Amanitins
Onset of nucleolar and extranucleolar transcription and expression of fibrillarin in macaque embryos developing in vitro. (1/436)
Specific aims were to characterize the onset of nucleolar and extranucleolar transcription and expression of the nucleolar protein fibrillarin during preimplantation development in vitro in macaque embryos using autoradiographic and immunocytochemical techniques. Autoradiography was performed on whole embryos cultured with [3H]uridine for assessment of nucleolar (rRNA) and extranucleolar (mRNA) transcription. Expression of fibrillarin was immunocytochemically assessed in whole embryos using a primary antibody against fibrillarin and a fluorescein isothiocyanate-conjugated secondary antibody. Extranucleolar incorporation of [3H]uridine was first detected in 2-cell embryos cultured 6-10 h with [3H]uridine. Culture with alpha-amanitin prevented incorporation of label in 2-cell embryos, and treatment with ribonuclease reduced the signal to background levels, indicating that [3H]uridine was incorporated into mRNA and not rRNA or DNA. Nucleolar incorporation of [3H]uridine was not evident in pronucleate-stage or 2- to 5-cell embryos, but it was detected in one 6-cell embryo and in all 8-cell to blastocyst-stage embryos. Fibrillarin was first expressed in some 6- to 7-cell embryos, but it was consistently expressed in all 8-cell embryos. Fibrillarin was localized to the perimeter of the nucleolar precursor bodies, forming a ring that completely encapsulated these structures. Fibrillarin was not expressed in 8- to 16-cell embryos cultured with alpha-amanitin, indicating that it is transcribed, rather than recruited, at the 8-cell stage. In conclusion, in in vitro-fertilized macaque embryos developing in vitro, extranucleolar synthesis of mRNA is initiated at the 2-cell stage while the onset of nucleolar transcription occurs at the 6- to 8-cell stage, coincident with expression of fibrillarin. (+info)Bone marrow ribonucleic acid polymerase. Effect of testosterone on nucleotide incorporation into nuclear RNA. (2/436)
The incorporation of 3H-UTP into RNA by isolated rat bone marrow nuclei is stimulated by testosterone. This effect is hormone and tissue specific. Using alpha-amanitine and different ionic strength conditions it was found that testosterone enhances preferentially RNA polymerase I activity. The sedimentation pattern of RNA isolated from bone marrow nuclei shows that the synthesis of RNA species within the 14-30 S range is mainly stimulated by the hormone. (+info)Stochastic and nonstochastic post-transcriptional silencing of chitinase and beta-1,3-glucanase genes involves increased RNA turnover-possible role for ribosome-independent RNA degradation. (3/436)
Stochastic and nonstochastic post-transcriptional gene silencing (PTGS) in Nicotiana sylvestris plants carrying tobacco class I chitinase (CHN) and beta-1,3-glucanase transgenes differs in incidence, stability, and pattern of expression. Measurements with inhibitors of RNA synthesis (cordycepin, actinomycin D, and alpha-amanitin) showed that both forms of PTGS are associated with increased sequence-specific degradation of transcripts, suggesting that increased RNA turnover may be a general feature of PTGS. The protein synthesis inhibitors cycloheximide and verrucarin A did not inhibit degradation of CHN RNA targeted for PTGS, confirming that PTGS-related RNA degradation does not depend on ongoing protein synthesis. Because verrucarin A, unlike cycloheximide, dissociates mRNA from ribosomes, our results also suggest that ribosome-associated RNA degradation pathways may not be involved in CHN PTGS. (+info)Isolation and characterization of RNA polymerase B from the larval fat body of the tobacco hornworm, Manduca sexta. (4/436)
DNA-dependent RNA polymerase B has been extensively purified from the larval fat body of the tobacco hornworm (Manduca sexta) by employing chromatography on ion-exchange columns of DEAE-Sephadex, DEAE-cellulose and phosphocellulose and centrifugation on glycerol gradients. The isolated enzyme after electrophoresis on acrylamide gels shows one main band and one minor band, both having enzyme activity sensitive to alpha-amanitin. The catalytic and physicochemical properties of the enzyme are similar to those of other eucaryotic B-type RNA polymerases. The enzyme has an apparent molecular weight of 530000, is inhibited 50% by alpha-amanitin at 0.04 microgram/ml and shows maximum activity on denatured DNA at 5 mM Mn2+ and 100 mM ammonium sulfate. An antibody was obtained that cross-reacts with the pure enzyme and forms a precipitin line. This antibody does not cross react with either Escherichia coli RNA polymerase or with wheat germ RNA polymerase but does react with one of the B polymerases isolated from wing tissue of the silkmoth, Antheraea pernyi. (+info)Inefficient processing impairs release of RNA from the site of transcription. (5/436)
