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Query: UMLS:C0155339 (Brown)
 12,436 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A new technique for single-step subcellular fractionation of adipose tissue homogenates by analytical sucrose density gradient centrifugation in a vertical pocket reorientating rotor is described. The density gradient distributions of mitochondrial and peroxisomal marker enzymes in brown and white adipose tissue of control and cold exposed rats are compared. The equilibrium density of brown fat mitochondria was found to be significantly increased compared with white fat mitochondria. GDP binding activity was localized solely to the mitochondria in both control and cold-adapted brown adipose tissue. Brown and white fat mitochondria fractions were isolated by differential centrifugation and the specific activities of various enzymes in the homogenate and mitochondrial preparations determined. The specific activity of creatine kinase in brown adipose tissue was found to be ten-fold higher than in white fat and subcellular fractionation studies showed the activity to have an exclusively cytosolic distribution in both tissues. GDP binding activity and some of the mitochondrial enzymes showed, in brown adipose, a striking increase in total activity in cold adapted rats compared to control animals. For some enzyme activities there was a small increase when expressed per mg tissue or per mg mitochondrial protein. When expressed per mg DNA i.e. per cell, there was a reduced specific activity of the mitochondrial and peroxisomal enzymes in both brown and white adipose tissue on cold adaptation.
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PMID:Comparative subcellular fractionation of control and cold-adapted rat brown and white adipose tissue with special reference to peroxisomal and mitochondrial distributions. 647 39

Two hundred twenty four dairy cattle (6 mo to second calving) representing four breeds (169 Holstein, 24 Guernsey, 19 Jersey, 12 Brown Swiss) were used to determine effects of age, temperature-season, and breed on blood characteristics. A total of 1183 blood samples were collected by jugular venipuncture in the middle of each temperature-season. Covariate age affected blood profile except for hemoglobin, oxyhemoglobin, glutamic-oxalacetic transaminase, and albumin. Temperature-season increased or decreased all measures except enzyme creatine phosphokinase, total creatine phosphokinase, calcium and phosphorus. Years differed for all measures except hemoglobin and oxyhemoglobin. Except for enzyme creatine phosphokinase, total creatine phosphokinase, and phosphorus, breeds differed in other measures. There were interactions between temperature-season and year, temperature-season and breed, and year and breed. Differences among temperature-seasons were not consistent from year to year. Breed differences were not consistent from temperature-season to temperature-season for calcium or protein-bound iodine. Breed differences were not consistent from year to year for glutamic-oxaloacetic transaminase, total protein, albumin, or calcium.
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PMID:Effects of age, temperature-season, and breed on blood characteristics of dairy cattle. 726 21

Rhesus monkeys were kept in a restraining apparatus and while conscious injected with the venoms of a range of Australian snakes. Although the action of restraining itself caused an elevation of the animals' plasma creatine kinase (C.K.), the rise was up to 5 times greater in envenomed monkeys. The venoms of the Tiger snake, Mulga, Beaked Sea snake, Rough-Scaled, Copperhead and Red-Bellied snakes were all powerfully myolytic, and those of the Taipan and Small-Eyed snake less so. No myolytic activity was found in the venoms of the Common Brown snake and Death Adder, and the results with Dugite, Gwardar and Small-Scaled snake venom were equivocal. Significant coagulation disturbances were produced by all venoms studied except those of the Small-Eyed and Rough-Scaled snakes. When first aid measures were used, the coagulation disturbances which developed after the release of the injected venom were significantly less than when no first aid was used. This finding, which was observed with all snake venoms studied, suggests that the procoagulant factor may be subject to some inactivation whilst immobilized at the injection site.
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PMID:A study of the major Australian snake venoms in the monkey (Macaca fascicularis). II. Myolytic and haematological effects of venoms. 733 77

A case of rhabdomyolysis following an asthmatic attack is reported. A 71-year-old man was admitted because of wheezing and hypoxemia. Brown urine was present on admission. Although these symptoms completely disappeared with the treatment with aminophylline, salbutamol and corticosteroid, transiently elevated serum creatine phosphokinase and myoglobinuria were present. Rhabdomyolysis has rarely been reported in cases of bronchial asthma. This case represents an extremely rare case of rhabdomyolysis following status asthmaticus.
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PMID:Rhabdomyolysis following status asthmaticus. 888 5

