Fab fragments from intravenous immunoglobulin prevent hyperacute rejection in the guinea pig-to-rat combination without reducing hemolytic complement activity in rat serum

2000 ◽  
Vol 32 (8) ◽  
pp. 2707-2709 ◽  
Author(s):  
L Urbani ◽  
J Cardoso ◽  
O Soubrane ◽  
D Houssin ◽  
C Gautreau
Keyword(s):  
Guinea Pig ◽  
Intravenous Immunoglobulin ◽  
Hyperacute Rejection ◽  
Rat Serum ◽  
Complement Activity ◽  
Fab Fragments ◽  
Hemolytic Complement Activity

Complement is not involved in monocrotaline pyrrole-induced pulmonary injury

1988 ◽  
Vol 254 (2) ◽  
pp. H258-H264
Author(s):  
L. H. Bruner ◽  
K. J. Johnson ◽  
G. O. Till ◽  
R. A. Roth
Keyword(s):  
Lung Injury ◽  
Complement Activation ◽  
Pulmonary Injury ◽  
Serum Complement ◽  
Rat Serum ◽  
Complement Activity ◽  
Hemolytic Complement Activity ◽  
Monocrotaline Pyrrole

Monocrotaline pyrrole (MCTP) causes pulmonary vascular injury, pulmonary hypertension, and right ventricular hypertrophy in rats. The mechanisms by which MCTP causes lung injury are not known. After treatment with a moderate dose of MCTP, several days pass before major lung injury is detected, thus suggesting that the damage is caused indirectly. Since activation of the complement system can cause lung injury, it was of interest to test whether complement activation may be important in lung injury due to MCTP. Accordingly, rats were given a single dose of MCTP (3.5 mg/kg iv), and serum hemolytic complement activity was measured at several times after rats were treated. Neutrophil aggregometry also was used to determine whether complement activation products could be detected in serum after MCTP was given in vivo. The effect of complement depletion on MCTP-induced pulmonary injury was tested by cotreating rats with purified cobra venom factor and MCTP. MCTP treatment did not cause detectable complement activation in vivo, and complement depletion did not protect rats from lung injury. The direct effect of MCTP on serum complement also was tested by exposing fresh rat serum to MCTP in vitro and measuring serum complement activity. MCTP decreased serum hemolytic complement activity in vitro, but it did not interfere with subsequent zymosan-induced activation of complement. These results suggest that complement does not play a role in the development of major lung injury that occurs several days after treatment of rats with MCTP.

scholarly journals The complement activity of canine serum

1957 ◽  
Vol 55 (3) ◽  
pp. 402-413 ◽  
Author(s):  
N. M. Larin ◽  
Rachel Gaddum ◽  
W. G. Orbell
Keyword(s):  
Guinea Pig ◽  
Technical Assistance ◽  
Specific Activity ◽  
Virus Antigen ◽  
Haemolytic Activity ◽  
Complement Activity ◽  
Undiluted Serum ◽  
Protein Particle ◽  
Canine Serum ◽  
Fixation Reaction

Quantitative studies have shown that the haemolytic activity of canine complement was in all essentials similar to guinea-pig complement. Canine serum which had been heated at 56° C. markedly enhanced the haemolytic activity of canine complement. The complement-enhancing power of heated canine serum was found to be increased with the concentration of serum up to 20%. Further concentration up to 50 % serum dilution, or the use of undiluted serum, resulted in a reduction of this effect.Serum aliquots were either pro-complementary or anti-complementary to cn, depending on whether they were heated at 56 or 62° C.Factors that possibly affect the complement-enhancement were investigated and evidence is presented which indicates that the electric charge on the protein particle is probably responsible for either the pro-complementary or anti-complementary serum activity; the mechanism of this, however, still remains obscure.The present work shows also that canine complement can be used instead of guinea-pig complement for testing canine sera with virus antigen by the complement-fixation reaction, an advantage of this being that the use of canine complement permits the testing of canine sera which are anti-complementary to guinea-pig complement.The data obtained are discussed in relation to canine complement and its specific activity.The authors are indebted to Professor W. I. B. Beveridge for his constructive advice, to Dr R. R. A. Coombs for his helpful comments on the complement activity, and to Dr Christine E. Rice of the Animal Diseases Research Institute, Canada, who has generously supplied the zymosan.Miss W. Barr and Miss M. Baker gave fine technical assistance throughout all the experiments. Miss M. Lambourne assisted in preparing the manuscript and graphs.

Early Decrease in Total Hemolytic Complement Activity (CH100) after Fasting or Intestinal Bypass in the Rat

1986 ◽  
Vol 18 (1) ◽  
pp. 36-40
Author(s):  
M. Montanari ◽  
V. Violi ◽  
M. Muri ◽  
L. Roncoroni ◽  
G. Mora ◽  
...  
Keyword(s):  
Intestinal Bypass ◽  
Complement Activity ◽  
Hemolytic Complement Activity

scholarly journals LOCALIZATION OF POLYSOME-BOUND ALBUMIN AND SERINE DEHYDRATASE IN RAT LIVER CELL FRACTIONS

1973 ◽  
Vol 59 (1) ◽  
pp. 28-44 ◽  
Author(s):  
Yukio Ikehara ◽  
Henry C. Pitot
Keyword(s):  
Serum Albumin ◽  
Rat Liver ◽  
Significant Degree ◽  
Rabbit Serum ◽  
Chow Diet ◽  
Rat Serum ◽  
Fab Fragments ◽  
Serine Dehydratase ◽  
Membrane Bound ◽  
Rat Serum Albumin