We describe here for the first time the site of retention within the nucleus of pre-mRNA processing mutants unable to be exported to the cytoplasm. Fluorescence in situ hybridization was used to detect transcripts from human beta-globin genes that are either normal or defective in splicing or 3' end formation. Nuclear transcripts of both wild-type and mutant RNAs are detected only as intranuclear foci that colocalize with the template gene locus. The kinetics of transcript release from the site of transcription was assessed by treatment of cells with the transcriptional inhibitors actinomycin D, alpha-amanitin and DRB. These drugs induce the rapid disappearance of nuclear foci corresponding to wild-type human beta-globin RNA. In contrast, pre-mRNA mutants defective in either splicing or 3' end formation and which fail to be transported to the cytoplasm, are retained at the site of transcription. Therefore, 3' end processing and splicing appear to be rate limiting for release of mRNA from the site of transcription. (+info)Ubiquitination of RNA polymerase II large subunit signaled by phosphorylation of carboxyl-terminal domain. (6/436)
A sensitive assay using biotinylated ubiquitin revealed extensive ubiquitination of the large subunit of RNA polymerase II during incubations of transcription reactions in vitro. Phosphorylation of the repetitive carboxyl-terminal domain of the large subunit was a signal for ubiquitination. Specific inhibitors of cyclin-dependent kinase (cdk)-type kinases suppress the ubiquitination reaction. These kinases are components of transcription factors and have been shown to phosphorylate the carboxyl-terminal domain. In both regulation of transcription and DNA repair, phosphorylation of the repetitive carboxyl-terminal domain by kinases might signal degradation of the polymerase. (+info)The transcriptional inhibitors, actinomycin D and alpha-amanitin, activate the HIV-1 promoter and favor phosphorylation of the RNA polymerase II C-terminal domain. (7/436)
Actinomycin D and alpha-amanitin are commonly used to inhibit transcription. Unexpectedly, however, the transcription of the human immunodeficiency virus (HIV-1) long terminal repeats (LTR) is shown to be activated at the level of elongation, in human and murine cells exposed to these drugs, whereas the Rous sarcoma virus LTR, the human cytomegalovirus immediate early gene (CMV), and the HSP70 promoters are repressed. Activation of the HIV LTR is independent of the NFkappaB and TAR sequences and coincides with an enhanced average phosphorylation of the C-terminal domain (CTD) from the largest subunit of RNA polymerase II. Both the HIV-1 LTR activation and the bulk CTD phosphorylation enhancement are prevented by several CTD kinase inhibitors, including 5, 6-dichloro-1-beta-D-ribofuranosylbenzimidazole. The efficacies of the various compounds to block CTD phosphorylation and transcription in vivo correlate with their capacities to inhibit the CDK9/PITALRE kinase in vitro. Hence, the positive transcription elongation factor, P-TEFb, is likely to contribute to the average CTD phosphorylation in vivo and to the activation of the HIV-1 LTR induced by actinomycin D. (+info)RNA polymerase II targets pre-mRNA splicing factors to transcription sites in vivo. (8/436)
Biochemical evidence indicates that pre-mRNA splicing factors physically interact with the C-terminal domain of the largest subunit of RNA polymerase II. We have investigated the in vivo function of this interaction. In mammalian cells, truncation of the CTD of RNA pol II LS prevents the targeting of the splicing machinery to a transcription site. In the absence of the CTD, pre-mRNA splicing is severely reduced. The presence of unspliced RNA alone is not sufficient for the accumulation of splicing factors at the transcription site, nor for its efficient splicing. Our results demonstrate a critical role for the CTD of RNA pol II LS in the intranuclear targeting of splicing factors to transcription sites in vivo. (+info)Amanitins are a type of bicyclic octapeptide toxin found in several species of mushrooms belonging to the Amanita genus, including the death cap (Amanita phalloides) and the destroying angel (Amanita virosa). These toxins are part of the group of compounds known as amatoxins.
