In Vitro Effects of Sodium Nitroprusside and L-Nω-Nitroarginine Methyl Ester (L-NAME) on Activity of Lysosomal Cysteine Proteinases and Lysosomal Membrane Permeability

2018 ◽  
Vol 165 (1) ◽  
pp. 36-39
Author(s):  
M. A. Fomina ◽  
A. M. Kudlaeva ◽  
S. A. Isakov ◽  
V. V. Davydov
Keyword(s):  
Methyl Ester ◽  
Sodium Nitroprusside ◽  
Membrane Permeability ◽  
Lysosomal Membrane ◽  
Cysteine Proteinases ◽  
In Vitro Effects

scholarly journals First Evidence of In Vitro Effects of C6O4—A Substitute of PFOA—On Haemocytes of the Clam Ruditapes philippinarum

Toxics ◽  
2021 ◽  
Vol 9 (8) ◽  
pp. 191
Author(s):  
Jacopo Fabrello ◽  
Francesca Targhetta ◽  
Maria Ciscato ◽  
Davide Asnicar ◽  
Ilaria Bernardini ◽  
...  
Keyword(s):  
Chromosomal Aberrations ◽  
Superoxide Anion ◽  
Ruditapes Philippinarum ◽  
Membrane Stability ◽  
Lysosomal Membrane ◽  
Superoxide Anion Production ◽  
Anion Production ◽  
Lysosomal Membrane Stability ◽  
In Vitro Effects

Alternative chemicals to per- and poly-fluoroalkyl substances have recently been introduced in various industrial processes. C6O4 (difluoro{[2,2,4,5-tetrafluoro-5-(trifluoromethoxy)-1,3-dioxolan-4-yl]oxy}acetic acid) is a new surfactant and emulsifier used as a replacement for perfluorooctanoic acid (PFOA). From an ecotoxicological point of view, in vitro assays are useful tools for assessing the negative effects and understanding the mechanisms of action of chemicals at the cellular level. Here, we present the results of an in vitro study in which the effects of C6O4 were evaluated—for the first time—on haemocytes of the clam Ruditapes philippinarum. Cells were exposed to three concentrations of C6O4 (0.05, 0.5, 5 μg/mL) and the effects on haemocyte viability, haemocyte morphology, differential haemocyte count, lysosomal membrane stability, superoxide anion production, acid phosphatase, and β-glucuronidase activities, as well as on the percentage of micronuclei and chromosomal aberrations were evaluated. The results demonstrated that C6O4 significantly affected haemocyte morphology, lysosomal membrane stability, hydrolytic enzyme activity, and superoxide anion production, and promoted chromosomal aberrations. To the best of our knowledge, this is the first study revealing the in vitro effects of C6O4, a substitute for PFOA, on haemocytes from a bivalve species.

scholarly journals Inhibitors of benzamidine type influence the virulence properties of Porphyromonas gingivalis strains.

2003 ◽  
Vol 50 (3) ◽  
pp. 725-734 ◽  
Author(s):  
Sigrun Eick ◽  
Wolfgang Pfister ◽  
Uta Stürzebecher ◽  
Sigrid Jarema ◽  
Jörg Stürzebecher
Keyword(s):  
Growth Inhibition ◽  
Negative Control ◽  
Related Structure ◽  
In Vitro Tests ◽  
Cysteine Proteinases ◽  
Amidolytic Activity ◽  
Kb Cells ◽  
In Vitro Effects ◽  
Virulence Properties

Synthetic inhibitors of benzamidine type have been found to have inhibiting effects on arginine specific cysteine proteinases of P. gingivalis. The purpose of our study was to assess the effects of these inhibitors on the virulence properties of two P. gingivalis strains, the reference strain ATCC 33277 and JH16-1, a clinical isolate obtained from a patient with severe periodontitis. The inhibitors tested were pentamidine, benzamidine, three bis-benzamidine derivatives with a pentamidine-related structure, one bis-benzamidine derivative with another structure, and one arginine derivative as a negative control, each in the concentrations of 2 microM and 20 microM. As virulence criteria the following parameters were determined: arginine-specific amidolytic activity, growth inhibition, hemagglutination of sheep erythrocytes, adherence to KB cells and immuno-phagocytosis including intracellular killing. Pentamidine and the bis-benzamidine derivatives with pentamidine-related structure showed the most remarkable effects on reduction of amidolytic activity by 35%, growth inhibition and reduced hemagglutination. Except for the arginine derivative all other inhibitors tested enhanced the phagocytosis capacities of granulocytes. No clear influence of the inhibitors on adherence of P. gingivalis to KB cells was seen. Although in vitro effects of the synthetic inhibitors of cysteine proteinases on virulence of P. gingivalis were observed further in vitro tests concerning immunomodulatory effects should be done before these substances are used for therapy in clinically controlled studies.