1. The aim of this study was to examine the effects of roxarsone (3-nitro-4-hydroxyphenylarsonic acid) inclusion in the diet on the performance, liver function and lipid metabolism in the liver of laying Brown Tsaiya ducks. 2. Sixty 36-week-old laying ducks were selected and allocated at random into 4 dietary treatments with 3 replications for each treatment. Feeding was for 7 weeks with 3 weeks of experimental diets followed by a 4 week withdrawal period. The experimental diets were supplemented with 0, 50, 100 and 300 mg/kg roxarsone, respectively 3. Dietary inclusion of 50 or 100 mg/kg roxarsone did not significantly promote performance. Inclusion of 300 mg/kg significantly depressed (P<0.05) performance, liver weight and content, serum triacylglycerol (TG), serum nonesterified fatty acid (NEFA) and increased (P<0.05) cholesterol, creatine kinase (CK) and aspartate aminotransferase (AST) in the serum at the end of 3 weeks on the experimental diet. 4. Laying characteristics returned to normal 4 weeks after withdrawal of roxarsone. The liver weight, fat and TG in the liver and serum concentrations of TG, NEFA, high density lipoprotein (HDL) and AST increased significantly (P<0.05), while the level of very low density lipoprotein (VLDL) decreased (P<0.05) at the end of the withdrawal period. More prominent vacuolised hepatic fatty cells were observed in laying ducks treated with 300 mg/kg of roxarsone.
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PMID:Effect of roxarsone inclusion in the diet on the performance and hepatic lipid metabolism of laying Tsaiya duck. 1108 32

Age-related protein nitration was studied in skeletal muscle of Fisher 344 and Fisher 344/Brown Norway (BN) F1 rats by a proteomic approach. Proteins from young (4 months) and old (24 months) Fisher 344 rats and young (6 months) and old (34 months) Fisher 344/BN F1 animals were separated by 2-D gel electrophoresis. Western blot showed an age-related increase in the nitration of a few specific proteins, which were identified by MALDI-TOF MS and ESI-MS/MS. We identified age-dependent apparent nitration of beta-enolase, alpha-fructose aldolase, and creatine kinase, which perform important functions in muscle energy metabolism, suggesting that the nitration of such key proteins can be, in part, responsible for the decline of muscle motor function of the muscle. Furthermore, we have identified the apparent nitration of succinate dehydrogenase, rab GDP dissociation inhibitor beta (GdI-2), triosephosphate isomerase, troponin I, alpha-crystallin, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH).
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PMID:Proteomic identification of age-dependent protein nitration in rat skeletal muscle. 1460 22

Proteomic techniques were used to identify cardiac proteins from whole heart homogenate and heart mitochondria of Fisher 344/Brown Norway F1 rats, which suffer protein nitration as a consequence of biological aging. Soluble proteins from young (5 mo old) and old (26 mo old) animals were separated by one- and two-dimensional gel electrophoresis. One- and two-dimensional Western blots with an anti-nitrotyrosine antibody show an age-related increase in the immunoresponse of a few specific proteins, which were identified by nanoelectrospray ionization-tandem mass spectrometry (NSI-MS/MS). Complementary proteins were immunoprecipitated with an immobilized anti-nitrotyrosine antibody followed by NSI-MS/MS analysis. A total of 48 proteins were putatively identified. Among the identified proteins were alpha-enolase, alpha-aldolase, desmin, aconitate hydratase, methylmalonate semialdehyde dehydrogenase, 3-ketoacyl-CoA thiolase, acetyl-CoA acetyltransferase, GAPDH, malate dehydrogenase, creatine kinase, electron-transfer flavoprotein, manganese-superoxide dismutase, F1-ATPase, and the voltage-dependent anion channel. Some contaminating blood proteins including transferrin and fibrinogen beta-chain precursor showed increased levels of nitration as well. MS/MS analysis located nitration at Y105 of the electron-transfer flavoprotein. Among the identified proteins, there are important enzymes responsible for energy production and metabolism as well as proteins involved in the structural integrity of the cells. Our results are consistent with age-dependent increased oxidative stress and with free radical-dependent damage of proteins. Possibly the oxidative modifications of the identified proteins contribute to the age-dependent degeneration and functional decline of heart proteins.
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PMID:Proteomic identification of 3-nitrotyrosine-containing rat cardiac proteins: effects of biological aging. 1534 82

