Diuretic action of the fruit of Catalpa ovata. G. DON. (I)

1964 ◽  
Vol 60 (6) ◽  
pp. 544-549 ◽  
Author(s):  
Yoshio SUZUKI
Keyword(s):  
Diuretic Action ◽  
Catalpa Ovata

ÜBER DIE ANTAGONISTISCHE WIRKUNG VON TRIJODTHYRONIN UND PROGESTERON AUF DEN PREDNISOLONEFFEKT AM EPIPHYSENKNORPEL (PRÜFUNG DER REISSFESTIGKEIT)

1963 ◽  
Vol 42 (1) ◽  
pp. 29-38 ◽  
Author(s):  
L. Ther ◽  
H. Schramm ◽  
G. Vogel
Keyword(s):  
Tensile Strength ◽  
Dose Response ◽  
Single Injection ◽  
Relative Effectiveness ◽  
Prednisolone Acetate ◽  
Response Curves ◽  
Deoxycorticosterone Acetate ◽  
Weight Range ◽  
Diuretic Action ◽  
Maximal Load

ABSTRACT Longitudinal tension exerted on a killed rat's femur results always in rupture on the same place viz: the distal epiphyseal line. The power required to produce this effect can be measured with a simple dynamometer. The tensile strength increases with advancing age and during exsiccation (thirst). In untreated rats (weight range 100–120 g) this value amounts to about 1.5–1.8 kg. Tensile strength of the femoral epiphyseal line may be influenced by hormones. Corticosteroids such as prednisolone acetate and cortisol acetate increase the level of maximal load to more than 2.0 kg. In general the effect of a single injection reaches a climax after 48 hours. Dose-response-curves can be established and relative effectiveness may be gathered therefrom. Deoxycorticosterone acetate likewise increases tensile strength in spite of the fact that contrary to prednisolone exhibiting diuretic action this compound has a water retaining effect. Triiodothyronine and progesterone when given alone produce a slight decrease in tensile strength. The effect of prednisolone when given simultaneously with one of these two compounds is antagonized: this phenomenon is more pronounced in the case of triiodothyronine.

Antagonism of Diuretic Action of Thyroxine by Ethanol

1956 ◽  
Vol 92 (2) ◽  
pp. 247-248
Author(s):  
L. M. Horger ◽  
M. X. Zarrow
Keyword(s):  
Diuretic Action

scholarly journals Diuretic Action of Isoproterenol in the Dog

1971 ◽  
Vol 35 (6) ◽  
pp. 601-610 ◽  
Author(s):  
SHIRO MORIMOTO ◽  
YOUICHI ABE ◽  
KENJIRO YAMAMOTO
Keyword(s):  
Diuretic Action

scholarly journals On the Diuretic Action of Na, K and Mg=lons

1929 ◽  
Vol 12 (4) ◽  
pp. 366-388
Author(s):  
HIDEICHI TAKETA
Keyword(s):  
Diuretic Action

Interference of different ACE-inhibitors with the diuretic action of furosemide and hydrochlorothiazide

1989 ◽  
Vol 67 (22) ◽  
pp. 1138-1146 ◽  
Author(s):  
C. Toussaint ◽  
A. Masselink ◽  
A. Gentges ◽  
G. Wambach ◽  
G. Bönner
Keyword(s):  
Ace Inhibitors ◽  
Diuretic Action

scholarly journals Identification of Catalposide Metabolites in Human Liver and Intestinal Preparations and Characterization of the Relevant Sulfotransferase, UDP-glucuronosyltransferase, and Carboxylesterase Enzymes

Pharmaceutics ◽  
2019 ◽  
Vol 11 (7) ◽  
pp. 355 ◽  
Author(s):  
Deok-Kyu Hwang ◽  
Ju-Hyun Kim ◽  
Yongho Shin ◽  
Won-Gu Choi ◽  
Sunjoo Kim ◽  
...  
Keyword(s):  
Human Liver ◽  
Individual Variability ◽  
Hydroxybenzoic Acid ◽  
Catalpa Ovata ◽  
Anti Oxidant ◽  
Extrahepatic Tissues ◽  
Udp Glucuronosyltransferase ◽  
Hydrolysis Of

Catalposide, an active component of Veronica species such as Catalpa ovata and Pseudolysimachion lingifolium, exhibits anti-inflammatory, antinociceptic, anti-oxidant, hepatoprotective, and cytostatic activities. We characterized the in vitro metabolic pathways of catalposide to predict its pharmacokinetics. Catalposide was metabolized to catalposide sulfate (M1), 4-hydroxybenzoic acid (M2), 4-hydroxybenzoic acid glucuronide (M3), and catalposide glucuronide (M4) by human hepatocytes, liver S9 fractions, and intestinal microsomes. M1 formation from catalposide was catalyzed by sulfotransferases (SULTs) 1C4, SULT1A1*1, SULT1A1*2, and SULT1E1. Catalposide glucuronidation to M4 was catalyzed by gastrointestine-specific UDP-glucuronosyltransferases (UGTs) 1A8 and UGT1A10; M4 was not detected after incubation of catalposide with human liver preparations. Hydrolysis of catalposide to M2 was catalyzed by carboxylesterases (CESs) 1 and 2, and M2 was further metabolized to M3 by UGT1A6 and UGT1A9 enzymes. Catalposide was also metabolized in extrahepatic tissues; genetic polymorphisms of the carboxylesterase (CES), UDP-glucuronosyltransferase (UGT), and sulfotransferase (SULT) enzymes responsible for catalposide metabolism may cause inter-individual variability in terms of catalposide pharmacokinetics.

scholarly journals STUDY OF DIURETIC ACTION OF CRYOPOWDERS PRODUCED FROM WILD ROSE ROOTS AND AGRIMONIA GRASS

2016 ◽  
pp. 73-77
Author(s):  
Sergey A. Rekkandt ◽  
Valerii V. Melik-Gusseinov ◽  
Svetlana A. Kuleshova ◽  
Fatima K. Sherieva
Keyword(s):  
Diuretic Action
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