In vitro effects of desoxycorticosterone on vascular smooth muscle

1979 ◽  
Vol 237 (2) ◽  
pp. H197-H203
Author(s):  
M. F. Koehler ◽  
R. C. Webb ◽  
A. W. Jones ◽  
D. F. Bohr
Keyword(s):  
Membrane Permeability ◽  
Calcium Binding ◽  
Contractile Response ◽  
Indirect Evidence ◽  
Rabbit Aorta ◽  
Rat Aorta ◽  
Free Solution ◽  
Tetraacetic Acid ◽  
In Vitro Effects

We present evidence in accord with the observations of S. Kalsner (Br. J. Pharmacol. 36: 582-593, 1969) that in the rabbit aorta, desoxycorticosterone (DOC) potentiates the contractile response to certain catecholamines by inhibiting their degradation by catechol-O-methyltransferase. In contrast, DOC depresses the contractile responses in rat aorta and tail arteries. To elucidate the mechanism of this depression the effect of DOC was evaluated under various conditions. DOC depressed the contractile response to epinephrine, phenylephrine, KCl, and angiotensin II. The depression was unaltered by ouabain or by a potassium-free solution, indicating that DOC did not produce its depression by altering Na-K-ATPase activity. The depression is unaltered in a chloride-free solution, demonstrating that the DOC effect is not caused by a change in membrane permeability to chloride. Radioisotope studies demonstrate that DOC does not alter membrane permeability to potassium. Removal of extracellular calcium with EGTA (ethylene glycol-bis (beta-aminoethyl ether) N, N'-tetraacetic acid) significantly reduced the magnitude of the DOC depression. Indirect evidence is presented suggesting that DOC might increase calcium binding to the plasma membrane, resulting in its stabilization and hence in a depression of the contractile response.

scholarly journals Influence of L-Nω-nitroarginine methyl ester and sodium nitroprusside in vitro on the oxidative modification of rat lysosome proteins

2017 ◽  
Vol 98 (6) ◽  
pp. 1005-1011
Author(s):  
M A Fomina ◽  
A M Kudlaeva ◽  
S A Isakov ◽  
A N Ryabkov
Keyword(s):  
Methyl Ester ◽  
Sodium Nitroprusside ◽  
Adaptive Capacity ◽  
Oxidative Modification ◽  
Control Group ◽  
Total Level ◽  
Protein Oxidative Modification ◽  
In Vitro Incubation ◽  
Lysosomal Proteins

Aim. To investigate in vitro effects of 5 mM L-Nω-nitroarginine methyl ester and 0.1 mM sodium nitroprusside on oxidative modification of lysosomal proteins of liver of intact sexually mature female rats of Wistar line. Methods. In the control groups in vitro incubation of isolated lysosomes in the isolation medium for 1, 2 and 4 hours was carried out. Experimental groups were incubated similarly in solutions of 5 mM L-Nω-nitroarginine methyl ester and 0.1 mM sodium nitroprusside. Protein oxidative modification was measured in sedimentary fraction according to R.L. Levine’s method in E.E. Dubinina’s modification. Reserve-adaptive capacity was calculated as the difference between total area under the curve of carbonyl derived proteins after metal-catalyzed oxidation (taken as 100%) and spontaneous oxidation, expressed as a percentage. Results. After 4-hour in vitro incubation 5 mM L-Nω-nitroarginine methyl ester was found to statically significantly increase the total level of protein oxidative modification compared to the control group by 2.41 times and to reduce reserve-adaptive capacity by 4.96 times, and 0.1 mM sodium nitroprusside increases the total level of protein oxidative modification compared to the control group by 2.05 times and reduces reserve-adaptive capacity by 1.56 times. One of the possible mechanisms of this phenomenon may be the reduced activity of lysosomal proteinases. 2-hour and 4-hour in vitro incubation of lysosomes in 5 mM L-Nω-nitroarginine methyl ester is accompanied by an increase of secondary markers of the ratio of protein oxidative modification relatively to 1-hour exposure by 1.18 times and 1.35 times, respectively. At 1-hour in vitro incubation in 0.1 mM sodium nitroprusside, increase of secondary markers of protein oxidative degradation by 1.64 times occurs. Conclusion. The in vitro effect of 5 mM -Nω-nitroarginine methyl ester and 0.1 mM sodium nitroprusside results in visible changes of oxidative modification of rat liver lysosomal proteins.

