scholarly journals The effect of X-irradiation on membrane lipids of lymphosarcoma cells in vivo and in vitro.

1982 ◽  
Vol 23 (3) ◽  
pp. 371-384 ◽  
Author(s):  
K. FONCK ◽  
G.L. SCHERPHOF ◽  
A.W.T. KONINGS
Keyword(s):  
Membrane Lipids ◽  
X Irradiation

Effect of X-irradiation on gene expression of rat liver chemokines: in vivo and in vitro studies

2008 ◽  
Vol 46 (01) ◽  
Author(s):  
F Moriconi ◽  
H Christiansen ◽  
H Christiansen ◽  
N Sheikh ◽  
J Dudas ◽  
...  
Keyword(s):  
Gene Expression ◽  
Rat Liver ◽  
In Vitro Studies ◽  
X Irradiation

Heme oxygenase-1 induction by hemin prevents oxidative stress-induced acute cholestasis in the rat

2019 ◽  
Vol 133 (1) ◽  
pp. 117-134 ◽  
Author(s):  
Pamela L. Martín ◽  
Paula Ceccatto ◽  
María V. Razori ◽  
Daniel E.A. Francés ◽  
Sandra M.M. Arriaga ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Heme Oxygenase ◽  
Bile Flow ◽  
Driving Forces ◽  
Membrane Lipids ◽  
Ex Vivo ◽  
Heme Oxygenase 1 ◽  
Canalicular Transporters

Abstract We previously demonstrated in in vitro and ex vivo models that physiological concentrations of unconjugated bilirubin (BR) prevent oxidative stress (OS)-induced hepatocanalicular dysfunction and cholestasis. Here, we aimed to ascertain, in the whole rat, whether a similar cholestatic OS injury can be counteracted by heme oxygenase-1 (HO-1) induction that consequently elevates endogenous BR levels. This was achieved through the administration of hemin, an inducer of HO-1, the rate-limiting step in BR generation. We found that BR peaked between 6 and 8 h after hemin administration. During this time period, HO-1 induction fully prevented the pro-oxidant tert-butylhydroperoxide (tBuOOH)-induced drop in bile flow, and in the biliary excretion of bile salts and glutathione, the two main driving forces of bile flow; this was associated with preservation of the membrane localization of their respective canalicular transporters, bile salt export pump (Bsep) and multidrug resistance-associated protein 2 (Mrp2), which are otherwise endocytosed by OS. HO-1 induction counteracted the oxidation of intracellular proteins and membrane lipids induced by tBuOOH, and fully prevented the increase in the oxidized-to-total glutathione (GSHt) ratio, a sensitive parameter of hepatocellular OS. Compensatory elevations of the activity of the antioxidant enzymes catalase (CAT) and superoxide dismutase (SOD) were also prevented. We conclude that in vivo HO-1 induction protects the liver from acute oxidative injury, thus preventing consequent cholestasis. This reveals an important role for the induction of HO-1 and the consequently elevated levels of BR in preserving biliary secretory function under OS conditions, thus representing a novel therapeutic tool to limit the cholestatic injury that bears an oxidative background.

scholarly journals GENETIC CONTROL OF IMMUNE RESPONSES IN VITRO

1974 ◽  
Vol 140 (3) ◽  
pp. 648-659 ◽  
Author(s):  
Judith A. Kapp ◽  
Carl W. Pierce ◽  
Stuart Schlossman ◽  
Baruj Benacerraf
Keyword(s):  
Immune Response ◽  
T Cells ◽  
Immune Responses ◽  
Cell Function ◽  
Suppressor Cells ◽  
Specific Response ◽  
Spleen Cells ◽  
X Irradiation

