Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P17174 (aspartate aminotransferase)
 14,872 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In rats, shortly after ligation of superior mesenteric artery serum enzyme activities are found significantly altered. Those changes concern aspartate aminotransferase (GOT), alanine aminotransferase (GPT), lipase, alpha amylase, and isocitrate dehydrogenase as well as glutamate dehydrogenase. The causes are discussed. The authors emphasize that the assessment of serum enzymes possibly gives some help in diagnosing acute intestinal ischemias in early stages.
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PMID:[Behavior of various serum enzymes following ligation of the superior mesenteric artery in the rat (preliminary report)]. 60 23

Eighty-three patients suffering from upper abdominal pain were studied to evaluate the contribution of commonly used biochemical markers in the diagnosis of acute pancreatitis. On admission to hospital, serum amylase, lipase, total bilirubin, aspartate aminotransferase, alanine aminotransferase, alkaline phosphatase and gamma-glutamyl transferase activities were measured. By stepwise logistic discrimination, only two determinations appeared to be of clinical value: lipase and alkaline phosphatase activities. A classification rule was established including these two measurements and its diagnostic performance evaluated by a jackknifed method amounted .83%. ROC curves were used to assess sensitivity and specificity. Our study clearly shows that serum lipase measurements should be preferred to amylase measurements, and that our two-test classification rule provides an efficient aid in clinical decision-making.
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PMID:Combined diagnostic value of biochemical markers in acute pancreatitis. 169 97

The effect of differences in sympathoadrenomedullary and pituitary-adrenocortical responses of individual animals to 35% hemorrhage on severity of shock induction has been studied in unanesthetized unrestrained rats by measuring plasma concentrations of adrenaline (A), noradrenaline (NA), corticosterone (CS) and adrenocorticotropin (ACTH). The responses of A, CS and ACTH were related to the decrease of blood volume and mean arterial pressure (MAP), whereas plasma NA remained unchanged. Higher susceptibility to blood loss was characterized by more pronounced hemorrhage-induced increase in blood lactate concentration and plasma enzyme activities as well as lethal outcome of hemorrhagic shock. In animals with irreversible hemorrhagic shock, enhanced catecholamine secretion and reduced ACTH release was observed. Furthermore, a revealed direct correlation between A and blood lactate concentration and plasma enzyme activities (aspartate aminotransferase, isocitric dehydrogenase, creatine kinase, lipase and glutathione-S-transferase) may indicate its possible participation in the mechanism of shock induction. In contrast, an inverse relationship of plasma CS to the indicators of shock severity was demonstrated. In conclusion, non-optimal neuroendocrine regulation of cardiovascular adjustments to hemorrhage in shock-prone animals might cause an exaggerated compensatory activation of adrenomedullary catecholamine secretion, which in turn has been shown to exert deleterious vascular and metabolic effects. The mechanisms responsible for reduced ACTH secretion in shock-prone animals remain to be established.
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PMID:Hormonal responses to hemorrhage and their relationship to individual hemorrhagic shock susceptibility. 216 2

The toxicity of L-canavanine was investigated because of its demonstrated potential as an antitumor drug. This natural product was only slightly toxic to Sprague-Dawley rats following a single sc injection: the LD50 was 5.9 +/- 1 8 g/kg in adult rats and 5.0 +/- 1.0 g/kg in 10-day-old rats. Following a single dose of 2.0 g/kg, the systemic clearance value for canavanine in adult rats was 0.114 liter/hr, the volume of distribution at steady state was 0.154 liter, and the half-life was 1.56 hr. Forty-eight percent of the dose was excreted unaltered in the urine following an iv injection, and 16% of a sc dose was recovered in the urine. Bioavailability of a 2.0 g/kg sc dose was 72%. Single oral doses of canavanine were less toxic to adult rats than sc injections. Bioavailability of a 2.0 g/kg po dose was 43%, and only 1% of the administered canavanine was recovered in the urine. Twenty-one percent of the administered canavanine remained in the gastrointestinal tract 24 hr after an oral dose. Less than 1% of a 2.0 g/kg dose of L-[guanidinooxy-14C]canavanine was incorporated into the proteins of adult and neonatal rats 4 or 24 hr following administration. Repeated sc administration of canavanine resulted in more severe toxicity. Weight loss and alopecia were observed in rats given daily sc canavanine injections for 7 days. Food intake was decreased by 80% in adult rats subjected to this dosing regimen, but returned to normal after canavanine injections were terminated. Histological studies of tissues from adult rats treated with 3.0 g/kg canavanine daily for 6 days revealed pancreatic acinar cell atrophy and fibrosis. Serum amylase and lipase levels were elevated following one sc injection of 2.0 g/kg canavanine; after three daily injections both serum enzymes were depleted. Elevations in serum glucose and urea nitrogen, and depletion of cholesterol, were observed. The most significant changes were severe attenuations of serum aspartate aminotransferase, alanine aminotransferase, and alkaline phosphatase activity.
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PMID:Toxicity and pharmacokinetics of the nonprotein amino acid L-canavanine in the rat. 244 82

Dietary hexachlorocyclohexane (HCH) and gamma-isomer of HCH produced significant increase in liver weights of mice. Elevated levels of alanine and aspartate aminotransferases and of alkaline phosphatase in the blood of these animals suggested hepatotoxicity. Hepatic soluble enzymes--aspartate aminotransferase and lactate dehydrogenase--were markedly lowered. Among the hepatic lysosomal enzymes, acid phosphatase and acid cathepsin were increased in the experimental animals. Hepatic glucose-6-phosphatase was lowered by HCH while aldolase activity was increased. Hydrolytic enzymes in small intestine, viz., disaccharidases, lipase, amylase, dipeptidase and phosphatases, were also affected by dietary HCH and gamma-HCH. The results suggested cellular toxicity in hepatocytes of HCH and gamma-HCH fed animals, and also interference in gastrointestinal absorption.
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PMID:Biochemical toxicity of hexachlorocyclohexane and its gamma-isomer in albino mice. 248 47