Anti-obesity role of Aster glehni extract: in vivo and in vitro effects

Planta Medica ◽  
2012 ◽  
Vol 78 (11) ◽  
Author(s):  
HM Lee ◽  
TG Ahn ◽  
CW Kim ◽  
HJ An
Keyword(s):  
In Vitro Effects

In Vitro Effects of Urokinase — Prevention by Different Inhibitors

1990 ◽  
Vol 64 (03) ◽  
pp. 402-406 ◽  
Author(s):  
M D Oethinger ◽  
E Seifried
Keyword(s):  
In Vitro Study ◽  
Thrombin Time ◽  
Plasma Samples ◽  
Temperature Dependent ◽  
Chloromethyl Ketone ◽  
Control Value ◽  
Dose Time ◽  
In Vitro Effects ◽  
Full Protection

SummaryThe present in vitro study investigated dose-, time- and temperature-dependent effects of two-chain urokinase plasminogen activato(u-PA, urokinase) on normal citrated plasma. When 10 μg/ml u-PA wereadded to pooled normal plasma and incubated for 30 min at an ambient temperature (25° C), α2-antiplas-min decreased to 8% of the control value. Incubation on ice yielded a decrease to 45% of control,whereas α2-antiplasmin was fully consumed at 37° C. Fibrinogen and plasminogen fell to 46% and 39%, respectively, after a 30 min incubation at 25° C. Thrombin time prolonged to 190% of control.Various inhibitors were studied with respect to their suitability and efficacy to prevent these in vitro effects. Aprotinin exhibited a good protective effect on fibrinogen at concentrations exceeding 500 KlU/ml plasma. Its use, however, was limited due to interferences with some haemostatic assays. We could demonstrate that L-Glutamyl-L-Glycyl-L-Arginyl chloromethyl ketone (GGACK) and a specific polyclonal anti-u-PA-antibody (anti-u-PA-IgG) effectively inhibited urokinase-induced plasmin generation without interfering with haemostatic assays. The anti-u-PA-antibody afforded full protection ofα2-antiplasmin at therapeutic levels of u-PA.It is concluded that u-PA in plasma samples from patients during thrombolytic therapy may induce in vitro effects which should be prevented by the use of a suitable inhibitor such as GGACK or specific anti-u-PA-antibody.

In Vitro Effects of Ethanol on Rabbit Platelet Aggregation, Secretion of Granule Contents, and Cyclic AMP Levels in the Presence of Prostacyclin

1989 ◽  
Vol 61 (02) ◽  
pp. 254-258 ◽  
Author(s):  
Margaret L Rand ◽  
Peter L Gross ◽  
Donna M Jakowec ◽  
Marian A Packham ◽  
J Fraser Mustard
Keyword(s):  
Cyclic Amp ◽  
Inhibitory Effect ◽  
Rabbit Platelet ◽  
Inhibitory Effects ◽  
Low Concentrations ◽  
Rabbit Platelets ◽  
High Concentrations ◽  
In Vitro Effects ◽  
Aggregation Of Platelets

SummaryEthanol, at physiologically tolerable concentrations, inhibits platelet responses to low concentrations of collagen or thrombin, but does not inhibit responses of washed rabbit platelets stimulated with high concentrations of ADP, collagen, or thrombin. However, when platelet responses to high concentrations of collagen or thrombin had been partially inhibited by prostacyclin (PGI2), ethanol had additional inhibitory effects on aggregation and secretion. These effects were also observed with aspirin- treated platelets stimulated with thrombin. Ethanol had no further inhibitory effect on aggregation of platelets stimulated with ADP, or the combination of ADP and epinephrine. Thus, the inhibitory effects of ethanol on platelet responses in the presence of PGI2 were very similar to its inhibitory effects in the absence of PGI2, when platelets were stimulated with lower concentrations of collagen or thrombin. Ethanol did not appear to exert its inhibitory effects by increasing cyclic AMP above basal levels and the additional inhibitory effects of ethanol in the presence of PGI2 did not appear to be brought about by further increases in platelet cyclic AMP levels.

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