scholarly journals Humoral immunostimulation. IV. Role of complement.

1975 ◽  
Vol 141 (4) ◽  
pp. 736-752 ◽  
Author(s):  
W T Shearer ◽  
J P Atkinson ◽  
M M Frank ◽  
C W Parker
Keyword(s):  
Cell Growth ◽  
Guinea Pig ◽  
Human Serum ◽  
Calf Serum ◽  
Rabbit Serum ◽  
Mouse Serum ◽  
Low Concentrations ◽  
High Concentrations ◽  
Nucleoside Uptake ◽  
Pig Serum

When L cells were treated with anti-L-cell antibody in medium containing heat-inactivated fetal calf serum, nucleoside uptake and cell growth were stimulated. The response was markedly increased when fresh, unheated sera from calves, guinea pigs, humans, mice, or rabbits were also present. The factors in unheated serum responsible for the enhancement of immunostimulation were studied. Using low concentrations of sera deficient in various complement (C) components and low concentrations of antibody no augmentation of immunostimulation was seen with Clr-deficient human serum, C2-deficient human serum, C2,4-deficient human serum, C4-deficient guinea pig serum, C3-C9-depleted guinea pig serum (by administration of cobra venom factor to animals), but stimulation was observed with C5-deficient human serum, C5-deficient mouse serum, and C6-deficient rabbit serum. When the concentration of anti-serum was raised, however, augmentation was observed with C4-deficient guinea pig serum. Thus, at low concentrations of antiserum enhancement appeared to occur through the classical C pathway, whereas at high concentrations of antibody either the classical or alternate C pathways appeared to be involved. Stimulation was specifically restored by purified C2 in C2-deficient serum and by C3 in C3-C9-deficient serum. Under the usual reaction conditions consumption of guinea pig C component C4 could be demonstrated which provided direct evidence for activation of the classical C pathway under conditions leading to immunostimulation. By immunofluorescence, cells treated with antibody and normal human serum had human C3 deposited at the cell surface. Taken together these observations suggest that C activated through C3 by either the classical or alternate pathways has the potential to enhance nucleoside incorporation into DNA and cell growth of cells exposed to limiting amounts of antibody. Although the mechanism of stimulation is unknown, it is likely to involve a direct effect of C3 at the level of the cell membrane.

scholarly journals Interactions of C-reactive protein with the complement system. III. Complement-dependent passive hemolysis initiated by CRP.

1975 ◽  
Vol 142 (5) ◽  
pp. 1065-1077 ◽  
Author(s):  
A.P. Osmand ◽  
R.F. Mortensen ◽  
Joan Siegel ◽  
H. Gewurz
Keyword(s):  
Guinea Pig ◽  
Human Serum ◽  
Complete System ◽  
Gel Filtration ◽  
C Reactive Protein ◽  
Inflammatory Reactions ◽  
Reactive Protein ◽  
Rabbit Igg ◽  
The Complement System ◽  
Pig Serum

Interactions of CRP with various substrates in the presence of human serum have been shown to result in efficient activation of C components C1-C5. We now report the ability of CRP to initiate C-dependent hemolysis. For this purpose CRP was isolated by affinity chromatography using pneumococcal CPS and gel filtration; its purity was established by several criteria. Erythrocytes were coated with CPS (E-CPS) and passively sensitized with CRP. C-dependent lysis of these cells was observed upon the addition of suitably absorbed human serum, and the efficiency of hemolysis compared favorably with that initiated by rabbit IgG anti-CPS antibody. CRP also sensitized E-CPS for lysis by guinea pig C; partial lysis was seen when C4-deficient guinea pig serum was used, suggesting that CRP also shares with antibody the ability of CRP to fully activate the C system and provide further evidence for a role for CRP similar to that of antibody in the initiation and modulation of inflammatory reactions via the complete system.

scholarly journals Control by fibroblast growth factor of differentiation in the BC3H1 muscle cell line.

1985 ◽  
Vol 100 (5) ◽  
pp. 1540-1547 ◽  
Author(s):  
B Lathrop ◽  
E Olson ◽  
L Glaser
Keyword(s):  
Growth Factor ◽  
Cell Growth ◽  
Fibroblast Growth Factor ◽  
Cell Line ◽  
Calf Serum ◽  
Specific Protein ◽  
Fibroblast Growth ◽  
Mouse Muscle ◽  
Differentiated Cells ◽  
High Concentrations