The proposed system of continuous monitoring of enzyme activities is based primarily on the electrochemical behaviour of thiol compounds, and the experimental equipment is extremely simple. The determination of cholinesterase (EC 3.1.1.8) activity is described. The normal values obtained for men (73.9, s +/- 10.3 microkat/l) and for women (71.1, s +/- 10.2 microkat/l), lie within the usual range of analogous photometric methods. Systems for determination of the activities of alkaline phosphatase (EC 3.1.3.1) and adenosylhomocysteinase (EC 3.3.1.1) are described. The activity of aspartate aminotransferase (EC 2.6.1.1) is determined by a combination of enzyme reactions, in which CoA is released from acetyl-CoA. Analogous procedures are discussed for determinations of alanine aminotransferase (EC 2.6.1.2), lactate dehydrogenase (EC 1.1.1.27), lipase (EC 3.1.1.2), and phospholipase A2 (EC 3.1.1.4) activities, and for determination of substrates, e.g., acetate and carnitine. Possible determinations of an additional 199 enzyme activities and of some of substrates are suggested. By determining electrochemically active groups other than thiols this method becomes almost universally applicable.
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PMID:New system of continuous monitoring of enzyme activities and determination of some substrates. 344 Aug 58

Four experiments were carried out with 10 to 12 day old leghorn chicks weighing approximately 93 to 101 g. The chicks were injected intraperitoneally with sterigmatocystin (STG) dissolved in olive oil. The LD50 values as established in the first two experiments were 10.0 and 14.0 mg/kg body weight with most of the deaths occurring between 9 and 21 h following injection. Histopathological studies demonstrated that there was hemorrhage, foci of degeneration and necrosis with fibroblastic proliferation in sinusoids of the liver while the kidneys showed tubular degeneration and necrosis. Biochemical analysis of blood sera demonstrated that STG caused a marked elevation in the activities of lactate dehydrogenase, aspartate aminotransferase, and alanine aminotransferase, and a depression of creatine kinase, but no effects on gamma-glutamyl transferase, amylase and lipase. Free and conjugated bilirubin were elevated in the sera while total protein, albumin, glucose, potassium, chloride and phosphorous concentrations were depressed. In addition, total white blood cells and circulating agranulocytes were depressed while circulating granulocytes were elevated. STG did not significantly affect the concentration of uric acid, cholesterol, triglycerides, calcium, magnesium and sodium in blood.
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PMID:Acute toxicity of sterigmatocystin to chicks. 356 71

The alterations of aspartate aminotransferase (GOT), lipase, alpha-amylase, glucose, urea and bilirubin plasma levels, as well as body weight and electrocardiogram tracings were monitored in individual mice, as organ dysfunction tests, throughout a graft-versus-host reaction (GVHR) induced by minor non-H-2 histocompatibility antigens. Starting in the first two weeks, elevations of GOT and decreases of alpha-amylase and lipase were found indicating deterioration of liver and exocrine pancreatic function.
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PMID:Minor graft-versus-host reaction: very early effects on hepatic and exocrine pancreatic functions in mice. 408 56

In a model developed to study acute pancreatitis in the dog, the disease process was comparable with the spontaneously occurring disease. Infusion of oleic acid into the accessory pancreatic duct induced, grossly and microscopically, acute hemorrhagic pancreatitis with pancreatic atrophy, fibrosis, fat necrosis, and edema. Clinical changes included persistent fever and tachycardia in all dogs and abdominal pain, vomiting, and diarrhea in most. Serum amylase and lipase activities increased markedly as did activities of alkaline phosphatase, aspartate aminotransferase, and alanine aminotransferase. Hematologic alterations included hemoconcentration (despite intensive fluid therapy) and leukocytosis due primarily to neutrophilia and monocytosis. Neither corticosteroid nor anticholinergic therapy begun 24 to 32 hours after oleic acid infusion altered the course of the disease. Dogs survived 8 days and appeared clinically normal when the study was terminated.
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PMID:Effects of an anticholinergic and a corticosteroid on acute pancreatitis in experimental dogs. 617 2

The genetics of lysosomal acid lipase (LIP) has been investigated in human-Chinese hamster and mouse-Chinese hamster somatic cell hybrids. Cellulose acetate electrophoresis of human fibroblast extracts demonstrated that LIP activity consists of three isozymes. A deficiency of LIP activity has been observed in Wolman's disease (WD), cholesterol ester storage disease (CESD), and I-cell disease (ICD); this deficiency was associated with only one LIP isozyme, LIPA. We have demonstrated concordant segregation between human LIPA and human chromosome 10 and its enzyme marker glutamate oxaloacetate transaminase-1 (GOT1) in cell hybrid clones. Previous evidence suggested the different mutations associated with WD and CESD to be in the structural gene which we assign to human chromosome 10, while a different gene, involved in the processing of LIPA, is altered in ICD. These results indicate that several types of gene products are involved in the final expression of LIPA. In mouse-Chinese hamster hybrid clones, mouse Lip-1 (homologous to human LIPA) was assigned to chromosome 19. Previously, mouse Got-1 has been assigned to chromosome 19. Thus, the LIPA-GOT1 linkage groups has remained intact during the 80 X 10(6) years of evolution that separates humans and mice.
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PMID:Assignment of LIPA, associated with human acid lipase deficiency, to human chromosome 10 and comparative assignment to mouse chromosome 19. 729 52


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