The nitration of protein tyrosine residues represents an important post-translational modification during development, oxidative stress, and biological aging. To rationalize any physiological changes with such modifications, the actual protein targets of nitration must be identified by proteomic methods. While several studies have used proteomics to screen for 3-nitrotyrosine-containing proteins in vivo, most of these studies have failed to prove nitration unambiguously through the actual localization of 3-nitrotyrosine to specific sequences by mass spectrometry. In this paper we have applied sequential solution isoelectric focusing and SDS-PAGE for the proteomic characterization of specific 3-nitrotyrosine-containing sequences of nitrated target proteins in vivo using nanoelectrospray ionization-tandem mass spectrometry. Specifically, we analyzed proteins from the skeletal muscle of 34-month-old Fisher 344/Brown Norway F1 hybrid rats, a well accepted animal model for biological aging. We identified the 3-nitrotyrosine-containing sequences of 11 proteins, including cytosolic creatine kinase, tropomyosin 1, glyceraldehyde-3-phosphate dehydrogenase, myosin light chain, aldolase A, pyruvate kinase, glycogen phosphorylase, actinin, gamma-actin, ryanodine receptor 3, and neurogenic locus notch homolog. For creatine kinase and neurogenic locus notch homolog, two 3-nitrotyrosine-containing sequences were identified, i.e. at positions 14 and 20 for creatine kinase and at positions 1175 and 1205 for the neurogenic locus notch homolog. The selectivity of the in vivo nitration of creatine kinase at Tyr14 and Tyr20 does not correspond to the product selectivity in vitro, where exclusively Tyr82 was nitrated when creatine kinase was exposed to peroxynitrite. The latter experiments demonstrate that the in vitro exposure of an isolated protein to peroxynitrite may not always be a good model to mimic protein nitration in vivo.
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PMID:Proteomic analysis of protein nitration in aging skeletal muscle and identification of nitrotyrosine-containing sequences in vivo by nanoelectrospray ionization tandem mass spectrometry. 1585 74

Different molecules have been studied as biochemical markers in heart transplantation. However, their utility is under discussion as results in human and animal models are controversial. In this work, lactate dehydrogenase (LDH), creatine kinase (CK) and cardiac troponin I (TnI) were studied as serologic markers of acute rejection after heterotopical heart transplantation in rats. In predictable rejection experiments, animals were divided into three groups: nonoperated (Lewis rats), control group (Lewis-Lewis isografts) and rejection group (Brown Norway-Lewis allografts). Nonpredictable rejection experiments were performed using nonconsanguineous Sprague-Dawley allografts. In predictable rejection experiments, LDH activity was similar between control and rejection groups. TnI values were heterogeneous in control and rejection groups. In contrast, the rejection group showed CK activity increased 4.5-fold compared with the control group. In addition to these predictable studies, we also presented novel nonpredictable experiments in which rats were divided into groups based on low and high CK activity. Histologic studies in these rats showed that none of those with low CK activity presented rejection signs, while all animals with high CK levels showed grade 2R rejection. These results suggest that CK might be an excellent marker for prediction of rejection in heart transplantation.
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PMID:Increased serum creatine kinase is a reliable marker for acute transplanted heart rejection diagnosis in rats. 1723 27

One mechanism that may influence the quality of skeletal muscle proteins, and explain the age-related decline in contractility, is protein damage. Advanced glycation end-products (AGE) in vivo are useful biomarkers of damage. In this study, comparison of extensor digitorum longus (EDL) muscles from young (8 months), old (33 months), and very old (36 months) Fischer 344 Brown Norway F1 (F344BNF1) hybrid rats shows that muscles from the very old rats have a significantly higher percentage of myofibers that immunolabel intracellularly for AGE-antibody 6D12 compared to the younger age group. The AGE-modified proteins, determined in the semimembranosus muscles from young (9 months) and old (27 months) F344 rats, identified by matrix-assisted laser desorption ionization-time of flight mass spectrometry include creatine kinase, carbonic anhydrase III, beta-enolase, actin, and voltage-dependent anion-selective channel 1. Moreover, there is a significant increase in AGE modification of beta-enolase with age. These results identify a common subset of proteins that contain AGE and suggest that metabolic proteins are targets for glycation with aging.
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PMID:Advanced glycation end-product accumulation and associated protein modification in type II skeletal muscle with aging. 1800 Jan 39


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