Browse
Submit Data
Databases
API
Help

Dataset Information

7 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Increased degradation rates of protein synthesized in hepatoma cells in the presence of amino acid analogues.

ABSTRACT: 1. Reuber H35 hepatoma cells incorporate the arginine analogue canavanine into cell protein when arginine is omitted from the incubation medium. 2. By labelling arginine-containing proteins with (14-C)leucine and then canavanine-containing proteins with (3-H)leucine in the same cells, it is possible to measure the degradation of both types of protein during a subsequent 'chase' period. With this technique it has been shown that canavanine-containing proteins are degraded at a rate severalfold greater than normal proteins. Comparable results were found when 6-fluorotryptophan was used as an analogue to tryptophan. 3. Control experiments in which the labelling order was reversed or where the animo acid and its analogue were incubated in separate cell cultures support the conclusion that abberrant proteins are rapidly degraded in vivo.

SUBMITTER: Knowles SE

PROVIDER: S-EPMC1165348 | biostudies-other | 1975 Mar

REPOSITORIES: biostudies-other

ACCESS DATA

Json Xml

Similar Datasets

Properties of phosphoenolpyruvate carboxykinase (guanosine triphosphate) synthesized in hepatoma cells in the presence of amino acid analogues.

Project description:Phosphoenolpyruvate carboxykinase (GTP) was induced by a combination of dibutyryl cyclic AMP, theophyline and dexamethasone in Reuber H35 hepatoma cells under conditions where an amino acid in the medium was replaced by an appropriate analogue. 2. With canavanine replacing arginine or with 5-fluorotryptophan or 6-fluorotryptophan replacing tryptophan the induced enzyme had a lower catalytic activity-relative to antibody reactivity. 3. These aberrant enzyme molecules were heat-labile in vitro. 4. Measurements of enzyme degradation in vivo indicated that the canavanine-containing enzyme and the 6-fluorotryptophan-containing enzyme were degraded more rapidly than the enzyme containing all natural amino acids.

| S-EPMC1165347 | biostudies-other

Transcription profiling of human hepatoma cells after amino acid limitation

Project description:1507 known genes have been identified differentially regulated during HisOH treatment by more than 2 fold. This includes 250 down-regulated genes and 1257 up-regulated genes. Experiment Overall Design: Two conditions were used, 8 arrays, 4 for each condition, M-basal condition, H-HisOH treatment.

2010-01-19 | E-GEOD-19495 | biostudies-arrayexpress

FOLD-RATE: prediction of protein folding rates from amino acid sequence.

Project description:We have developed a web server, FOLD-RATE, for predicting the folding rates of proteins from their amino acid sequences. The relationship between amino acid properties and protein folding rates has been systematically analyzed and a statistical method based on linear regression technique has been proposed for predicting the folding rate of proteins. We found that the classification of proteins into different structural classes shows an excellent correlation between amino acid properties and folding rates of two and three-state proteins. Consequently, different regression equations have been developed for proteins belonging to all-alpha, all-beta and mixed class. We observed an excellent agreement between predicted and experimentally observed folding rates of proteins; the correlation coefficients are, 0.99, 0.97 and 0.90, respectively, for all-alpha, all-beta and mixed class proteins. The prediction server is freely available at http://psfs.cbrc.jp/fold-rate/.

| S-EPMC1538837 | biostudies-literature

Predicting protein folding rates from geometric contact and amino acid sequence.

Project description:Protein folding speeds are known to vary over more than eight orders of magnitude. Plaxco, Simons, and Baker (see References) first showed a correlation of folding speed with the topology of the native protein. That and subsequent studies showed, if the native structure of a protein is known, its folding speed can be predicted reasonably well through a correlation with the "localness" of the contacts in the protein. In the present work, we develop a related measure, the geometric contact number, N (alpha), which is the number of nonlocal contacts that are well-packed, by a Voronoi criterion. We find, first, that in 80 proteins, the largest such database of proteins yet studied, N (alpha) is a consistently excellent predictor of folding speeds of both two-state fast folders and more complex multistate folders. Second, we show that folding rates can also be predicted from amino acid sequences directly, without the need to know the native topology or other structural properties.

| S-EPMC2441995 | biostudies-literature

Global Gene Expression of Human Hepatoma Cells After Amino Acid Limitation

Project description:1507 known genes have been identified differentially regulated during HisOH treatment by more than 2 fold. This includes 250 down-regulated genes and 1257 up-regulated genes.

2009-12-20 | GSE19495 | GEO

Degradation of protein translation machinery by amino acid starvation-induced macroautophagy.

Project description:Macroautophagy is regarded as a nonspecific bulk degradation process of cytoplasmic material within the lysosome. However, the process has mainly been studied by nonspecific bulk degradation assays using radiolabeling. In the present study we monitor protein turnover and degradation by global, unbiased approaches relying on quantitative mass spectrometry-based proteomics. Macroautophagy is induced by rapamycin treatment, and by amino acid and glucose starvation in differentially, metabolically labeled cells. Protein dynamics are linked to image-based models of autophagosome turnover. Depending on the inducing stimulus, protein as well as organelle turnover differ. Amino acid starvation-induced macroautophagy leads to selective degradation of proteins important for protein translation. Thus, protein dynamics reflect cellular conditions in the respective treatment indicating stimulus-specific pathways in stress-induced macroautophagy.

| S-EPMC5486358 | biostudies-literature

Prediction of protein folding rates from the amino acid sequence-predicted secondary structure.

