scholarly journals Serum γ -Glutamyltransferase, Alanine Aminotransferase and Aspartate Aminotransferase Activity in Healthy Blood Donor of Different Ethnic Groups in Gorgan

Author(s):  
Abdoljalal Marjani
2020 ◽  
pp. 29-30
Author(s):  
B.R. Dzis ◽  
S.V. Prymak ◽  
R.P. Dzis ◽  
V.L. Novak ◽  
M.P. Dzisiv ◽  
...  

Objective. To study the effect of intravenous infusions of Rheosorbilact on the activity of alanine aminotransferase and aspartate aminotransferase in the plasma of operated patients with gastric cardiac cancer after proximal gastrectomy. Materials and methods. Alanine aminotransferase and aspartate aminotransferase activity levels were studied in plasma of 40 operated patients with gastric cardiac cancer after proximal gastrectomy immediately after surgery, on the 1st, 2nd, 3rd, 5th day after intravenous infusions of the drug. The infusion of Rheosorbilact was administered intravenously, drip, for 5 days at a rate of 40 drops per minute. The daily dose of the drug was 1000.0 ml. Results. In patients with gastric cardiac cancer after proximal gastrectomy in the first days after surgery revealed changes in aminotransferases, which are accompanied by an increase in the activity of alanine aminotransferase and aspartate aminotransferase in blood plasma. To correct the activity of plasma aminotransferases in such patients, Rheosorbilact was administered intravenously immediately after surgery. After repeated intravenous infusions of Rheosorbilact for 5 days, a significant decrease in the activity of alanine aminotransferase and aspartate aminotransferase in blood plasma in the operated patients was revealed. Conclusions. In the first days after proximal gastrectomy in patients with gastric cardiac cancer, an increase in the activity of aminotransferases in blood plasma was revealed. Repeated intravenous infusions of Rheosorbilact normalize the activity of alanine aminotransferase and aspartate aminotransferase in the blood plasma of such patients in the early postoperative period. Infusion drug Rheosorbilact is recommended for widespread medical use in patients with cardiac gastric cancer after proximal gastrectomy, especially in the early postoperative period.


2013 ◽  
Vol 5 ◽  
pp. CMT.S11120
Author(s):  
Edwin K. Kuffner ◽  
Kimberly M. Cooper ◽  
Jeffrey S. Baggish ◽  
Joseph M. Lynch ◽  
Brenda A. Zimmerman ◽  
...  

Published analyses have noted elevated alanine aminotransferase (ALT) activity in patients taking up to 4000 mg/day of acetaminophen. Data from 3 osteoarthritis trials of acetaminophen 3900–4000 mg/day in which ALT and aspartate aminotransferase (AST) were recorded within approximately 2 weeks of therapy initiation were retrospectively analyzed. Patients with baseline ALT or AST above the upper limit of the reference range (ULRR) were excluded. Among 466 patients, 376 (80.7%) had no ALT elevations within approximately 2 weeks of treatment initiation. Elevations >1.5 and >3.0 times ULRR occurred in 4.5% and 0.9% of patients, respectively. Elevations were transient as most resolved (72.9%) or declined (22.4%) with continued treatment beyond 2 weeks. Within approximately 2 weeks of therapy initiation, no patient had ALT > 5 times ULRR or ALT > 3 times ULRR combined with bilirubin >2 times ULRR. ALT elevations were transient and asymptomatic; almost all resolved or declined while on continued therapy and appear not to be clinically important. Clinical trials.gov ID numbers: NCT00240799, NCT00240786


1984 ◽  
Vol 220 (3) ◽  
pp. 707-716 ◽  
Author(s):  
N W Cornell ◽  
P F Zuurendonk ◽  
M J Kerich ◽  
C B Straight

Experiments were conducted with intact rat hepatocytes to identify inhibitors and incubation conditions that cause selective inhibition of alanine aminotransferase or aspartate aminotransferase. Satisfactory results were obtained by preincubating cells with L-cycloserine or L-2-amino-4-methoxy-trans-but-3-enoic acid in the absence of added substrates. When cells were incubated for 20 min with 50 microM-L-cycloserine, alanine aminotransferase activity was decreased by 90%, whereas aspartate aminotransferase was inhibited by 10% or less. On subsequent incubation, synthesis of glucose and urea from alanine was strongly inhibited, but glucose synthesis from lactate was unaffected. L-2-Amino-4-methoxy-trans-but-3-enoic acid (400 microM) in hepatocyte incubations caused 90-95% inactivation of aspartate aminotransferase, but only 15-30% loss of alanine aminotransferase activity. After preincubation with the inhibitor, glucose synthesis from lactate was almost completely blocked; with alanine as the substrate, gluconeogenesis was unaffected, and urea synthesis was only slightly decreased. By comparison with preincubation with inhibitors, simultaneous addition of substrates (alanine; lactate plus lysine) and inhibitors (cycloserine; aminomethoxybutenoic acid) resulted in smaller decreases in aminotransferase activities and in metabolic rates. Other compounds were less satisfactory as selective inhibitors. Ethylhydrazinoacetate inactivated the two aminotransferases to similar extents. Vinylglycine was almost equally effective in blocking the two enzymes in vitro, but was a very weak inhibitor when used with intact cells. Concentrations of DL-propargylglycine (4 mM) required to cause at least 90% inhibition of alanine aminotransferase in hepatocytes also caused a 16% decrease in aspartate aminotransferase. When tested in vitro, alanine aminotransferase was, as previously reported by others, more sensitive to inhibition by amino-oxyacetate than was aspartate aminotransferase, but in liver cell incubations the latter enzyme was more rapidly inactivated by amino-oxyacetate.


