Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0151744 (myocardial ischemia)
 31,282 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The authors studied teh effect of cultured Polyscias filcifolia Bailey cells on protein biosynthesis in an acellular system obtained from the liver of rabbits in experimental myocardial ischemia. It was found that the preparation normalizes the values of protein biosynthesis, the duration of the average polypeptide chain synthesis, and the activity of aminoacyl-tRNA synthetases.
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PMID:[Effect of cultured Polyscias cells on the activity of components of the protein-synthesizing system of rabbit liver]. 162 35

Composition of high-molecular-weight aminoacyl-tRNA synthetases complexes from rabbit liver both in norm and after 12 h experimental myocardial ischemia (EMI) has been investigated. Partial redistribution of aminoacyl-tRNA synthetases activity from 1820 kD complex into 840 kD complex was observed in case of EMI which resulted in changes of protein biosynthesis rate in cell-free system.
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PMID:[Role of aminoacyl-tRNA-synthetases in changes in the rate of protein biosynthesis in the rabbit liver during myocardial ischemia]. 239 92

Subcellular distribution of aminoacyl-tRNA synthetase activities has been studied in normal rabbit liver and under experimental myocardial ischemia (EMI). An increase in the activity of a number of aminoacyl-tRNA synthetases in postmitochondrial and postribosomal supernatants from rabbit liver has been determined 12 hr after EMI. Gel chromatography of the postribosomal supernatant on Sepharose 6B shows that aminoacyl-tRNA synthetase activities are distributed among the fractions with M(r) 1.82 x 10(6), 0.84 x 10(6) (high-M(r) aminoacyl-tRNA synthetase complexes) and 0.12-0.35 x 10(6). In the case of EMI aminoacyl-tRNA synthetase activities are partly redistributed from the 1.82 x 10(6) complex into the 0.84 x 10(6) complex. The catalytic properties of both free and complex leucyl-tRNA synthetases have been compared. KM for all the substrates are the values of the same order in norm and under EMI. A decrease in some aminoacyl-tRNA synthetase activities associated with polyribosomes has been observed 12 hr after EMI. The interaction of aminoacyl-tRNA synthetases with polyribosomes stimulates the catalytic activity of some enzymes and protects them from heat inactivation in vitro. It is assumed that the changes in association of aminoacyl-tRNA synthetases with high-M(r) complexes and compartmentalization of these enzymes on polyribosomes may be related to the alteration of protein biosynthesis under myocardial ischemia.
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PMID:Subcellular distribution and properties of rabbit liver aminoacyl-tRNA synthetases under myocardial ischemia. 828 66

Left ventricular function and morphology were assessed using M-mode echocardiography in 3 patients with diabetes mellitus associated with mitochondrial tRNA(Leu)(UUR) gene mutation, who were free of clinical, electrocardiographic, or thallium scan evidence of ischemic heart disease. Echocardiograms revealed hypertrophic cardiomyopathy in all 3 patients. Hypertrophy of the interventricular septum was mild in Cases 1 and 3 (12 and 13 mm, respectively) and severe in Case 2 (22 mm) (normal 7-10 mm). When they had neither signs nor symptoms suggestive of congestive heart failure, percentage fractional shortening (%FS), an index of wall motion of the left ventricle (normal > 28%), was normal in Cases 2 and 3 (28 and 32%, respectively) whereas it was slightly decreased in Case 1 (22%). In Case 1 with mild hypertrophy, the development of congestive heart failure was associated with a marked decrease in %FS to 13%; this patient responded well to diuretics and captopril and %FS rose to 22%. However, a mild decrease in %FS to 21% caused congestive heart failure in Case 2 with severe hypertrophy. His response to treatment was marginal. The present study indicates that mitochondrial DNA analysis should be done in patients with diabetic cardiomyopathy, and that sequential echocardiography is invaluable for the detection of hypertrophic cardiomyopathy and the management of subsequent myocardial dysfunction in patients with mitochondrial diabetes mellitus and cardiomyopathy.
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PMID:Hypertrophic cardiomyopathy in patients with diabetes mellitus associated with mitochondrial tRNA(Leu)(UUR) gene mutation. 856 88

A 34-year-old female IDDM patient complained of chest oppression in hypoglycemic episodes and electrocardiograms revealed reversible ischemic changes occurring concomitantly with hypoglycemia. The ECG changes improved and the chest oppression disappeared following increasing blood glucose level by glucose intake. Master's double load test and treadmill load test were positive for ischemic changes. Radioisotopic myocardial scintigraphy by thallium and BMIPP did not show any filling defects and coronary angiography revealed no remarked stenosis in the coronary arteries. She had no mitochondrial tRNA(Leu) (A-->G) gene mutation at nucleotide position 3243, but both the patient and her mother had a G-to-A transition within the replication origin of the light strand at nucleotide position 5744 of the mitochondrial gene. As the patient's maternal family had no history of ischemic heart disease, it is not clear whether mitochondrial gene mutation at nucleotide position 5744 reflects the occurrence of cardiac ischemia. Some disorders of microcirculation in capillary vessels in cardiac muscles may occur in such patients.
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PMID:An IDDM patient who complained of chest oppression with ischemic changes on ECG in insulin-induced hypoglycemia. 959 72