Project description:We present a method for predicting folding rates of proteins from their amino acid sequences only, or rather, from their chain lengths and their helicity predicted from their sequences. The method achieves 82% correlation with experiment over all 64 "two-state" and "multistate" proteins (including two artificial peptides) studied up to now.

| S-EPMC428451 | biostudies-literature

Degradation and Mineralization of Benzohydroxamic Acid by Synthesized Mesoporous La/TiO?.

Project description:Rare earth element La-doped TiO? (La/TiO?) was synthesized by the sol-gel method. Benzohydroxamic acid was used as the objective pollutant to investigate the photocatalytic activity of La/TiO?. The physicochemical properties of the prepared materials were characterized by X-ray diffraction, X-ray photoelectron spectroscopy, UV-vis diffuse reflectance spectroscopy, specific surface area and porosity, scanning electron microscopy and transmission electron microscopy. As a result, the doping of La could inhibit the crystal growth of TiO?, increase its specific surface area and expand its response to visible light, thus improving its photocatalytic activity. La/TiO? with the doping ratio of 0.75% calcined at 500 °C, showing the highest photocatalytic activity to degrade benzohydroxamic acid under the irradiation of 300 W mercury lamp. About 94.1% of benzohydroxamic acid with the original concentration at 30 mg·L-1 was removed after 120 min in a solution of pH 4.4 with an La/TiO? amount of 0.5 g·L-1. Furthermore, 88.5% of the total organic carbon was eliminated after 120 min irradiation. In addition, after four recycling runs, La/TiO? still kept high photocatalytic activity on the photodegradation of benzohydroxamic acid. The interfacial charge transfer processes were also hypothesized.

| S-EPMC5086736 | biostudies-literature

Increased oxidation and degradation of cytosolic proteins in alcohol-exposed mouse liver and hepatoma cells.

Project description:We recently developed a sensitive method using biotin-N-maleimide (biotin-NM) as a probe to positively identify oxidized mitochondrial proteins. In this study, biotin-NM was used to identify oxidized cytosolic proteins in alcohol-fed mouse livers. Alcohol treatment for 6 wk elevated the levels of CYP2E1 and nitrotyrosine, a marker of oxidative stress. Markedly increased levels of oxidized proteins were detected in alcohol-fed mouse livers compared to pair-fed controls. The biotin-NM-labeled oxidized proteins from alcohol-exposed mouse livers were subsequently purified with streptavidin-agarose and resolved on 2-DE. More than 90 silver-stained protein spots that displayed differential intensities on 2-D gels were identified by MS. Peptide sequence analysis revealed that many enzymes or proteins involved in stress response, chaperone activity, intermediary metabolism, and antioxidant defense systems such as peroxiredoxin were oxidized after alcohol treatment. Smaller fragments of many proteins were repeatedly detected only in alcohol-fed mice, indicating that many oxidized proteins after alcohol exposure were degraded. Immunoblot results showed that the level of oxidized peroxiredoxin (inactivated) was markedly increased in the alcohol-exposed mouse livers and ethanol-sensitive hepatoma cells compared to the corresponding controls. Our results may explain the underlying mechanism for cellular dysfunction and increased susceptibility to other toxic agents following alcohol-mediated oxidative stress.

| S-EPMC1368983 | biostudies-literature

Nonadaptive Amino Acid Convergence Rates Decrease over Time.

Project description:Convergence is a central concept in evolutionary studies because it provides strong evidence for adaptation. It also provides information about the nature of the fitness landscape and the repeatability of evolution, and can mislead phylogenetic inference. To understand the role of adaptive convergence, we need to understand the patterns of nonadaptive convergence. Here, we consider the relationship between nonadaptive convergence and divergence in mitochondrial and model proteins. Surprisingly, nonadaptive convergence is much more common than expected in closely related organisms, falling off as organisms diverge. The extent of the convergent drop-off in mitochondrial proteins is well predicted by epistatic or coevolutionary effects in our "evolutionary Stokes shift" models and poorly predicted by conventional evolutionary models. Convergence probabilities decrease dramatically if the ancestral amino acids of branches being compared have diverged, but also drop slowly over evolutionary time even if the ancestral amino acids have not substituted. Convergence probabilities drop-off rapidly for quickly evolving sites, but much more slowly for slowly evolving sites. Furthermore, once sites have diverged their convergence probabilities are extremely low and indistinguishable from convergence levels at randomized sites. These results indicate that we cannot assume that excessive convergence early on is necessarily adaptive. This new understanding should help us to better discriminate adaptive from nonadaptive convergence and develop more relevant evolutionary models with improved validity for phylogenetic inference.

| S-EPMC4572784 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data