Actions ofp-synephrine on hepatic enzyme activities linked to carbohydrate metabolism and ATP levels in vivo and in the perfused rat liver

2017 ◽  
Vol 36 (1) ◽  
pp. 4-12 ◽  
Author(s):  
Marcos Rodrigues Maldonado ◽  
Lívia Bracht ◽  
Anacharis Babeto de Sá-Nakanishi ◽  
Rúbia Carvalho Gomes Corrêa ◽  
Jurandir Fernando Comar ◽  
...  
Keyword(s):  
Carbohydrate Metabolism ◽  
Rat Liver ◽  
Enzyme Activities ◽  
Perfused Rat Liver ◽  
Hepatic Enzyme ◽  
Atp Levels

scholarly journals Metabolism of inorganic sulphate in the isolated perfused rat liver. Effect of sulphate concentration on the rate of sulphation by phenol sulphotransferase

1978 ◽  
Vol 176 (3) ◽  
pp. 959-965 ◽  
Author(s):  
Gerard J. Mulder ◽  
Katja Keulemans
Keyword(s):  
Steady State ◽  
Plasma Concentration ◽  
Rat Liver ◽  
Isolated Perfused Rat Liver ◽  
Perfused Rat Liver ◽  
Perfusion Medium ◽  
Physiological Concentration ◽  
Sulphate Concentration ◽  
Inorganic Sulphate

1. The metabolism of inorganic [35S]sulphate (Na235SO4) was studied in the isolated perfused rat liver at three initial concentrations of inorganic sulphate in the perfusion medium (0, 0.65 and 1.30mm), in relation to sulphation and glucuronidation of a phenolic drug, harmol (7-hydroxy-1-methyl-9H-pyrido[3,4-b]indole). 2. [35S]Sulphate rapidly equilibrated with endogenous sulphate in the liver. It was excreted in bile and reached, at the lowest concentration in the perfusion medium, concentrations in bile that were much higher than those in the perfusion medium; at the higher sulphate concentrations, these concentrations were equal. The physiological concentration of inorganic sulphate in the liver, available for sulphation of drugs, is similar to the plasma concentration. 3. At zero initial inorganic sulphate in the perfusion medium, the rate of sulphation was very low and harmol was mainly glucuronidated. At 0.65mm-sulphate glucuronidation was much decreased and considerable sulphation took place, indicating efficient competition of conjugation by sulphation. At 1.30mm-sulphate the sulphation increased still further. 4. The results suggest that an important factor in sulphation is the relatively high Km of synthesis of adenosine 3′-phosphate 5′-sulphatophosphate (the co-substrate of sulphation) for inorganic sulphate, which is of the order of the plasma concentration of inorganic sulphate. The steady-state adenosine 3′-phosphate 5′-sulphatophosphate concentration may determine the rate of sulphate conjugation of drugs in the rat in vivo.

Bioassay of endotoxin clearance in vivo and by perfused rat liver

1976 ◽  
Vol 231 (1) ◽  
pp. 258-264 ◽  
Author(s):  
BJ Buchanan ◽  
JP Filkins
Keyword(s):  
Linear Relationship ◽  
Rat Liver ◽  
Salt Solution ◽  
Isolated Perfused Rat Liver ◽  
Perfused Rat Liver ◽  
Half Time ◽  
Rat Blood ◽  
Endotoxin Concentration ◽  
Induction Of Tolerance

Endotoxin clearances in vivo and by the isolated perfused rat liver were evaluated via bioassay in lead-sensitized rats. A linear relationship between the probit of shock lethality and the endotoxin dose in the probit range of 4-6 was validated. Endotoxin clearance in normal, fed rats displayed a linear relationship between the logarithm of the blood endotoxin concentration and time throughout the period of 15-240 min at doses of 500 and 1,000 mug/ rat; the half-time values were 58-63 min. Decreasing the endotoxin dose to 250 mug resulted in multiphasic clearance curves. Induction of tolerance to endotoxin resulted in marked acceleration of endotoxin clearance. Endotoxin clearance from the isolated perfused rat liver was not influenced by serum or rat blood as compared to clearance from a balanced salt solution. These data suggest that a physiologically stressful dose of endotoxin is slowly cleared from the blood and, therefore, circulates for prolonged periods.

Effects of in Vivo Captan Administration on Cytotoxicity, Gluconeogenesis, ATP Levels, and Parameters Related to Oxidative Stress in Rat Liver

1999 ◽  
Vol 64 (3) ◽  
pp. 185-193 ◽  
Author(s):  
M.J. Moreno-Aliaga ◽  
J.C. Arenas-Vidal ◽  
A. Berjóaan ◽  
M.P. Fernández-Otero
Keyword(s):  
Oxidative Stress ◽  
Rat Liver ◽  
Atp Levels

Comparison of somatostatin-28 and somatostatin-14 clearance by the perfused rat liver

