scholarly journals Accurate Prediction of Dose-Dependent CYP3A4 Inhibition by Itraconazole and Its Metabolites From In Vitro Inhibition Data

2010 ◽  
Vol 88 (4) ◽  
pp. 499-505 ◽  
Author(s):  
I Templeton ◽  
C-C Peng ◽  
K E Thummel ◽  
C Davis ◽  
K L Kunze ◽  
...  
Keyword(s):  
Accurate Prediction ◽  
Cyp3a4 Inhibition ◽  
Inhibition Data ◽  
In Vitro Inhibition ◽  
Dose Dependent

In vitro inhibition of phosphodiesterase-5 and arginase activities from rat penile tissue by two Nigerian herbs (Hunteria umbellata and Anogeissus leiocarpus)

2017 ◽  
Vol 28 (4) ◽  
Author(s):  
Ganiyu Oboh ◽  
Adeniyi Abiodun Adebayo ◽  
Ayokunle Olubode Ademosun ◽  
Aline August Boligon
Keyword(s):  
Lipid Peroxidation ◽  
Dependent Manner ◽  
Inhibitory Property ◽  
In Vitro Inhibition ◽  
Anogeissus Leiocarpus ◽  
Dose Dependent ◽  
Phosphodiesterase 5

AbstractBackground:andMethods:The effects of the extracts on important enzymes (PDE-5 and arginase) linked with ED and pro-oxidants (FeResults:The results showed that both extracts inhibited PDE-5 and arginase activities in a dose-dependent manner. Inhibitory property ofConclusions:The ability of the extracts to inhibit PDE-5, arginase and pro-oxidant induced lipid peroxidation, and chelate metal might suggest their folkloric use for the management of ED.

In Vitro Inhibition of the Diphenolase Activity of Tyrosinase by Insecticides and Allelochemicals in Micromelalopha troglodyta (Lepidoptera: Notodontidae)

2009 ◽  
Vol 44 (2) ◽  
pp. 111-119 ◽  
Author(s):  
Fang Tang ◽  
Xin Shen ◽  
Xi-Wu Gao
Keyword(s):  
Tannic Acid ◽  
Dependent Manner ◽  
Insect Development ◽  
Inhibitory Effects ◽  
Emamectin Benzoate ◽  
Lambda Cyhalothrin ◽  
In Vitro Inhibition ◽  
Dose Dependent ◽  
Diphenolase Activity

Tyrosinase is a copper enzyme and plays a key role in normal insect development. We studied the in vitro inhibitory effects of selected insecticides and allelochemicals on the diphenolase activity of tyrosinase in Micromelalopha troglodyta (Graeser) (Lepidoptera: Notodontidae). Two pyrethriods (cyfluthrin and deltamethrin) and 3 other insecticides (hexaflumuron, abamectin and imidacloprid) were the least inhibitory, whereas 5 organophosphates (triazophos, malathion, chlorpyrifos, omethoate and profenofos), 1 carbamate (methomyl), 4 pyrethriods (fenpropathrin, beta-cypermethrin, bifenthrin and lambda-cyhalothrin), 1 organochlorine (endosulfan), 2 allelochemicals (tannic acid and 2-tridecanone) and 4 other insecticides (emamectin benzoate, fipronil, acetamiprid and pyridaben) were moderately inhibitory. Three chemicals (quercetin, phenyl thiourea and phoxim) were the most potent inhibitors of the enzymes among all compounds tested and inhibited the diphenolase activity of tyrosinase in vitro in a dose-dependent manner. Furthermore, phenyl thiourea, phoxim and quercetin showed neither typical competitive nor noncompetitive binding to the substrate, with Ki of 0.13 μM, 49.30 μM and 37.71 μM, respectively.

Increased Protein Synthesis by Human Platelets during Phagocytosis of Latex Particles in Vitro

1976 ◽  
Vol 35 (02) ◽  
pp. 350-357 ◽  
Author(s):  
Hana Bessler ◽  
Galila Agam ◽  
Meir Djaldetti
Keyword(s):  
Protein Synthesis ◽  
Fold Increase ◽  
Human Platelets ◽  
Polystyrene Latex ◽  
Latex Particles ◽  
The Third ◽  
Platelet Protein ◽  
Dose Dependent ◽  
Phagocytotic Activity

SummaryA three-fold increase of protein synthesis by human platelets during in vitro phagocytosis of polystyrene latex particles was detected. During the first two hours of incubation, the percentage of phagocytizing platelets and the number of latex particles per platelet increased; by the end of the third hour, the first parameter remained stable, while the number of latex particles per cell had decreased.Vincristine (20 μg/ml of cell suspension) inhibited platelet protein synthesis. This effect was both time- and dose-dependent. The drug also caused a decrease in the number of phagocytizing cells, as well as in their phagocytotic activity.