The polysomes involved in albumin and serine dehydratase synthesis were identified and localized by the binding to rat liver polysomes of anti-rat serum albumin and anti-serine dehydratase [125I]Fab dimer and monomer. Techniques were developed for the isolation of undegraded free and membrane-bound polysomes and for the preparation of [125I]Fab monomers and dimers from the IgG obtained from the antisera to the two proteins, rat serum albumin and serine dehydratase. The distribution of anti-rat serum albumin [125I]Fab dimer in the polysome profile is in accordance with the size of polysomes that are expected to be synthesizing albumin. By direct precipitation, it has been demonstrated that nascent chains isolated from the membrane-bound polysomes by puromycin were precipitated by anti-rat serum albumin-IgG at a level of 5–6 times those released from free polysomes. Anti-rat serum albumin-[125I]Fab dimer reacted with membrane-bound polysomes almost exclusively compared to the binding of nonimmune, control [125I]Fab dimer; a significant degree of binding of anti-rat serum albumin-[125I]Fab to free polysomes was also obtained. The [125I]Fab dimer made from normal control rabbit serum does not react with polysomes from liver at all and this preparation will not interact with polysomes extracted from tissues that do not synthesize rat serum albumin. Both anti-serine dehydratase-[125I]Fab monomer and dimer react with free and bound polysomes from livers of animals fed a chow diet or those fed a high 90% protein diet and given glucagon. In the latter instance, however, it is clear that the majority of the binding occurs to the bound polysomes. Furthermore, the specificity of this reaction may be further shown by the use of kidney polysomes that do not normally synthesize serine dehydratase. When these latter polysomes are isolated, even after the addition of crude and purified serine dehydratase, no reaction with anti-serine dehydratase-Fab fragments could be demonstrated. These results indicate that the reaction of the Fab fragments are specific for polysomes that synthesize rat serum albumin or rat liver serine dehydratase. Furthermore, they demonstrate that even with this high degree of specificity, some polysomes in the fraction labeled "free" are in the process of synthesizing rat serum albumin while bound polysomes to a significant, if not major, degree are the site of the synthesis of rat liver serine dehydratase.

Inactivation of hemolytic actiyities of serum complement by phenothiazines

1969 ◽  
Vol 47 (5) ◽  
pp. 547-552 ◽  
Author(s):  
Thomas S. S. Mao ◽  
Joseph J. Noval ◽  
Paul Pellerin ◽  
Otto J. Plescia
Keyword(s):  
Guinea Pig ◽  
Potent Inhibitor ◽  
Relative Effectiveness ◽  
Serum Complement ◽  
Complement Components ◽  
Complement Activity ◽  
Complement Level

The hemolytic titers of human and guinea pig sera were greatly reduced by pretreatment with any of several phenothiazines. The anti-complement activity of the phenothiazines depended on the nature of substituents at positions 2 and 10. In the promazine group, the relative effectiveness of the position-2 substituents was in the order H > Cl > OCH3 > CF3. The presence of a piperazinyl group in the chain at position 10 conferred strong anti-complement activity. Thioridazine was the most potent inhibitor among the 12 phenothiazines studied. Complement components C′2 and C′4 in both human and guinea pig sera were more sensitive than other components to inactivation by phenothiazines. Phenothiazines administered orally in moderate doses did not lower the complement level of serum in three subjects. There was no correlation between anti-complement activity of the phenothiazines and their relative therapeutic potency.

scholarly journals Study of hemolytic activity and subfactors of complement in smokers intoxication

2019 ◽  
Author(s):  
Rojan Ghanim Al Allaf
Keyword(s):  
Hemolytic Activity ◽  
Normal Values ◽  
Control Group ◽  
Healthy Individuals ◽  
Complement Components ◽  
Complement Activity ◽  
Normal People ◽  
Hemolytic Complement Activity ◽  
Heavy Smokers

Abstract Heavy Smokers appeared to be less resistant to infection, such as bacteria, viruses, and parasites. Many studies have examined the complement components concentrations than compared with normal people and ignored the functional sequencing of complement components, our study included the determination of complement activity by using Sheep red blood cells (SRBCs) as antigen and extracting the hemolytic activity (50%) of complement compounds, and because of difficulty of this method we using statistical analysis program (SPSS 23) and derived the inverse equation which gives the decomposition percentage (1-100%) of complement components by using five serum dilutions only. The total hemolytic complement activity (CH50) and its C3 and C4 fractions were determined in 30 heavy smokers. The results were compared with a control group that contained 30 persons matched in age and sex. Generally, both C3 and C4 concentrations were increased in smoker's individual in compared with the control group. However, when the independent t-test has applied the differences in the C3 and C4 levels in the control group (healthy individuals) and in the smoker group were found to be statistically insignificant but the inverse equation showed a 7% reduction in CH50 in smokers compared with the control group, where 18% reduction was observed. Our current study suggests that the complement components of the heavy smokers suffer from a significant dysfunction in the function, although the concentration of the basic components in the serum is parallel with normal values.

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