The regulation of creatine phosphokinase (CPK) expression by polypeptide growth factors has been examined in the clonal mouse muscle BC3H1 cell line. After arrest of cell growth by exposure to low concentrations of serum, BC3H1 cells accumulate high levels of muscle-specific proteins including CPK. The induction of this enzyme is reversible in the presence of high concentrations of fetal calf serum, which cause quiescent, differentiated cells to reenter the cell cycle. Under these conditions, the rate of CPK synthesis is drastically reduced. We show in the present communication that either pituitary-derived fibroblast growth factor (FGF) or brain-derived FGF are as effective as serum in repressing the synthesis of CPK when added to quiescent, differentiated cells. The decrease in the rate of synthesis of CPK occurs within 22 h after the addition of pituitary FGF to the cells. Pituitary FGF had very little effect, if any, on the rate CPK degradation. The overall rate of protein synthesis and the pattern of synthesis of the major polypeptides made by these cells was not altered by the addition of FGF. Although pituitary FGF was mitogenic for BC3H1 cells, the rate of cell growth was not absolutely correlated with the extent of repression of CPK. Brain-derived FGF fully repressed CPK induction under conditions where it showed no significant mitogenic activity. These results show that the expression of a muscle-specific protein, CPK, can be controlled by a single defined polypeptide growth factor in fully differentiated cultures, and that initiation of cell division is not required for their regulation to take place.

INCORPORATION OF INORGANIC P32INTO PHOSPHOLIPIDS OF BRAIN SLICES: EFFECT OF CERTAIN TRANQUILLIZING DRUGS

1963 ◽  
Vol 41 (1) ◽  
pp. 1155-1162 ◽  
Author(s):  
W. L. Magee ◽  
R. J. Rossiter
Keyword(s):  
Methylene Blue ◽  
Guinea Pig ◽  
Aerobic Glycolysis ◽  
Brain Slices ◽  
Inorganic P ◽  
Pig Brain ◽  
Low Concentrations ◽  
High Concentrations ◽  
Derivatives Of ◽  
Guinea Pig Brain

Promazine, promethazine, tetrameprazine, and WY 1172, four tranquillizing drugs that are derivatives of phenothiazine, resembled chlorpromazine in that when they were added in a concentration of 0.1 mM to slices of guinea pig brain respiring in a suitable medium they stimulated the incorporation of inorganic P32into the phospholipids of the slices. With one of the drugs, promethazine, this concentration of 0.1 mM was found to cause no significant increase in respiration, in aerobic glycolysis, or in the concentration of phosphocreatine. In higher concentrations (1.0 mM), all of the compounds inhibited the labelling of phospholipid. Promethazine caused a reduction in respiration and in the concentration of phosphocreatine, accompanied by an increase in aerobic glycolysis. Methylene blue, a derivative of phenothiazine with no reported tranquillizing properties, did not stimulate the labelling of phospholipid in brain slices. Azacyclonol, pipradrol, and mepazine, drugs that are derivatives of piperidine, also stimulated phospholipid labelling in low concentrations and inhibited the labelling at higher concentrations. Piperidine and benzhydrol, the two components from which azacyclonol is derived, did not stimulate phospholipid labelling at the concentration which was most effective for azacyclonol. Low concentrations of benzhydrol, however, caused a slight stimulation. Meprobamate and phenaglycodol, two other compounds with reputed tranquillizing action, had either little or no effect. Most of the substances tested inhibited phospholipid labelling when they were added in sufficiently high concentrations.

scholarly journals THE MECHANISM OF ANAPHYLATOXIN FORMATION

1914 ◽  
Vol 20 (1) ◽  
pp. 37-51 ◽  
Author(s):  
James W. Jobling ◽  
William Petersen
Keyword(s):  
Guinea Pig ◽  
Diphtheria Toxin ◽  
Serum Proteins ◽  
Horse Serum ◽  
Cobra Venom ◽  
Rabbit Serum ◽  
Partial Removal ◽  
The Matrix ◽  
Previously Treated ◽  
Pig Serum

1. The unsaturated lipoids (serum antitrypsin) can be adsorbed from guinea pig serum, rabbit serum, and horse serum by kaolin, starch, agar, and bacteria. 2. Diphtheria toxin and cobra venom also reduce the serum antitrypsin, possibly because of their affinity for lipoids. 3. Anaphylatoxins represent sera rendered toxic by partial removal of serum antitrypsin. 4. The matrix of the protein split products lies in the serum proteins so exposed. 5. The amount of removal of serum antitrypsin depends on definite quantitative relations; very large amounts and very small amounts of adsorbing substances are least effective (kaolin, starch, and bacteria). 6. Bacteria previously treated with serum or with oils do not adsorb serum antitrypsin. 7. Bacteria treated with serum become more resistant to the action of trypsin.

scholarly journals QUANTITATIVE CHEMICAL STUDIES ON COMPLEMENT OR ALEXIN

1942 ◽  
Vol 75 (3) ◽  
pp. 285-295 ◽  
Author(s):  
Michael Heidelberger ◽  
Manfred Mayer
Keyword(s):  
Guinea Pig ◽  
Human Serum ◽  
Human Complement ◽  
Modified Method ◽  
Chemical Studies ◽  
Quantitative Chemical ◽  
Pig Serum

