Deoxyribonuclease (Pyrimidine Dimer)
Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)
Nucleic Acid Conformation
Oxidoreductases Acting on CH-CH Group Donors
Molecular Sequence Data
Dihydrouracil Dehydrogenase (NADP)
Folic Acid Antagonists
Nucleoside Transport Proteins
Carbamoyl-Phosphate Synthase (Ammonia)
Dose-Response Relationship, Radiation
Magnetic Resonance Spectroscopy
Nucleotide Transport Proteins
Amino Acid Sequence
Deoxyribonuclease IV (Phage T4-Induced)
DNA-Directed DNA Polymerase
Chromatography, High Pressure Liquid
Nucleic Acid Heteroduplexes
Heterocyclic Compounds, 2-Ring
Dihydropyrimidine Dehydrogenase Deficiency
Polypyrimidine Tract-Binding Protein
DNA-(Apurinic or Apyrimidinic Site) Lyase
Xeroderma Pigmentosum Group A Protein
Proton-Coupled Folate Transporter
Single-Strand Specific DNA and RNA Endonucleases
Activation of c-Abl tyrosine kinase requires caspase activation and is not involved in JNK/SAPK activation during apoptosis of human monocytic leukemia U937 cells. (1/8131)Genotoxic stress triggers the activation of several sensor molecules, such as p53, JNK1/SAPK and c-Abl, and occasionally promotes the cells to apoptosis. We previously reported that JNK1/SAPK regulates genotoxic stress-induced apoptosis in p53-negative U937 cells by activating caspases. c-Abl is expected to act upstream of JNK1/SAPK activation upon treatment with genotoxic stressors, but its involvement in apoptosis development is still unclear. We herein investigated the kinase activities of c-Abl and JNK1/SAPK during apoptosis elicited by genotoxic anticancer drugs and tumor necrosis factor (TNF) in U937 cells and their apoptosis-resistant variant UK711 cells. We found that the activation of JNK1/SAPK and c-Abl correlated well with apoptosis development in these cell lines. Unexpectedly, however, the JNK1/SAPK activation preceded the c-Abl activation. Moreover, the caspase inhibitor Z-Asp suppressed c-Abl activation and the onset of apoptosis but not the JNK1/SAPK activation. Interestingly, c-Abl tyrosine kinase inhibition by CGP 57148 reduced apoptosis without interfering with JNK1/SAPK activation. These results indicate that c-Abl acts not upstream of JNK1/ SAPK but downstream of caspases during the development of p53-independent apoptosis and is possibly involved in accelerating execution of the cell death pathway. (+info)
Selection and characterization of pre-mRNA splicing enhancers: identification of novel SR protein-specific enhancer sequences. (2/8131)Splicing enhancers are RNA sequences required for accurate splice site recognition and the control of alternative splicing. In this study, we used an in vitro selection procedure to identify and characterize novel RNA sequences capable of functioning as pre-mRNA splicing enhancers. Randomized 18-nucleotide RNA sequences were inserted downstream from a Drosophila doublesex pre-mRNA enhancer-dependent splicing substrate. Functional splicing enhancers were then selected by multiple rounds of in vitro splicing in nuclear extracts, reverse transcription, and selective PCR amplification of the spliced products. Characterization of the selected splicing enhancers revealed a highly heterogeneous population of sequences, but we identified six classes of recurring degenerate sequence motifs five to seven nucleotides in length including novel splicing enhancer sequence motifs. Analysis of selected splicing enhancer elements and other enhancers in S100 complementation assays led to the identification of individual enhancers capable of being activated by specific serine/arginine (SR)-rich splicing factors (SC35, 9G8, and SF2/ASF). In addition, a potent splicing enhancer sequence isolated in the selection specifically binds a 20-kDa SR protein. This enhancer sequence has a high level of sequence homology with a recently identified RNA-protein adduct that can be immunoprecipitated with an SRp20-specific antibody. We conclude that distinct classes of selected enhancers are activated by specific SR proteins, but there is considerable sequence degeneracy within each class. The results presented here, in conjunction with previous studies, reveal a remarkably broad spectrum of RNA sequences capable of binding specific SR proteins and/or functioning as SR-specific splicing enhancers. (+info)
Base excision repair of oxidative DNA damage activated by XPG protein. (3/8131)Oxidized pyrimidines in DNA are removed by a distinct base excision repair pathway initiated by the DNA glycosylase--AP lyase hNth1 in human cells. We have reconstituted this single-residue replacement pathway with recombinant proteins, including the AP endonuclease HAP1/APE, DNA polymerase beta, and DNA ligase III-XRCC1 heterodimer. With these proteins, the nucleotide excision repair enzyme XPG serves as a cofactor for the efficient function of hNth1. XPG protein promotes binding of hNth1 to damaged DNA. The stimulation of hNth1 activity is retained in XPG catalytic site mutants inactive in nucleotide excision repair. The data support the model that development of Cockayne syndrome in XP-G patients is related to inefficient excision of endogenous oxidative DNA damage. (+info)