The Effect of Adrenaline Infusions on Blood Coagulation in Normal and Haemophilia B Dogs

1966 ◽  
Vol 15 (03/04) ◽  
pp. 349-364 ◽  
Author(s):  
A.H Özge ◽  
H.C Rowsell ◽  
H.G Downie ◽  
J.F Mustard
Keyword(s):  
Body Weight ◽  
Factor Viii ◽  
Factor Ix ◽  
Clotting Factor ◽  
Blood Ph ◽  
Order Of Magnitude ◽  
Dose Dependent ◽  
Generation Test ◽  
Plasma Activity

SummaryThe addition of trace amounts of adrenaline to whole blood in plasma in vitro increased factor VIII, factor IX and whole plasma activity in the thromboplastin generation test. This was dose dependent.Adrenaline infusions less than 22 (μg/kg body weight in normal dogs accelerated clotting, increased factor IX, factor VIII and whole plasma activity in the thromboplastin generation test and caused a fall in blood pH. In a factor IX deficient dog, there was no increase in factor IX activity. After adrenaline infusions, however, the other changes occurred and were of the same order of magnitude as in the normal. Adrenaline in doses greater than 22 μg/kg body weight did not produce as great an effect on clotting in normal or factor IX deficient dogs. The platelet count in the peripheral blood was increased following the infusion of all doses of adrenaline. These observations suggest that the accelerating effect of adrenaline on clotting is not mediated through increase in activity of a specific clotting factor.

Soluble Thrombomodulin Purified from Human Urine Exhibits a Potent Anticoagulant Effect In Vitro and In Vivo

1995 ◽  
Vol 73 (05) ◽  
pp. 805-811 ◽  
Author(s):  
Yasuo Takahashi ◽  
Yoshitaka Hosaka ◽  
Hiromi Niina ◽  
Katsuaki Nagasawa ◽  
Masaaki Naotsuka ◽  
...  
Keyword(s):  
Human Urine ◽  
Specific Activity ◽  
Anticoagulant Activity ◽  
Rabbit Lung ◽  
Soluble Thrombomodulin ◽  
Molecular Weights ◽  
Dose Dependent Fashion ◽  
Dose Dependent

SummaryWe examined the anticoagulant activity of two major molecules of soluble thrombomodulin purified from human urine. The apparent molecular weights of these urinary thrombomodulins (UTMs) were 72,000 and 79,000, respectively. Both UTMs showed more potent cofactor activity for protein C activation [specific activity >5,000 thrombomodulin units (TMU)/mg] than human placental thrombomodulin (2,180 TMU/mg) and rabbit lung thrombomodulin (1,980 TMU/mg). The UTMs prolonged thrombin-induced fibrinogen clotting time (>1 TMU/ml), APTT (>5 TMU/ml), TT (>5 TMU/ml) and PT (>40 TMU/ml) in a dose-dependent fashion. These effects appeared in the concentration range of soluble thrombomodulins present in human plasma and urine. In the rat DIC model induced by thromboplastin, administration of UTMs by infusion (300-3,000 TMU/kg) restored the hematological abnormalities derived from DIC in a dose-dependent fashion. These results demonstrate that UTMs exhibit potent anticoagulant and antithrombotic activities, and could play a physiologically important role in microcirculation.

Effekte von Substanz P und Neurotensin auf die Kontraktilität des Ileums der Maus in vitro: Inhibition durch STW 5

2007 ◽  
Vol 45 (08) ◽  
Author(s):  
D Hagelauer ◽  
O Kelber ◽  
D Weiser ◽  
S Laufer ◽  
H Heinle
Keyword(s):  
Substanz P ◽  
In Vitro Inhibition

Oxygenation of 18-hydroxycorticosterone as the final reaction for aldosterone biosynthesis

1984 ◽  
Vol 107 (3) ◽  
pp. 395-400 ◽  
Author(s):  
Itaru Kojima ◽  
Etsuro Ogata ◽  
Hiroshi Inano ◽  
Bun-ichi Tamaoki
Keyword(s):  
Carbon Monoxide ◽  
Hydroxysteroid Dehydrogenase ◽  
Dependent Manner ◽  
In Vitro Production ◽  
Mitochondrial Preparation ◽  
Final Reaction ◽  
Vitro Production ◽  
Dose Dependent ◽  
Cytochrome P 450

Abstract. Incubation of 18-hydroxycorticosterone with the sonicated mitochondrial preparation of bovine adrenal glomerulosa tissue leads to the production of aldosterone, as measured by radioimmunoassay. The in vitro production of aldosterone from 18-hydroxycorticosterone requires both molecular oxygen and NADPH, and is inhibited by carbon monoxide. Cytochrome P-450 inhibitors such as metyrapone, SU 8000. SU 10603, SKF 525A, amphenone B and spironolactone decrease the biosynthesis of aldosterone from 18-hydroxycorticosterone. These results support the conclusion that the final reaction in aldosterone synthesis from 18-hydroxycorticosterone is catalyzed by an oxygenase, but not by 18-hydroxysteroid dehydrogenase. By the same preparation, the production of [3H]aldosterone but not [3H]18-hydroxycorticosterone from [1,2-3H ]corticosterone is decreased in a dose-dependent manner by addition of non-radioactive 18-hydroxycorticosterone.

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