Amanitins are highly toxic to humans and other animals, affecting the liver and kidneys in particular. They work by inhibiting RNA polymerase II, an enzyme that plays a crucial role in gene expression by transcribing DNA into messenger RNA (mRNA). This interference with protein synthesis can lead to severe damage to cells and tissues, potentially resulting in organ failure and death if left untreated.
Symptoms of amanitin poisoning typically appear in two phases. The first phase, which occurs within 6-24 hours after ingestion, includes gastrointestinal distress such as vomiting, diarrhea, and abdominal pain. This initial phase may subside for a short period, giving a false sense of recovery. However, the second phase, which can occur 3-7 days later, is characterized by liver and kidney damage, with symptoms such as jaundice, disorientation, seizures, coma, and ultimately, multiple organ failure if not treated promptly and effectively.
Treatment for amanitin poisoning usually involves supportive care, such as fluid replacement and addressing any complications that arise. In some cases, medications like silibinin (from milk thistle) or activated charcoal may be used to help reduce the absorption and toxicity of the amanitins. Additionally, liver transplantation might be considered in severe cases where organ failure is imminent. Prevention is key when it comes to amanitin poisoning, as there is no antidote available. Being able to identify and avoid potentially deadly mushrooms is essential for foragers and those who enjoy gathering wild fungi.
Amanitin
Β-Amanitin
Α-Amanitin
Γ-Amanitin
Ε-Amanitin
Galerina marginata
Amanita hygroscopica
Amatoxin
RNA polymerase
Lepiota brunneoincarnata
Amanita phalloides
Mushroom poisoning
Galerina sulciceps
Galerina
Amanita
Hepatotoxicity
Oligopeptide
Cyclic peptide
Amanita bisporigera
Ribosomally synthesized and post-translationally modified peptides
Amanita citrina
Amaninamide
Horizontal gene transfer
Amanita exitialis
Indocyanine green
Amanita virosa
Protein synthesis inhibitor
Amanita fuliginea
Aptamer
Patrick Cramer
Amanitin - Wikipedia
Transcription organizes euchromatin via microphase separation | Nature Communications
How does Alpha-Amanitin work? - Whatisflike.com
Mushroom Toxicity: Practice Essentials, Pathophysiology, Etiology
Beware the Amanitin mushroom in Michigan | aec.vet
Molecular mechanism of the interaction between amanitin and RNA polymerase II
HDP-101; Anti-CD269-ADC; Anti-CD269-amanitin-ADC » ADC Review
List of devices falling within Class AMANITIN ( ORGANIC POISONS ) - codice: W01029002
Emergency Response Branch Laboratory Capability | CDC
Evaluation and comparison of alpha- and beta-amanitin toxicity on MCF-7 cell line
Botanical Electronic News - 416
Mushroom Poisoning Syndromes - North American Mycological Association
"Effects of alpha-amanitin on the development of mouse ova in culture." by I L. Levey, D E. Troike et al.