A correlation between changes in gamma-aminobutyric acid metabolism and seizures induced by antivitamin B6. (4/8131)The effects of DL-penicillamine (DL-PeA), hydrazine and toxopyrimidine (TXP, 2-methyl-6-amino-5-hydroxymethylpyrimidine) on gamma-aminobutyric acid (GABA) metabolism in mouse brain were studied. All these compounds inhibited the activity of glutamate decarboxylase [EC 126.96.36.199] (GAD) and slightly inhibited that of 4-aminobutyrate: 2-oxoglutarate aminotransferase [EC 188.8.131.52] (GABA-T). In contrast, very different effects were observed on GABA levels; hydrazine caused a marked increase, DL-PeA had no effect, and TXP caused a slight decrease in the content of the amino acid. These results could be described by an equation which related the excitable state to changes in the flux of the GABA bypass. Since the values obtained from the equation clearly reflect the seizure activity, it is suggested that the decreased GABA flux might be a cause of convulsions induced by these drugs. (+info)
Selective antiaggressive effects of alnespirone in resident-intruder test are mediated via 5-hydroxytryptamine1A receptors: A comparative pharmacological study with 8-hydroxy-2-dipropylaminotetralin, ipsapirone, buspirone, eltoprazine, and WAY-100635. (5/8131)The present study characterized the effects of the novel, selective, and potent 5-hydroxytryptamine1A (serotonin) (5-HT1A) receptor agonist, alnespirone [S-20499, (S)-N-4-[5-methoxychroman-3-yl)propylamino)butyl- 8-azaspiro-(4,5)-diacetamide, hydrochloride] on offensive and defensive resident-intruder aggression in wild-type rats and compared its actions with those of the prototypical full 5-HT1A agonist 8-hydroxy-2- dipropylaminotetralin (8-OH-DPAT), the partial 5-HT1A agonists ipsapirone and buspirone, and the mixed 5-HT1A/1B agonist eltoprazine. All five agonists exerted effective dose-dependent decreases of offensive aggressive behavior in resident rats; 8-OH-DPAT was the most potent (ID50 = 0.074 mg/kg), followed by eltoprazine (0.24), buspirone (0.72), ipsapirone (1.08), and alnespirone (1.24). However, in terms of selectivity of the antiaggressive effects as determined by the absence of decrements in social interest and general motor activity, alnespirone appeared to be superior. In the defensive aggression test, neither alnespirone nor any of the other four agonists changed defensive behaviors in the intruder rats. The involvement of 5-HT1A receptors in the antiaggressive actions of these drugs was confirmed by showing that the selective 5-HT1A receptor antagonist WAY-100635 (N-[2-[4-(2-methoxyphenyl)-1-piperazinyl]ethyl]-N-(2- pyridinyl)cyclohexanecarboxamide trihydrochloride), which was inactive alone, fully prevented the antiaggressive effects of alnespirone, 8-OH-DPAT, and buspirone and partly reversed those of ipsapirone and eltoprazine. The data clearly indicate that alnespirone effectively suppresses offensive aggression with an advantageous profile of action compared with other full or partial 5-HT1A agonists. These selective antiaggressive actions of alnespirone are mediated by stimulating 5-HT1A receptors, presumably the somatodendritic autoreceptors at the raphe nuclei. Furthermore, the data provide evidence for a major involvement of these 5-HT1A receptors in the modulation of aggressive behavior by 8-OH-DPAT, ipsapirone, buspirone, and eltoprazine. (+info)
Increased lipophilicity and subsequent cell partitioning decrease passive transcellular diffusion of novel, highly lipophilic antioxidants. (6/8131)Oxidative stress is considered a cause or propagator of acute and chronic disorders of the central nervous system. Novel 2, 4-diamino-pyrrolo[2,3-d]pyrimidines are potent inhibitors of iron-dependent lipid peroxidation, are cytoprotective in cell culture models of oxidative injury, and are neuroprotective in brain injury and ischemia models. The selection of lead candidates from this series required that they reach target cells deep within brain tissue in efficacious amounts after oral dosing. A homologous series of 26 highly lipophilic pyrrolopyrimidines was examined using cultured cell monolayers to understand the structure-permeability relationship and to use this information to predict brain penetration and residence time. Pyrrolopyrimidines were shown to be a more permeable structural class of membrane-interactive antioxidants where transepithelial permeability was inversely related to lipophilicity or to cell partitioning. Pyrrole substitutions influence cell partitioning where bulky hydrophobic groups increased partitioning and decreased permeability and smaller hydrophobic groups and more hydrophilic groups, especially those capable of weak hydrogen bonding, decreased partitioning, and increased permeability. Transmonolayer diffusion for these membrane-interactive antioxidants was limited mostly by desorption from the receiver-side membrane into the buffer. Thus, in this case, these in vitro cell monolayer models do not adequately mimic the in vivo situation by underestimating in vivo bioavailability of highly lipophilic compounds unless acceptors, such as serum proteins, are added to the receiving buffer. (+info)