1985 ◽  
Vol 63 (1) ◽  
pp. 62-67 ◽  
Author(s):  
M. Seno ◽  
Y. Seino ◽  
Y. Takemura ◽  
S. Nishi ◽  
H. Ishida ◽  
...  
Keyword(s):  
Rat Liver ◽  
Gel Filtration ◽  
Perfused Rat Liver ◽  
Half Time ◽  
Hepatic Extraction Ratio ◽  
Plasma Extract ◽  
Second Peak ◽  
Somatostatin 14

The hepatic clearances of somatostatin (SS)-28 and SS-14 by the perfused rat liver were compared, using a recirculating, plasma-free, erythrocyte-containing perfusion system. The disappearance rate constant, half time, clearance, and hepatic extraction ratio when 1.2 nM SS-28 was added to the perfusate were 0.0221 ± 0.0051 min−1, 36.6 ± 7.6 min, 0.34 ± 0.08 mL/min, and 17.2 ± 3.9%, respectively. The corresponding values obtained when SS-14 was added to the perfusate were 0.0405 ± 0.0022 min−1, 17.3 ± 1.0 min, 0.71 ± 0.05 mL/min, and 35.4 ± 2.6%, respectively. The differences between the SS-28 and SS-14 indices were all statistically significant. In addition, the perfusates with SS-28 added were eluted on Sephadex G-25 fine columns and somatostatinlike immunoreactivity (SLI) was determined. No SS-14 was found in perfusate containing SS-28 at both 5 and 30 min after the beginning of the perfusion. To investigate whether or not the liver plays an important role in the clearance of SS-28 or the conversion of SS-28 to SS-14 in vivo, the plasma disappearance of 2 μg SS-28 was compared in the whole rat and the functionally hepatectomized model. The half time of plasma SS-28 was 1.43 ± 0.12 min in the whole rat, significantly shorter than the 2.20 ± 0.14 min in the hepatectomized model. Gel filtration of plasma extract samples at 0.5 min after the SS-28 injection showed two major peaks of SLI: a first peak corresponding to SS-28 and a second peak coeluted in the position of SS-14 in both the whole rat and the hepatectomized model. At 4 min after the SS-28 injection, the first peak disappeared and only a small second peak was observed. These results suggest that SS-28 is cleared by the rat liver in vivo and in vitro and that it is cleared more slowly than SS-14. Furthermore, we find that little, if any, conversion of SS-28 to SS-14 occurs in the liver.

Metabolic characteristics of the isolated perfused rat liver

1960 ◽  
Vol 199 (3) ◽  
pp. 395-399 ◽  
Author(s):  
Alvin S. Ostashever ◽  
Irving Gray ◽  
Samuel Graff
Keyword(s):  
Rat Liver ◽  
Amino Nitrogen ◽  
Experimental Period ◽  
Isolated Perfused Rat Liver ◽  
Perfused Rat Liver ◽  
Metabolic Characteristics ◽  
Respiration Rates ◽  
Substrate Respiration ◽  
Body Production

The use of the isolated perfused rat liver for quantitative biochemical studies of liver metabolism over an experimental period of as long as 4 hours is demonstrated. Respiration rates responded immediately to the addition of substrates and the liver could be restimulated by a second dose of substrate, respiration rates reflecting the nature of the substrate. Net amino nitrogen uptake was consistently exceeded by urea nitrogen production, the latter comparing favorably with in vivo rates. Fructose was rapidly removed from the perfusate by the liver, and the liver efficiently removed lactic acid formed by erythrocyte glycolysis. Ketone body production was continuous and within normal in vivo rates. Bile production declined gradually over a 4-hour period.

Ca2+ waves are organized among hepatocytes in the intact organ

1995 ◽  
Vol 269 (1) ◽  
pp. G167-G171 ◽  
Author(s):  
M. H. Nathanson ◽  
A. D. Burgstahler ◽  
A. Mennone ◽  
M. B. Fallon ◽  
C. B. Gonzalez ◽  
...  
Keyword(s):  
Blood Flow ◽  
Rat Liver ◽  
Peristaltic Flow ◽  
Perfused Rat Liver ◽  
V1a Receptor ◽  
Confocal Fluorescence ◽  
Organ Level ◽  
Vasopressin V1a Receptor ◽  
Peristaltic Contractions

Hormone-induced increases in cytosolic Ca2+ (Cai2+) begin as Cai2+ waves in cells isolated from most types of tissue (1, 11), but whether such waves actually occur in vivo is unknown. To investigate this, we examined vasopressin-induced Cai2+ signals in hepatocytes within the perfused rat liver. Using confocal fluorescence video microscopy, we found that increases in Cai2+ began as waves that usually originated in hepatocytes near central venules, then spread opposite to the direction of blood flow, to hepatocytes near portal venules. We used immunochemistry to determine that the liver vasopressin V1a receptor is most concentrated among hepatocytes in the pericentral region, providing the mechanism by which Cai2+ waves originate there. Pericentral-to-periportal Cai2+ waves may direct peristaltic flow of bile, since Cai2+ induces contraction of the apical pole of hepatocytes and since peristaltic contractions in liver also occur in a pericentral-to-periportal direction. The organization of Cai2+ waves among cells in intact tissue may be a means by which an integrative, organ-level response is provided in response to hormonal stimuli.

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