR1 per E. > 90% of the cell-bound IC were associated with E from 1 to 5 min of incubation, decreasing to 12 +/- 13% after 40 min. Upon comparison of the IC-binding to leucocytes in whole blood with that of isolated leucocytes we found that E, despite their extensive early complex uptake, only reduced the IC-deposition on polymorphonuclear leucocytes (PMN) by 61 +/- 26% after 30 seconds of incubation and 47 +/- 14% after 5 min. During the subsequent 10 min, this buffering capacity of E was essentially abolished E restricted the initial IC-binding to B cells by 73 +/- 19%, but from 3 min of incubation the presence of E promoted, in a CR1-dependent manner, a progressive uptake via CR2 by the B cells. CR1 was the dominant receptor in the early IC-uptake by B cells as well as PMN and monocytes, since CR1-blockade inhibited the initial IC-uptake by these populations in a preparation of isolated leucocytes suspended in serum by > or = 84% after 30 seconds of incubation. We conclude, that E exert a substantial buffering effect on the IC-deposition on PMN, monocytes and B cells, while CR1 is the dominant receptor in the uptake by these cells. However, this effect is short-lived and less than expected from the proportion of IC bound to E. Moreover, E are efficient processors of IC-attached C3b/iC3b fragments to C3dg as indicated by a pronounced enhancement by E of IC-uptake via CR2 on B cells. We propose that this mechanism may play a role in preventing phagocyte activation via CR3.
Authors:
C H Nielsen; S H Matthiesen; I Lyng; R G Leslie
Related Documents :
22918643 - Effects of simvastatin on the expression of heme oxygenase-1 in human rpe cells.
8386423 - Ultracytochemical study of ouabain-sensitive k(+)-dependent p-nitro-phenylphosphatase a...
23670863 - The use of fish-derived cell lines for investigation of environmental contaminants: an ...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Immunology     Volume:  90     ISSN:  0019-2805     ISO Abbreviation:  Immunology     Publication Date:  1997 Jan 
Date Detail:
Created Date:  1997-03-07     Completed Date:  1997-03-07     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0374672     Medline TA:  Immunology     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  129-37     Citation Subset:  IM    
Affiliation:
Department of Medical Microbiology, Odense University, Denmark.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Adult
Antigen-Antibody Complex / immunology*,  metabolism
B-Lymphocytes / immunology
Cell Culture Techniques
Erythrocytes / immunology*
Female
Humans
Male
Monocytes / immunology
Neutrophils / immunology
Phagocytosis / immunology*
Receptors, Complement 3b / immunology*
Tetanus Toxoid / immunology
Chemical
Reg. No./Substance:
0/Antigen-Antibody Complex; 0/Receptors, Complement 3b; 0/Tetanus Toxoid
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Binding of human and rat CD59 to the terminal complement complexes.
Next Document:  Human dendritic cells handling of binding, uptake and degradation of free and IgG-immune complexed d...