Growth Inhibitory Mechanism of Quercetin on the Anabena flos-aquae

2018 ◽  
Vol 08 (03) ◽  
pp. 238-248
Author(s):  
圣琳 徐
Keyword(s):  
Inhibitory Mechanism ◽  
Growth Inhibitory

Inonotus obliquus aqueous extract suppresses carbon tetrachloride induced hepatic injury through modulation of antioxidant enzyme system and anti-inflammatory mechanism

2021 ◽  
Vol 08 ◽  
Author(s):  
Pir Mohammad Ishfaq ◽  
Anjali Mishra ◽  
Shivani Mishra ◽  
Zaved Ahmad ◽  
Shovanlal Gayen ◽  
...  
Keyword(s):  
Docking Studies ◽  
Liver Inflammation ◽  
Inhibitory Mechanism ◽  
Inonotus Obliquus ◽  
Ergosterol Peroxide ◽  
Anticancer Effects ◽  
Growth Inhibitory ◽  
Inflammatory Mechanism ◽  
Cox 2 ◽  
Anti Inflammatory

Background: Chaga mushroom [Inonotus obliquus] is an edible macrofungus used in traditional and folk medicine for treatment of various gastrointestinal disorders. It has shown potent anti-inflammatory, antioxidant and anticancer effects in several experimental studies including our anti-inflammatory and anticancer effects in colorectal cancer and intestinal inflammation. Whole extract or purified compound ergosterol peroxide from chaga mushroom showed anti-inflammatory mechanism via suppression of NF-κB/iNOS-COX-2 and growth inhibitory mechanism via regulation of apoptosis activation and β-catenin suppression. The emergence of diverse inflammatory and carcinogenic agents like carbon tetrachloride [CCl4] is a potent hepatotoxic chemical that caused liver damage by inducing lipid peroxidation and other oxidative damages. Aims: The study was aimed to analyze the biochemical, cellular and molecular mechanism of CCl4 induced chronic liver inflammation and carcinoma and to analyze the effect of the extract of chaga mushroom on liver inflammation and cancer by virtue of anti-inflammatory mechanisms. Method: Physiological, histological and immunohistochemical the physiological functions and cellular functions. Biochemical assays for assessing enzymatic changes in tissues. Molecular simulation and docking studies were performed for proposing the molecular interaction. Results: CCl4-exposed mice exhibited a significant decrease in the body weight followed by altered histopathological signatures in the liver. Supplementation of IOAE showed that treatment restored towards normal structure of the tissues with large round nuclei in most of the cells. CCl4 caused a steep elevation in the levels of SGOT and SGPT to 2.32- and 1.8-fold as compared to control. The LDH level was increased to 447 IU/L in CCl4 treated mice as compared to control [236 IU/L]. Analysis of the oxidant enzyme pathway showed that CCl4 reduced the GSH level to 16.5 μM as compared to control [52 μM], and induced the catalase enzyme activity to 259 U/mL as compared to control [124 U/L]. These physiological and biochemical alterations were restored towards normal levels by IOAE administration. Immunohistochemical staining for caspase-3 and p53 showed that CCl4 notably increased their expressions which were subsequently suppressed by administration of IOAE. The molecular simulation and docking studies using ergosterol peroxide from chaga mushroom with iNOS, COX-2 and TNF-α showed binding energy of -10.5, -8.9 and -9.1 Kcal/mol, respectively. These proteins interacting with ergosterol peroxide suggests an inhibitory effect on these critical proinflammatory signaling proteins. Conclusions: The results point out that IOAE is able to prevent damage of hepatic cells caused by CCl4 in mouse models through anti-inflammatory and growth inhibitory mechanism which can be utilized in natural prevention of the liver toxicity.

scholarly journals Growth Inhibitory Mechanism of Contact-independent Antifungal TM-I-3 Bacillus sporothermodurans Strain against Aspergillus fumigatus and Cladosporium cladosporioides

2021 ◽  
Vol 26 (1) ◽  
pp. 49-53
Author(s):  
CHIHIRO OSAKI ◽  
SARASA MIYAKE ◽  
SHINJI URAKAWA ◽  
SHINJI MITSUIKI ◽  
HITOMI SHIMOMOTO ◽  
...  
Keyword(s):  
Aspergillus Fumigatus ◽  
Cladosporium Cladosporioides ◽  
Inhibitory Mechanism ◽  
Growth Inhibitory

scholarly journals Anti-tumor Activity of Arginine Deiminase fromMycoplasma argininiand Its Growth-inhibitory Mechanism

1995 ◽  
Vol 86 (9) ◽  
pp. 840-846 ◽  
Author(s):  
Haruo Takaku ◽  
Mitsuhiro Matsumoto ◽  
Satoru Misawa ◽  
Kaoru Miyazaki
Keyword(s):  
Arginine Deiminase ◽  
Inhibitory Mechanism ◽  
Growth Inhibitory ◽  
Anti Tumor Activity

Screening for naturally occurring oxyprenylated secondary metabolites as cancer cell growth inhibitory agents

Planta Medica ◽  
2012 ◽  
Vol 78 (11) ◽  
Author(s):  
F Epifano ◽  
S Genovese ◽  
P Lullo ◽  
S Fiorito ◽  
G Trivisonno ◽  
...  
Keyword(s):  
Cell Growth ◽  
Secondary Metabolites ◽  
Cancer Cell ◽  
Cancer Cell Growth ◽  
Naturally Occurring ◽  
Growth Inhibitory ◽  
Inhibitory Agents

Plasminogen-Plasmin System IX. Specific Binding of Tranexamic Acid to Plasmin

1975 ◽  
Vol 33 (03) ◽  
pp. 573-585 ◽  
Author(s):  
Masahiro Iwamoto
Keyword(s):  
Tranexamic Acid ◽  
Affinity Chromatography ◽  
Dissociation Constant ◽  
Factor Xiii ◽  
Specific Binding ◽  
The Other ◽  
Inhibitory Mechanism ◽  
Binding Studies ◽  
Similar Affinity ◽  
Fibrin Structure

SummaryInteractions between tranexamic acid and protein were studied in respect of the antifibrinolytic actions of tranexamic acid. Tranexamic acid did neither show any interaction with fibrinogen or fibrin, nor was incorporated into cross-linked fibrin structure by the action of factor XIII. On the other hand, tranexamic acid bound to human plasmin with a dissociation constant of 3.5 × 10−5 M, which was very close to the inhibition constant (3.6 × 10−5 M) for this compound in inhibiting plasmin-induced fibrinolysis. The binding site of tranexamic acid on plasmin was not the catalytic site of plasmin, because TLCK-blocked plasmin also showed a similar affinity to tranexamic acid (the dissociation constant, 2.9–4.8 × 10−5 M).In the binding studies with the highly purified plasminogen and TLCK-plasmin preparations which were obtained by affinity chromatography on lysine-substituted Sepharose, the molar binding ratio was shown to be 1.5–1.6 moles tranexamic acid per one mole protein.On the basis of these and other findings, a model for the inhibitory mechanism of tranexamic acid is presented.

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