2014 ◽  
Vol 50 (3) ◽  
pp. 437-447
Author(s):  
Genowefa Kubik-Dobosz

It was found that K<sup>+</sup> or Ca<sup>2+</sup> deficiency in a nitrate or ammonium medium increased the amount of accumulated total and non-protein nitrogen in some organs of cucumber seedlings, as also caused changes in accumulated potassium and calcium. Lack of K<sup>+</sup> or Ca<sup>2+</sup> in a medium which did not contain nitrogen led to an increased level of glutamate dehydrogenase, alanine aminotransferase and aspartate aminotransferase activity in the cotyledons and roots of cucumbers. Similar changes in the activity of these enzymes were noted in certain organs of seedlings growing in nitrate or ammonium medium with decreased K<sup>+</sup> or Ca<sup>2+</sup> contents, although the magnitude of these changes depended upon the applied dosage of these cations, the form of mineral nitrogen, developmental phase of plants and the plant organ dealt with.


2019 ◽  
Vol 18 (4) ◽  
pp. 297-302
Author(s):  
Sriset Yollada ◽  
Chatuphonprasert Waranya ◽  
Jarukamjorn Kanokwan

Bergenin is a C-glucoside derivative of gallic acid but its antioxidant and hepatoprotective effects have not previously been compared with gallic acid. Male ICR mice were administered bergenin (10, 50, and 250 mg/kg/day) or gallic acid (100 mg/kg/day) for 7 consecutive days before a single administration of ethanol (5 g/kg). Liver sections were histopathologically examined. Aspartate aminotransferase, alanine aminotransferase, reactive oxygen species, and malondialdehyde levels were determined in plasma. Total glutathione, reduced glutathione, and oxidized glutathione levels were determined in liver homogenates. Ethanol induced hepatic injury with prominent histopathological markers including nuclear pyknosis and necrotic areas and this accorded with increases in the plasma levels of aspartate aminotransferase, alanine aminotransferase, reactive oxygen species, and malondialdehyde. Moreover, ethanol disturbed hepatic glutathione homeostasis by reducing glutathione stores. Hepatic injury in the ethanol-induced mice was prevented with bergenin and gallic acid by significant decreases in plasma aspartate aminotransferase, alanine aminotransferase, reactive oxygen species, and malondialdehyde levels and restoration of the hepatic glutathione profile through an increase in the reduced glutathione/oxidized glutathione ratio. Bergenin at 10 mg/kg/day showed comparable hepatoprotective activity to gallic acid in an ethanol-induced mouse model of oxidative stress. Therefore, bergenin might be a promising candidate for further development as a novel hepatoprotective product.


Author(s):  
Haixia Yun ◽  
Xinyu Wu ◽  
Yiwei Ding ◽  
Wendou Xiong ◽  
Xianglan Duan ◽  
...  

Background and Objective : A Tibetan traditional herb named Swertia mussotii Franch., also called “Zangyinchen” by the local people of Qinghai-Tibet area, has been used to protect the liver from injury for many years. However, the curative effect and molecular mechanism of the herb have not been demonstrated clearly. Materials and Methods: In our study, serum alanine aminotransferase, aspartate aminotransferase, total bilirubin levels were examined after S. mussotii Franch. treatment in the acute liver injury of the carbon tetrachloride-induced rat model. Then, Proteome Analysis was applied to explore the potential mechanism of SMT for hepatoprotective effects after iTRAQLC-MS/MS analysis (isobaric tag for relative and absolute quantification-liquid chromatograph-mass spectrometer with tandem mass spectrometry). Results: Serum results showed, alanine aminotransferase, aspartate aminotransferase, total bilirubin levels of rats with acute liver injury were all improved with SMT treatment. Moreover, Proteome Analysis suggested that, with S. Mussotii Franch. treatment, the levels of lipid catabolic process and lipid homeostasis were all enhanced. And the results of protein-protein interaction (PPI) analysis illustrated that these proteins assembled in PPI networks were found almost significantly enriched in response to lipid, negative regulation of lipase activity, response to lipopolysaccharide etc. Furthermore, the downregulated MRP14 and MRP8 proteins were found involved in the lipid metabolism, which may indicate the mechanism of SMT protection liver from ALI induced by carbon tetrachloride. Conclusion: SMT herb could play a role in hepatoprotection and alleviate the effect of acute liver injury by impacting the lipid metabolism associated biological process.


Sign in / Sign up

Export Citation Format

Share Document