scholarly journals STUDIES ON IMMUNE HUMAN HEMOLYSIS

1961 ◽  
Vol 113 (1) ◽  
pp. 177-192 ◽  
Author(s):  
Carl F. Hinz ◽  
Mary E. Picken ◽  
Irwin H. Lepow

The Donath-Landsteiner reaction was studied using low and high titer antisera and purified antibody, normal and PNH erythrocytes, and human serum complement. The requirement for complement in both the cold and warm phases of the reaction depended upon the level of antibody used and the sensitivity of the cells to hemolytic antibodies. Complement was not necessary in the cold phase using PNH cells and a potent source of antibody, but complement was required to be present at some stage if hemolysis were to occur. Optimal conditions for the cold phase were at 1°C. for 30 minutes at pH 7.4. Ca++ ions were required. Hemolysis in the warm phase occurred within one minute, was optimal at 32°C., and required Mg++. The relation of these observations to previous reports is discussed with respect to discrepant observations on the nature of the Donath-Landsteiner reaction.

1995 ◽  
Vol 69 (12) ◽  
pp. 7430-7436 ◽  
Author(s):  
F L Cosset ◽  
Y Takeuchi ◽  
J L Battini ◽  
R A Weiss ◽  
M K Collins
Keyword(s):  

1984 ◽  
Vol 73 (4) ◽  
pp. 321-329 ◽  
Author(s):  
I. von Zabern ◽  
H. Przyklenk ◽  
R. Nolte ◽  
W. Vogt

1985 ◽  
Vol 76 (3) ◽  
pp. 205-213 ◽  
Author(s):  
I. von Zabern ◽  
R. Nolte ◽  
H. Przyklenk ◽  
W. Vogt

2006 ◽  
Vol 51 (6) ◽  
pp. 627-632 ◽  
Author(s):  
G. Bugla-Płoskońska ◽  
A. Cisowska ◽  
K. Karpińska ◽  
S. Jankowski ◽  
W. Doroszkiewicz

Blood ◽  
1996 ◽  
Vol 87 (6) ◽  
pp. 2329-2336 ◽  
Author(s):  
C Susal ◽  
M Kirschfink ◽  
M Kropelin ◽  
V Daniel ◽  
G Opelz

Recombinant glycoprotein 120 (rgp120) of human immunodeficiency virus type-1 (HIV-1) activates the human complement system in the absence of anti-gp120 antibodies. HIV-1 glycoprotein gp120 can dissociate from the viral envelope either spontaneously or after binding of HIV-1 to the CD4 molecule. As a consequence, gp120 can circulate in the patient's serum and attach to the surface of uninfected CD4+ T cells. Complement activation by cell-bound HIV-1 glycoprotein gp120 with subsequent opsonization may represent a mechanism for the elimination of uninfected CD4+ cells by the reticuloendothelial system, thereby enhancing the progression of HIV disease. In the current study, the complement proteins C4,C3,C5,C9, and properdin were found to bind to a synthetic peptide covering positions 233–251 of the gp120BRU sequence on incubation with normal human serum. Complement activation by the peptide was comparable with that induced by aggregated IgG, complete rgp120, and the previously described complement-activating gp41-peptide 609y623. Activation occurred via the classical pathway and was abrogated in the presence of EDTA, Mg2+/EGTA, or C4-deficient human serum. Peptides partly overlapping the sequence 233–251 activated complement to a lesser extent. The complement-activating capacity of the gp120 sequence 233–251 was not restricted to the HIV-1BRU isolate, because a peptide from the corresponding sequence of the HIV-1MN strain was also capable of activating complement. An additional strong complement-activating site was identified in the gp120 sequence 321–360 of the HIV-1MN strain. These data indicate that distinct sites in gp120 are able to activate human serum complement via the classical pathway in the absence of anti-gp120 and independent of glycosylation.


Blood ◽  
1948 ◽  
Vol 3 (Special_Issue_Number_2) ◽  
pp. 66-79 ◽  
Author(s):  
ERNEST WITEBSKY ◽  
MRS. LIVIA BLUM ◽  
MISS DORIS HOWLES ◽  
MISS HELEN WARD

Abstract The isoantibodies anti-A and anti-B which are described differ in several respects from those occurring in normal human serum. This type of antibody has first been observed in the serum of an Rh negative woman who exhibited a history of erythroblastosis. Her husband belonged to the subtype Rh1 and to the blood group A. The patient’s serum completely neutralized with A and B substances still agglutinated strongly the husband’s cells provided normal human serum replaced physiological saline solution as a diluent for all dilutions. The impression was thus created that an Rh blocking antibody was responsible for the agglutination observed. It could be shown, however, that the abnormal antibody present in this patient’s serum was not an Rh antibody at all but instead, an antibody directed against the A property. This type of anti-A antibody resembles the Rh blocking antibody in many respects. It becomes manifest only if undiluted human serum is used as a diluent. Surprisingly enough this antibody agglutinated cells of group A, although the amount of AB substances added to the serum was sufficient to neutralize completely the isoagglutinin anti-A under normal conditions in which saline solution is used as a diluent. This anti-A antibody therefore cannot be neutralized as easily as the normal isoagglutinin anti-A. For its neutralization much larger amounts of the blood group specific substances are apparently necessary. The patient’s serum fixed complement when mixed with material containing water soluble A substance, in contrast to the normal isoantibody anti-A which failed to do so. The titer of isoantibodies found in the patient’s serum upon titration in saline solution was not extensively high and, as a matter of fact, was average. It is therefore felt that an extremely high titer is neither a necessary requirement nor proof of isoimmunization toward the A and B factors. Another interesting characteristic of the peculiar anti-A antibody occurring in our patient’s serum was the fact that it was essentially an anti-A1 antibody. The difference in agglutination between A1 and A2 cells respectively becomes manifest if normal serum is used as a diluent instead of saline solution. This difference becomes even more marked after neutralization of the patient’s serum with A and B substances. During the course of Mrs. Bong’s pregnancy the special anti-A antibody described did not increase but rather decreased in strength. However, even after delivery the antibody was demonstrable for at least several weeks although we had no opportunity to examine the patient’s serum further. That one must be very careful in contributing any pathological significance to isoantibodies anti-A or anti-B, even of the type described, is evident from the fact that the patient was delivered of a perfectly normal baby belonging to the blood group O and being Rh negative. Whether the difficulties experienced by the patient in previous pregnancies were due to sensitization toward the Rh factor or to the A factor cannot be decided. Antibodies anti-A and anti-B of the type reported were also found in the sera of patients who had received large amounts of pooled plasma or O blood conditioned with A and B specific substances. Again the anti-A antibody occurring in the serum of these patients was mainly directed against the A1 property. Under the experimental conditions described in this paper, such a serum can be used for the differential diagnosis of the subgroups A1 and A2 and constitutes a sensitive reagent for the recognition of the differences occurring within the A factor. With the aid of such a serum only 10 per cent of A cells were found to belong to subgroup A2, 75 per cent to A1, and 15 per cent were considered to be of the intermediate type. No subgroups were found so far in human cells of group B.


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