An increased concentration of homocysteine is an important risk factor of atherosclerosis; however, the mechanism of the proatherogenic effect of this amino acid is not yet known. Studies performed during the last two decades suggest that the atherogenic effect of homocysteine may be accounted for by homocysteine thiolactone (HCTL). Homocysteine is nonspecifically activated by methionyl-tRNA synthetase; however, it is not transferred to tRNA and incorporated into proteins, but is transformed to a cyclic thioester, homocysteine thiolactone. HCTL is highly reactive and acylates free amino groups of protein lysine residues, the process referred to as protein N-homocysteinylation. Various plasma proteins are homocysteinylated in vitro and in vivo. Homocysteinylation results in the incorporation of additional thiol groups which may alter the physicochemical properties and biological activity of proteins. In particular, homocysteinylation of low-density lipoproteins (LDLs) increases their susceptibility to oxidation and accelerates their uptake by macrophages. In addition, homocysteinylated LDL elicit humoral immune response. Anti-homocysteinyllysine antibodies are detected in plasma of healthy humans and their titer is elevated in patients with ischemic heart disease or ischemic cerebral stroke. Homocysteine thiolactone is hydrolyzed to homocysteine by paraoxonase (PON), a calcium-dependent esterase synthesized in the liver and contained in plasma high-density lipoproteins (HDLs). Protein homocysteinylation may contribute to accelerated atherogenesis in individuals with hyperhomocysteinemia.
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PMID:Protein homocysteinylation: a new mechanism of atherogenesis? 1610 41

Resina draconis (bright red resin isolated from Dracaena cochinchinensis, RD) has been clinically used for treatment of myocardial ischemia (MI) for many years. However, the mechanisms of its pharmacological action on MI are still poorly understood. This study aimed to characterize the plasma metabolic profiles of MI and investigate the mechanisms of RD on MI using ultraperformance liquid chromatography/quadrupole time-of-flight mass spectrometry-based metabolomics combined with pattern recognition methods and metabolic pathway analysis. Twenty metabolite markers characterizing metabolic profile of MI were revealed, which were mainly involved in aminoacyl-tRNA biosynthesis, phenylalanine, tyrosine, and tryptophan biosynthesis, vascular smooth muscle contraction, sphingolipid metabolism, and so forth. After RD treatment, however, levels of seven MI metabolite markers, including phytosphingosine, sphinganine, acetylcarnitine, cGMP, cAMP, L-tyrosine, and L-valine, were turned over, indicating that RD is likely to alleviate MI through regulating the disturbed vascular smooth muscle contraction, sphingolipid metabolism, phenylalanine metabolism, and BCAA metabolism. To our best knowledge, this is the first comprehensive study to investigate the mechanisms of RD for treating MI, from a metabolomics point of view. Our findings are very valuable to gain a better understanding of MI metabolic profiles and provide novel insights for exploring the mechanisms of RD on MI.
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PMID:Metabolomics Study of Resina Draconis on Myocardial Ischemia Rats Using Ultraperformance Liquid Chromatography/Quadrupole Time-of-Flight Mass Spectrometry Combined with Pattern Recognition Methods and Metabolic Pathway Analysis. 2376 36

The pathological process and mechanism of myocardial ischemia (MI) is very complicated, and remains unclear. An integrated proteomic-metabolomics analysis was applied to comprehensively understand the pathological changes and mechanism of MI. Male Sprague-Dawley rats were randomly divided into a mock surgery (MS) group and an MI group. The MI model was made by ligating the left anterior descending coronary artery, twenty-four hours after which, echocardiography was employed to assess left ventricular (LV) function variables. Blood samples and left ventricular tissues were collected for ELISA, metabolomics and proteomics analysis. The results showed that LV function, including ejection fraction (EF) and fractional shortening (FS), was significantly reduced and the level of cTnT in the serum increased after MI. iTRAQ proteomics showed that a total of 169 proteins were altered including 52 and 117 proteins with increased and decreased expression, respectively, which were mainly involved in the following activities: complement and coagulation cascades, tight junction, regulation of actin cytoskeleton, MAPK signaling pathway, endocytosis, NOD-like receptor signaling pathway, as well as phagosome coupled with vitamin digestion and absorption. Altered metabolomic profiling of this transition was mostly enriched in pathways including ABC transporters, glycerophospholipid metabolism, protein digestion and absorption and aminoacyl-tRNA biosynthesis. The integrated metabolomics and proteomics analysis indicated that myocardial injury after MI is closely related to several metabolic pathways, especially energy metabolism, amino acid metabolism, vascular smooth muscle contraction, gap junction and neuroactive ligand-receptor interaction. These findings may contribute to understanding the mechanism of MI and have implication for new therapeutic targets.
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PMID:Proteomic and metabolomic characterization of cardiac tissue in acute myocardial ischemia injury rats. 3236 12