Document Detail

Restriction of cell lysis by homologous complement: I. An analysis of membrane attack complex formation on target membranes.
MedLine Citation:
PMID:  3337896     Owner:  NLM     Status:  MEDLINE    
The hemolytic efficiency and binding of C9 to homologous and heterologous erythrocytes was evaluated by using a standardized passive sensitization procedure to prepare antigen- and antibody-coated erythrocytes (EA) and human serum for lysis. Heterologous bovine EA were readily lysed by human serum, whereas human EA were quite resistant to lysis. Human EA bound as many C8 and C9 molecules per cell as bovine EA when incubated under identical conditions, but four times as much bound C9 was required to lyse an equal number of human EA compared with bovine EA. The susceptibility of human erythrocytes did not increase when increased volumes of undiluted human serum were used although C9 binding increased to as much as 100,000 molecules per cell. Sodium dodecyl sulfate-resistant polymerized C9 (poly(C9)) was detected on both lysed ghosts and unlysed EA bearing complement proteins C1 through C9 (EAC1-9) after incubation with undiluted human serum; however, the ratio of poly(C9) to monomeric C9 was higher on unlysed cells than on ghosts. Although bovine and human EA bound equal amounts of human C9 at the end point, the rate of lysis and C9 uptake was slower on homologous cells. The rate-limiting step occurred before C9 binding and lysis because the rates of lysis and C9 binding were equal on homologous and heterologous EAC1-8 targets, but the extent of lysis of homologous cells was still lower than lysis of heterologous cells. Human erythrocytes lose restriction against homologous hemolysis during storage in autologous plasma or in isotonic buffers.
J J Houle; E M Hoffmann; A F Esser
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Blood     Volume:  71     ISSN:  0006-4971     ISO Abbreviation:  Blood     Publication Date:  1988 Feb 
Date Detail:
Created Date:  1988-03-04     Completed Date:  1988-03-04     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  7603509     Medline TA:  Blood     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  280-6     Citation Subset:  AIM; IM    
Department of Comparative & Experimental Pathology, University of Florida, Gainesville.
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MeSH Terms
Antigen-Antibody Complex
Complement C8 / metabolism
Complement C9 / metabolism*
Complement Membrane Attack Complex
Complement Pathway, Classical
Complement System Proteins / physiology*
Erythrocyte Membrane / metabolism
Species Specificity
Grant Support
Reg. No./Substance:
0/Antigen-Antibody Complex; 0/Complement C8; 0/Complement C9; 0/Complement Membrane Attack Complex; 9007-36-7/Complement System Proteins

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

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