Novel, highly lipophilic antioxidants readily diffuse across the blood-brain barrier and access intracellular sites. (7/8131)In an accompanying article, an in vitro assay for permeability predicts that membrane-protective, antioxidant 2,4-diamino-pyrrolo[2, 3-d]pyrimidines should have improved blood-brain barrier (BBB) permeation over previously described lipophilic antioxidants. Using a first-pass extraction method and brain/plasma quantification, we show here that two of the pyrrolopyrimidines, one of which is markedly less permeable, readily partition into rat brain. The efficiency of extraction was dependent on serum protein binding, and in situ efflux confirms the in vitro data showing that PNU-87663 is retained in brain longer than PNU-89843. By exploiting inherent fluorescence properties of PNU-87663, its distribution within brain and within cells in culture was demonstrated using confocal scanning laser microscopy. PNU-87663 rapidly partitioned into the cell membrane and equilibrates with cytoplasmic compartments via passive diffusion. Although partitioning of PNU-87663 favors intracytoplasmic lipid storage droplets, the compound was readily exchangeable as shown by efflux of compound from cells to buffer when protein was present. The results demonstrated that pyrrolopyrimidines were well suited for quickly accessing target cells within the central nervous system as well as in other target tissues. (+info)
Channeling of carbamoyl phosphate to the pyrimidine and arginine biosynthetic pathways in the deep sea hyperthermophilic archaeon Pyrococcus abyssi. (8/8131)The kinetics of the coupled reactions between carbamoyl-phosphate synthetase (CPSase) and both aspartate transcarbamoylase (ATCase) and ornithine transcarbamoylase (OTCase) from the deep sea hyperthermophilic archaeon Pyrococcus abyssi demonstrate the existence of carbamoyl phosphate channeling in both the pyrimidine and arginine biosynthetic pathways. Isotopic dilution experiments and coupled reaction kinetics analyzed within the context of the formalism proposed by Ovadi et al. (Ovadi, J., Tompa, P., Vertessy, B., Orosz, F., Keleti, T., and Welch, G. R. (1989) Biochem. J. 257, 187-190) are consistent with a partial channeling of the intermediate at 37 degrees C, but channeling efficiency increases dramatically at elevated temperatures. There is no preferential partitioning of carbamoyl phosphate between the arginine and pyrimidine biosynthetic pathways. Gel filtration chromatography at high and low temperature and in the presence and absence of substrates did not reveal stable complexes between P. abyssi CPSase and either ATCase or OTCase. Thus, channeling must occur during the dynamic association of coupled enzymes pairs. The interaction of CPSase-ATCase was further demonstrated by the unexpectedly weak inhibition of the coupled reaction by the bisubstrate analog, N-(phosphonacetyl)-L-aspartate (PALA). The anomalous effect of PALA suggests that, in the coupled reaction, the effective concentration of carbamoyl phosphate in the vicinity of the ATCase active site is 96-fold higher than the concentration in the bulk phase. Channeling probably plays an essential role in protecting this very unstable intermediate of metabolic pathways performing at extreme temperatures. (+info)
Some common examples of purine-pyrimidine metabolism, inborn errors include:
1. Adenine sulfate accumulation: This disorder is caused by a deficiency of the enzyme adenylosuccinase, which is needed to break down adenine sulfate. The build-up of this compound can lead to developmental delays, intellectual disability, and seizures.
2. Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) deficiency: This disorder is caused by a lack of the enzyme HGPRT, which is needed to break down hypoxanthine and guanine. The build-up of these compounds can lead to developmental delays, intellectual disability, and an increased risk of certain cancers.
3. Phosphoribosylpyrophosphate synthase (PRPS) deficiency: This disorder is caused by a lack of the enzyme PRPS, which is needed to break down phosphoribosylpyrophosphate. The build-up of this compound can lead to developmental delays, intellectual disability, and an increased risk of certain cancers.
4. Purine nucleotide phosphorylase (PNP) deficiency: This disorder is caused by a lack of the enzyme PNP, which is needed to break down purine nucleotides. The build-up of these compounds can lead to developmental delays, intellectual disability, and an increased risk of certain cancers.
5. Adenylosuccinate lyase (ADSL) deficiency: This disorder is caused by a lack of the enzyme ADSL, which is needed to break down adenylosuccinate. The build-up of this compound can lead to developmental delays, intellectual disability, and an increased risk of certain cancers.
