scholarly journals Phospholipid synthesis in HeLa cells exposed to immunoglobulin G and complement

1972 ◽  
Vol 128 (4) ◽  
pp. 953-960 ◽  
Author(s):  
Flemming Güttler

1. HeLa cells were cultured in the presence of heterologous immunoglobulin G and guinea-pig serum together with [32P]phosphate. 2. Incorporation of [32P]phosphate was significantly stimulated by anti-HeLa immunoglobulin G and complement-sufficient serum compared with immunoglobulin G from unimmunized rabbits and complement. Within 2.5h heat-inactivated guinea-pig serum and anti-HeLa immunoglobulin G stimulated [32P]phosphate incorporation to the same extent as heat-inactivated complement and immunoglobulin G from unimmunized rabbits. 3. Compared with cells exposed to immunoglobulin G from unimmunized rabbits together with complement, anti-HeLa immunoglobulin G with complement increased the phospholipid content of HeLa cells twofold within 5h of incubation. 4. Exposure of HeLa cells to anti-HeLa immunoglobulin G and complement for 5–22h resulted in a twofold increase in the net accumulation of [32P]phosphate in sphingomyelin and phosphatidylcholine and a 50% increase in the net accumulation of [32P]phosphate in phosphatidylethanolamine, compared with cultures exposed to immunoglobulin G from unimmunized rabbits and complement. 5. A transient accumulation of 32P-labelled lysophosphoglycerides in HeLa cells exposed to antibody and complement was detected, confirming previous findings (Güttler & Clausen, 1969b). 6. The stimulation of [32P]phosphate turnover occurred in cells filling up their cytoplasma with vacuoles. This supports the suggestion that the accumulation of phospholipid in these cells may be concerned with the synthesis and function of cytomembranes.

Allergy ◽  
1993 ◽  
Vol 48 (8) ◽  
pp. 608-614 ◽  
Author(s):  
M. Al-Laith* ◽  
A. Weyer ◽  
N. Havet ◽  
C. Dumarey ◽  
B. B. Vargaftig ◽  
...  

1988 ◽  
Vol 251 (1) ◽  
pp. 189-194 ◽  
Author(s):  
G Jakab ◽  
S T Rapundalo ◽  
R J Solaro ◽  
E G Kranias

Phosphorylation of phospholipids was studied in Langendorff perfused guinea pig hearts subjected to beta-adrenergic stimulation. Hearts were perfused with Krebs-Henseleit buffer containing [32P]Pi and freeze-clamped in a control condition or at the peak of the inotropic response to isoprenaline. 32P incorporation into total phospholipids, individual phospholipids and polyphosphoinositides was analysed in whole tissue homogenates and membranes, enriched in sarcoplasmic reticulum, prepared from the same hearts. Isoprenaline stimulation of the hearts did not result in any significant changes in the levels of phosphate incorporation in the total phospholipid present in cardiac homogenates (11.6 +/- 0.4 nmol of 32P/g for control hearts and 12.4 +/- 0.5 nmol of 32P/g for isoprenaline-treated hearts; n = 6), although there was a significant increase in the degree of phospholipid phosphorylation in sarcoplasmic reticulum (3.5 +/- 0.3 nmol of 32P/mg for control hearts and 6.7 +/- 0.2 nmol of 32P/mg for isoprenaline-treated hearts; n = 6). Analysis of 32P incorporation into individual phospholipids and polyphosphoinositides revealed that isoprenaline stimulation of the hearts was associated with a 2-3-fold increase in the degree of phosphorylation of phosphatidylinositol monophosphate and bisphosphate as well as phosphatidic acid in both cardiac homogenates and sarcoplasmic reticulum membranes. In addition, there was increased phosphate incorporation into phosphatidylinositol in sarcoplasmic reticulum membranes. Thus, perfusion of guinea pig hearts with isoprenaline is associated with increased formation of polyphosphoinositides and these phospholipids may be involved, at least in part, in mediating the effects of beta-adrenergic agents in the mammalian heart.