In recent studies we have found that GAT not only fails to elicit a GAT-specific response in nonresponder mice but also specifically decreases the ability of nonresponder mice to develop a GAT-specific PFC response to a subsequent challenge with GAT bound to the immunogenic carrier, MBSA. Studies presented in this paper demonstrate that B cells from nonresponder, DBA/1 mice rendered unresponsive by GAT in vivo can respond in vitro to GAT-MBSA if exogenous, carrier-primed T cells are added to the cultures. The unresponsiveness was shown to be the result of impaired carrier-specific helper T-cell function in the spleen cells of GAT-primed mice. Spleen cells from GAT-primed mice specifically suppressed the GAT-specific PFC response of spleen cells from normal DBA/1 mice incubated with GAT-MBSA. This suppression was prevented by pretreatment of GAT-primed spleen cells with anti-θ serum plus C or X irradiation. Identification of the suppressor cells as T cells was confirmed by the demonstration that suppressor cells were confined to the fraction of the column-purified lymphocytes which contained θ-positive cells and a few non-Ig-bearing cells. The significance of these data to our understanding of Ir-gene regulation of the immune response is discussed.

scholarly journals Improved red blood cell preservation correlates with decreased loss of bands 3, 4.1, acetylcholinestrase, and lipids in microvesicles

Blood ◽  
1996 ◽  
Vol 87 (4) ◽  
pp. 1612-1616 ◽  
Author(s):  
UJ Dumaswala ◽  
RU Dumaswala ◽  
DS Levin ◽  
TJ Greenwalt
Keyword(s):  
Fluorescence Anisotropy ◽  
Ache Activity ◽  
Membrane Lipids ◽  
Final Concentration ◽  
Vesicle Membrane ◽  
Rbc Membrane ◽  
Additive Solution ◽  
Cell Preservation

In earlier studies we have shown that a final concentration of 0.69% glycerol in blood mixed with an experimental additive solution, EAS 25, improves the in vitro quality and in vivo survival of red blood cells (RBCs). The objective of this study was to determine if the better preservation of RBCs in EAS 25 is correlated with the improved maintenance of membrane lipids and proteins and decreased vesiculation. Split units of RBCs were stored in Adsol or EAS 25 (mmol/L: adenine 2/2, dextrose 122/110, mannitol 42/55, glycerol 0/150, NaCl 154/50). After 12 weeks storage, RBC and microvesicle membranes were analyzed for cholesterol, phospholipid, diphenyl hexatriene fluorescence anisotropy, and acetylcholinesterase (AchE) activity. Bands 3 and 4.1 were identified in the microvesicle membranes by immunoblotting. The RBC membrane cholesterol, phospholipids, and AchE remained higher in EAS 25 than in Adsol (P < .001). Vesicle membrane lipids and AchE in EAS 25 were significantly less than in Adsol (P < .001). The fluidity of stored cells in both the solutions was greater than the prestorage samples. Immunoblotting analyses showed that bands 3 and 4.1 were greatly reduced in the microvesicle membranes shed by the RBCs stored in EAS 25 compared with those formed in Adsol.

THE ROLE OF THIOL GROUPS IN THE DEVELOPMENT OF RADIATION DAMAGE IN THYMOCYTES AND EHRLICH ASCITES CARCINOMA CELLS

1964 ◽  
Vol 42 (12) ◽  
pp. 1717-1727 ◽  
Author(s):  
J. F. Scaife
Keyword(s):  
Ehrlich Ascites Carcinoma ◽  
Carcinoma Cells ◽  
Irradiation Damage ◽  
Thiol Groups ◽  
Protein Thiol ◽  
Ehrlich Ascites ◽  
X Irradiation ◽  
The Difference

The effect of 800–1000 rads of X-irradiation on the thiol content of thymocytes and Ehrlich ascites carcinoma cells has been compared. Four hours after irradiation there was a decrease in the non-protein thiol (NP.SH) content of thymus and thymocytes but no change in ascites cells. In both cells the main NP.SH compound was glutathione. There was no significant effect of irradiation on the protein thiol (P.SH) content of thymus or ascites cells, but there was a slight decrease in P.SH in thymocytes after 4 hours incubation. Isolated thymus nuclei showed an immediate small decrease in P.SH content following 800 rads in vitro. Nuclei isolated from rat thymus 1 hour after 1000 rads in vivo showed an increase in the SH content of the globulin fraction and a decrease in the SH content of the nucleohistones. The total SH content of thymocytes and ascites cells was reduced by slow diffusion of H2O2into the cell suspension, but no effect of prior irradiation on this decrease of SH was found. Inhibition of catalase in vivo and in vitro did not produce any of the morphological signs of irradiation damage in thymocytes. There was no effect of irradiation on the copper content of thymus, thymocytes, or ascites cells. The ratio of NP.SH/P.SH is higher in thymocytes than in ascites cells, but, allowing for the difference in cell size, the overall total thiol concentration was the same. Anoxia produced only a small increase in NP.SH content in both cells and a small and doubtful increase in P.SH. It is concluded that, if thiol groups are involved in cell sensitivity to radiation, only a small fraction of the total SH groups are involved at critical sites.