1. A modified method is given for the titration of human complement so that C'1 titers are measured, as in guinea pig serum, instead of the C'2 titers yielded by the usual titration. 2. The measurement of complement combining component or components in weight units, instead of relative terms, is carried out as in guinea pig serum and leads to similar values, 0.03 to 0.05 mg. of C' N per ml. of human serum. 3. Other similarities in human and guinea pig complements are noted and discussed.

scholarly journals A Cytochemical Study on the Pancreas of the Guinea Pig

1960 ◽  
Vol 7 (4) ◽  
pp. 631-644 ◽  
Author(s):  
Philip Siekevitz ◽  
George E. Palade
Keyword(s):  
Molecular Structure ◽  
Guinea Pig ◽  
Incubation Medium ◽  
Sedimentation Coefficient ◽  
Dry Weight ◽  
Analytical Ultracentrifuge ◽  
Cytochemical Study ◽  
Low Concentrations ◽  
Proteolytic Activities ◽  
High Concentrations

Ribonucleoprotein (RNP)1 particles isolated by DOC treatment from pancreatic microsomes have a RNA content of 35 to 45 per cent of their dry weight. In the analytical ultracentrifuge about 85 per cent of the material has a sedimentation coefficient of ∼85 S. These particles contain amylase, RNase, and trypsin-activatable proteolytic activities which cannot be washed off or detached by incubation in 0.44 M sucrose. The enzymes are released, however, by incubation in the presence of low concentrations of ATP, PP, or EDTA, and high concentrations of IP and AMP. At the same time, and at the same concentrations, ∼80 per cent of the RNA and ∼25 per cent of the protein of the particles becomes also non-sedimentable. The simultaneous addition of Mg++ to the incubation medium prevents these losses. This finding, together with the observation that all the Mg++ of the particles is released by the same agents, makes it likely that Mg++ holds the particles together, and that its removal by the chelators used causes the particles to disintegrate. These findings are discussed in relation to the molecular structure of the RNP particles.

Action of theophylline on secretagogue-stimulated amylase release from dispersed pancreatic acini

1980 ◽  
Vol 239 (4) ◽  
pp. G324-G333
Author(s):  
L. Y. Korman ◽  
M. D. Walker ◽  
J. D. Gardner
Keyword(s):  
Guinea Pig ◽  
Vasoactive Intestinal Peptide ◽  
Enzyme Secretion ◽  
Amylase Release ◽  
Pancreatic Acini ◽  
Modes Of Action ◽  
Low Concentrations ◽  
High Concentrations ◽  
Stimulation Of

In dispersed acini from guinea pig pancreas, theophylline did not alter basal amylase release, but had three functionally distinct modes of action on the stimulation of amylase release caused by various secretagogues. 1) At relatively low concentrations (0.1-1.0 mM), theophylline augmented the increase in enzyme secretion caused by vasoactive intestinal peptide, secretin, or 8-bromoadenosine 3',5'-monophosphate, but did not alter the increase in amylase release caused by other secretagogues. 2) At intermediate concentrations (1-10 mM), theophylline selectively altered the increase in enzyme secretion caused by carbamylcholine, but did not alter the effects of cholecystokinin or bombesin, secretagogues whose modes of action are similar to that of cabamylcholine. 3) At high concentrations (greater than 10 mM), theophylline inhibited the increase in enzyme secretion caused by all secretagogues tested.

THE EFFECT OF FREE FATTY ACIDS ON RESIN UPTAKE OF TRI-IODOTHYRONINE FROM HUMAN, RAT, RABBIT AND GUINEA-PIG SERUM AND HUMAN SERUM ALBUMIN

1969 ◽  
Vol 45 (4) ◽  
pp. 489-493 ◽  
Author(s):  
P. W. NATHANIELSZ
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Free Fatty Acid ◽  
Human Serum Albumin ◽  
Guinea Pig ◽  
Serum Albumin ◽  
Free Fatty Acids ◽  
Human Serum ◽  
Rat Serum ◽  
Pig Serum

SUMMARY Recently changes in plasma free fatty acids have been suggested as a possible regulator of the levels of free thyroxine in the plasma. Oleic acid has been shown to displace tri-iodothyronine from human serum, human serum albumin, rat serum, rabbit serum and guinea-pig serum. The extent of the displacement, much greater from human serum albumin than from whole serum, suggests that free fatty acid does not affect the globulin binding site. It would also appear that, in the rat, all the binding sites are sensitive to free fatty acids and hence there is probably only albumin binding in this species. The results with rabbit and guinea-pig serum were intermediate to those with human and rat serum. A significant rise in resin uptake of tri-iodothyronine in vitro occurred with an increase of free fatty acid level of 0·5 m-equiv./l., well within the physiological range.

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