Blood ◽  
1969 ◽  
Vol 34 (4) ◽  
pp. 472-476 ◽  
Author(s):  
GERMANO SALVATORELLI ◽  
ANNA MARIA GULINATI ◽  
PAOLO DEL GRANDE

Abstract It is demonstrated that anemic guinea pig serum maintains erythropoiesis in organotypic cultures of fetal guinea pig liver for at least 14 days. The action of the anemic serum seems be due to the stimulation of the differentiation of stem-cells into erythroblasts. If fetal guinea pig liver is cultured on normal serum the cytodifferentiation stops during the first days of culture whereas the maturation of normoblasts can continue for a few days. The number of stem-cells diminishes considerably and after 4 days they all disappear. On the contrary in culture on anemic serum, their number is unaltered even after two weeks in culture and this seems to indicate that the anemic serum displays a favorable action in the maintenance of the pool of undifferentiated cells in the explants.


1993 ◽  
Vol 264 (3) ◽  
pp. H791-H797 ◽  
Author(s):  
L. Talosi ◽  
I. Edes ◽  
E. G. Kranias

The changes in 32P labeling of phosphoproteins were studied in Langendorff-perfused guinea pig hearts during reversal of the stimulatory effects of isoproterenol. Exposure of the hearts to isoproterenol was associated with significant increases in adenosine 3',5'-cyclic monophosphate (cAMP) levels and in the phosphate incorporation into phospholamban in sarcoplasmic reticulum, the 15-kDa protein in the sarcolemma, and troponin I in the myofibrils. Phospholamban was phosphorylated on serine and threonine residues, both of which are sites for cAMP-dependent and Ca(2+)-calmodulin-dependent protein kinases, respectively. Termination of isoproterenol infusion was associated with reversal of the mechanical effects of isoproterenol stimulation and reversal of the increases in tissue cAMP levels. However, the decreases in cAMP levels correlated only with dephosphorylation of phosphoserine in phospholamban. Dephosphorylation of phosphothreonine in phospholamban, the 15-kDa sarcolemmal protein, and troponin I occurred at a slower rate. These findings suggest that cAMP-dependent phosphorylation of phospholamban (phosphoserine) may play a prominent role during beta-adrenergic stimulation of intact hearts.


1971 ◽  
Vol 1 (4) ◽  
pp. 309-311 ◽  
Author(s):  
M. P. Dierich ◽  
D. Bitter-Suermann ◽  
W. König ◽  
U. Hadding

1963 ◽  
Vol 10 (01) ◽  
pp. 120-132 ◽  
Author(s):  
E. S Olesen

SummaryTreatment of serum with bentonite led to a reduced content of inhibitors of trypsin and urokinase in the isoelectrically precipitated euglobulin, and removed fibrinolytic agents and precursors from serum. Bentonite-treated serum added to untreated serum reduced precipitation of the above inhibitors, and presumably also precipitation of inhibitors against a plasminogen activator of serum.Bentonite-treated serum (whether from pig, ox, guinea-pig, or man), added to untreated guinea-pig serum, produced fibrinolytic activity on isoelectric precipitation of the mixture; the activity of the euglobulin was due to an activator of plasminogen as well as an active protease, probably plasmin. The described effects of bentonite-treated serum are similar to those previously reported for anionic polyelectrolytes. Possible mechanisms are discussed.The “non-specific” activation of fibrinolytic activity by means of bentonite emphasizes that guinea-pig serum [which is characterized by a high potential for “nonspecific” activation of its fibrinolytic system Olesen (1962)] contains all the elements required for the formation of an activator of plasminogen, and thus the activation of its plasminogen to plasmin.


1975 ◽  
Vol 142 (5) ◽  
pp. 1065-1077 ◽  
Author(s):  
A.P. Osmand ◽  
R.F. Mortensen ◽  
Joan Siegel ◽  
H. Gewurz

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.


1963 ◽  
Vol 4 (1) ◽  
pp. 64-84
Author(s):  
I. Koefoed Jensen
Keyword(s):  

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