Response of Cells in Vitro and Tissues in Vivo to Hyperthermia and X-Irradiation

1976 ◽  
pp. 211-227 ◽  
Author(s):  
Donald E. Thrall ◽  
Leo E. Gerweck ◽  
Edward L. Gillette ◽  
William C. Dewey
Keyword(s):  
X Irradiation

scholarly journals Modulation Effects of Curcumin on Erythrocyte Ion-Transporter Activity

2015 ◽  
Vol 2015 ◽  
pp. 1-8 ◽  
Author(s):  
Prabhakar Singh ◽  
Syed Ibrahim Rizvi
Keyword(s):  
Oxidative Stress ◽  
Membrane Lipids ◽  
Curcuma Longa ◽  
Membrane Lipid ◽  
Membrane Transporters ◽  
Protective Mechanism ◽  
Lipid Hydroperoxides ◽  
Beneficial Effects

Curcumin ((1E,6E)-1,7-Bis(4-hydroxy-3-methoxyphenyl)-1,6-heptadiene-3,5-dione), the yellow biphenolic pigment isolated from turmeric (Curcuma longa), has various medicinal benefits through antioxidation, anti-inflammation, cardiovascular protection, immunomodulation, enhancing of the apoptotic process, and antiangiogenic property. We explored the effects of curcuminin vitro(10−5 M to 10−8 M) andin vivo(340 and 170 mg/kg b.w., oral) on Na+/K+ATPase (NKA), Na+/H+exchanger (NHE) activity, and membrane lipid hydroperoxides (ROOH) in control and experimental oxidative stress erythrocytes of Wistar rats. As a result, we found that curcumin potently modulated the membrane transporters activity with protecting membrane lipids against hydro-peroxidation in control as well as oxidatively challenged erythrocytes evidenced by stimulation of NKA, downregulation of NHE, and reduction of ROOH in the membrane. The observed results corroborate membrane transporters activity with susceptibility of erythrocyte membrane towards oxidative damage. Results explain the protective mechanism of curcumin against oxidative stress mediated impairment in ions-transporters activity and health beneficial effects.

scholarly journals In vivo analysis reveals substrate-gating mutants of a rhomboid intramembrane protease display increased activity in living cells

2008 ◽  
Vol 389 (8) ◽  
Author(s):  
Sinisa Urban ◽  
Rosanna P. Baker
Keyword(s):  
Enzyme Activity ◽  
Active Site ◽  
Membrane Lipids ◽  
Fold Increase ◽  
Living Cells ◽  
Transmembrane Segment ◽  
Intramembrane Proteases ◽  
Gating Mechanism

Abstract Intramembrane proteases hydrolyze peptide bonds within cell membranes. Recent crystal structures revealed that rhomboid intramembrane proteases contain a hydrated active site that opens to the outside of the cell, but is protected laterally from membrane lipids by protein segments. Using Escherichia coli rhomboid (GlpG) structures as a guide, we previously took a mutational approach to identify the GlpG gating mechanism that allows substrates to enter the active site laterally from the membrane. Mutations that weaken contacts keeping the gate closed increase enzyme activity and implicate transmembrane segment 5 as the substrate gate. Since these analyses were performed in vitro with pure proteins in detergent micelles, we have now examined GlpG in its natural environment, within the membrane of live E. coli cells. In striking congruity with in vitro analysis, gate-opening mutants in transmembrane segment 5 display up to a 10-fold increase in protease activity in living cells. Conversely, mutations in other parts of the protease, including the membrane-inserted L1 loop previously thought to be the gate, decrease enzyme activity. These observations provide evidence for the existence of both closed and open forms of GlpG in cells, and show that inter-conversion between them via substrate gating is rate limiting physiologically.

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