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Toxin6
- How does mushroom toxin alpha Amanitin inhibits the process of transcription? (whatisflike.com)
- The test also could be a practical and definitive way for mushroom foragers to identify and avoid eating mushrooms with amanitin toxin if a commercial partner can be found to produce and market a test kit. (usda.gov)
- The lethal amanitas all produce a toxin called ɑ-amanitin, also known as AMA, which attacks the liver and kidneys. (kunr.org)
- It is an oncology specialist and the first company to develop the toxin Amanitin into cancer therapies. (goerg.de)
- Heidelberg Pharma is an oncology specialist and the first company to develop the toxin Amanitin into cancer therapies using its proprietary Antibody Targeted Amanitin Conjugate (ATAC) technology and to advance the biological mode of action of the toxin as a novel therapeutic principle. (bio-pro.de)
- amanitin poisoning model with three different toxin levels. (erbakan.edu.tr)
Toxicity5
- In addition, the relationship between the toxicity and the structures of amanitins was carefully studied. (magtech.com.cn)
- The difference of toxicity in nine amanitins derived from the different substitutes of R2, and the binding ability was closely related with the toxicity. (magtech.com.cn)
- Results: The alpha-amanitin showed a higher toxicity at 36 h, while the highest inhibition of protein synthesis by the beta-amanitin was observed at 24 h. (ibu.edu.tr)
- Conclusion: It was shown that the beta-amanitin may be responsible for toxicity, like alpha-amanitin, in Amanita phalloides mushroom poisoning. (ibu.edu.tr)
- If the gastrointestinal distress begins 6 to 24 hours after ingestion of the mushrooms, there is a possibility of a very serious toxicity from Amatoxins (see Amanitin). (namyco.org)
Amatoxin1
- Amanitin may refer to several related amatoxins: α-Amanitin β-Amanitin γ-Amanitin ε-Amanitin Amatoxin, a class of toxic compounds that include the amanitins Amanin, another amatoxin This set index article lists chemical compounds articles associated with the same name. (wikipedia.org)
Mushroom4
- Background/aim: Alpha- and beta-amanitins are the main toxins of the poisonous Amanita phalloides mushroom. (ibu.edu.tr)
- Amanitin is the class of mushroom toxins that cause the most serious issues. (usda.gov)
- The new test can identify the presence of as little as 10 parts per billion (equivalent to 10 cents out of $10 million) of amanitin in about 10 minutes from a rice grain size sample of a mushroom or in the urine of someone who has eaten a poisonous amanitin-containing mushroom. (usda.gov)
- This test can provide more information about a wild mushroom beyond physical appearance and characteristics, and detect something we cannot even see-the presence of amanitins," said Bever. (usda.gov)
Cyclic3
- Platform Technologies in Drug Discovery and Validation α-Amanitin is a highly toxic cyclic octopeptide found in genus of mushrooms known as Amanita, including Amanita phalloides, Amanita verna, and Amanita virosa (Fig. 12). (whatisflike.com)
- Toxicology and Human Environments Alpha-amanitin, a cyclic octapeptide, is toxic because of its affinity for RNA polymerase II in eukaryotic cells. (whatisflike.com)
- Alpha-amanitin, a cyclic octapeptide, is toxic because of its affinity for RNA polymerase II in eukaryotic cells. (whatisflike.com)
Amanita1
- Materials and methods: The alpha- and beta-amanitins used for this research were purified from Amanita phalloides by preparative high-performance liquid chromatography The MCF-7 breast cancer cell line was used, and specific concentrations of the toxins (100, 10, 1, 0.1, and 0.01 mu g/mL) were applied to the cells. (ibu.edu.tr)
Mushrooms2
Polymerase7
- α-Amanitin has an unusually strong and specific attraction to the enzyme RNA polymerase II. (whatisflike.com)
- Alpha amanitin inhibits RNA polymerase II (pol II) by blocking initiation and elongation of transcription. (whatisflike.com)
- How does Alpha Amanitin inhibit RNA polymerase? (whatisflike.com)
- Which RNA polymerase in man is inhibited by Amanitin? (whatisflike.com)
- α-Amanitin is a well-known specific inhibitor of RNA polymerase II (RNAPII) in vitro and in vivo. (whatisflike.com)
- Molecular docking was introduced to study the molecular mechanism of the interaction between amanitin and RNA polymerase II. (magtech.com.cn)
- E. coli RNA polymerase added to a yeast extract pretreated with α-amanitin was also halted by rho at these same two sites. (elsevierpure.com)
Liver2
- Several toxins have been isolated from this poisonous toadstool, but the constituent that damages the liver and kidneys of anyone that eats the Deathcap is known as α-amanitin. (first-nature.com)
- The principal toxic constituent is α-amanitin , which damages the liver and kidneys , causing hepatic and renal failure that can be fatal. (amanitaresearch.com)
Toxic principle1
- Silymarin protects against its toxic principle α-amanitin by preventing its uptake through hepatocyte membranes and inhibiting the effects of tumour necrosis factor-α, which exacerbates lipid peroxidation. (springer.com)
Urine1
- Early detection of amanitin in a patient's urine would help doctors trying to make a diagnosis. (usda.gov)
Inhibition2
- Through the analyses of docking results, the binding mode, the binding site, the docking energy, and the inhibition constant of nine amanitins were obtained, which were in accordance with the experimental results. (magtech.com.cn)
- The early inhibition of protein synthesis for beta-amanitin might be useful for future experiments and research. (ibu.edu.tr)
Fatal1
- Why is α Amanitin fatal? (whatisflike.com)
Alpha8
- How does Alpha-Amanitin work? (whatisflike.com)
- Where is Alpha-Amanitin found? (whatisflike.com)
- Why is Alpha-Amanitin toxic? (whatisflike.com)
- Although there are many studies available concerning alpha-amanitin, there are limited data about beta-amanitin in the literature. (ibu.edu.tr)
- Therefore, this study is aimed at comparing the toxic effects of alpha- and beta-amanitin on the MCF-7 cell line. (ibu.edu.tr)
- Effects of alpha-amanitin on the development of mouse ova in culture. (jax.org)
- the most significant of these are the alpha and beta subtypes of amanitin. (medscape.com)
- About 60% of absorbed alpha-amanitin is excreted into the bile. (medscape.com)
Medical1
- A través de la International Medical Devices Database no estamos sugiriendo que compañías u otras entidades mencionadas en la base de datos hayan sido parte de una conducta ilegal o hayan actuado de manera impropia. (icij.org)
Alpha-amanitin5
- It has specific requirements for cations and salt and has shown an intermediate sensitivity to alpha-amanitin in comparison to RNA polymerase I and II. (harvard.edu)
- In the first group (n:14), the serum levels of alpha-amanitin were measured within the first 24 hours of admittance and eight cases (57%) were diagnosed as having intoxication by the species of Amanita phalloides. (cshd.org.tr)
- In the second group of patients, serum alpha-amanitin levels could not be measured. (cshd.org.tr)
- Alpha-amanitin is the main toxin from the species Amanitia phalloides, poisonous if ingested by humans or animals. (bvsalud.org)
- It has different requirements for cations and salts than RNA polymerase II and III and is not inhibited by alpha-amanitin. (ucdenver.edu)
Toxins2
- The mushroom contains toxins known as amanitin, which damage liver cells. (livescience.com)
- Amanitin is thought to be the most lethal of all mushroom toxins and is found in both the death cap and the destroying angel. (mushroom-appreciation.com)
Therapeutic1
- 21. Therapeutic potential of amanitin-conjugated anti-epithelial cell adhesion molecule monoclonal antibody against pancreatic carcinoma. (nih.gov)
Toxic1
- Amanitin may refer to several related amatoxins: α-Amanitin β-Amanitin γ-Amanitin ε-Amanitin Amatoxin, a class of toxic compounds that include the amanitins Amanin, another amatoxin This set index article lists chemical compounds articles associated with the same name. (wikipedia.org)
Article1
- For an interesting article on how poisonous mushrooms produce amanitin see this article from Science News . (mushroom-appreciation.com)
Include1
- Examples include netropsin, amanitin, and others. (newscase.com)
Effects1
- amanitin by preventing its uptake through hepatocyte membranes and inhibiting the effects of tumour necrosis factor- , which exacerbates lipid peroxidation. (medscape.com)