6. Leukemia-lymphoma-related gene (LRG) deficiency: This disorder is caused by a lack of the LRG gene, which is needed for the development of immune cells. The build-up of abnormal immune cells can lead to an increased risk of leukemia and lymphoma.
7. Methylmalonyl-CoA mutase (MUT) deficiency: This disorder is caused by a lack of the enzyme MUT, which is needed to break down methylmalonyl-CoA. The build-up of this compound can lead to developmental delays, intellectual disability, and an increased risk of certain cancers.
8. Mycobacterium avium intracellulare infection: This disorder is caused by an infection with the bacteria Mycobacterium avium intracellulare. The infection can lead to a variety of symptoms, including fever, fatigue, and weight loss.
9. NAD+ transhydrogenase (NAT) deficiency: This disorder is caused by a lack of the enzyme NAT, which is needed to break down NAD+. The build-up of this compound can lead to developmental delays, intellectual disability, and an increased risk of certain cancers.
10. Neuronal ceroid lipofuscinosis (NCL) diseases: These disorders are caused by a lack of the enzyme ALDH7A1, which is needed to break down certain fats in the body. The build-up of these fats can lead to developmental delays, intellectual disability, and an increased risk of certain cancers.
11. Phenylketonuria (PKU): This disorder is caused by a lack of the enzyme phenylalanine hydroxylase (PAH), which is needed to break down the amino acid phenylalanine. The build-up of phenylalanine can lead to developmental delays, intellectual disability, and an increased risk of certain cancers.
12. Propionic acidemia: This disorder is caused by a lack of the enzyme propionyl-CoA carboxytransferase (PCC), which is needed to break down the amino acid propionate. The build-up of propionate can lead to developmental delays, intellectual disability, and an increased risk of certain cancers.
13. Methylmalonic acidemia: This disorder is caused by a lack of the enzyme methylmalonyl-CoA mutase (MCM), which is needed to break down the amino acid methionine. The build-up of methylmalonyl-CoA can lead to developmental delays, intellectual disability, and an increased risk of certain cancers.
14. Homocystinuria: This disorder is caused by a lack of the enzyme cystathionine beta-synthase (CBS), which is needed to break down the amino acid homocysteine. The build-up of homocysteine can lead to developmental delays, intellectual disability, and an increased risk of certain cancers.
15. maple syrup urine disease (MSUD): This disorder is caused by a lack of the enzyme branched-chain alpha-keto acid dehydrogenase (BCKDH), which is needed to break down the amino acids leucine, isoleucine, and valine. The build-up of these amino acids can lead to developmental delays, intellectual disability, and an increased risk of certain cancers.
16. Tyrosinemia type I: This disorder is caused by a lack of the enzyme fumarylacetoacetate hydrolase (FAH), which is needed to break down the amino acid tyrosine. The build-up of tyrosine can lead to developmental delays, intellectual disability, and an increased risk of certain cancers.
17. Hereditary tyrosinemia type II: This disorder is caused by a lack of the enzyme tyrosine ammonia lyase (TAL), which is needed to break down the amino acid tyrosine. The build-up of tyrosine can lead to developmental delays, intellectual disability, and an increased risk of certain cancers.
18. Galactosemia: This disorder is caused by a lack of the enzyme galactose-1-phosphate uridylyltransferase (GALT), which is needed to break down the sugar galactose. The build-up of galactose can lead to developmental delays, intellectual disability, and an increased risk of certain cancers.
19. Phenylketonuria (PKU): This disorder is caused by a lack of the enzyme phenylalanine hydroxylase (PAH), which is needed to break down the amino acid phenylalanine. The build-up of phenylalanine can lead to developmental delays, intellectual disability, and an increased risk of certain cancers.
20. Methylmalonic acidemia (MMA): This disorder is caused by a lack of the enzyme methylmalonyl-CoA mutase (MCM), which is needed to break down the amino acids methionine and homocysteine. The build-up of these amino acids can lead to developmental delays, intellectual disability, and an increased risk of certain cancers.
In addition to these specific disorders, there are also many other inborn errors of metabolism that can affect various aspects of the body, including the nervous system, the skin, and the muscles. These disorders can be caused by a variety of genetic mutations, and they can have a wide range of symptoms and effects on the body.
Overall, inborn errors of metabolism are a group of rare genetic disorders that can affect various aspects of the body and can have serious health consequences if left untreated. These disorders are often diagnosed through newborn screening programs, and they can be managed with dietary changes, medication, and other treatments. With appropriate treatment, many individuals with inborn errors of metabolism can lead active and productive lives.
The main symptoms of XP include:
1. Extremely sensitive skin that burns easily and develops freckles and age spots at an early age.
2. Premature aging of the skin, including wrinkling and thinning.
3. Increased risk of developing skin cancers, especially melanoma, which can be fatal if not treated early.
4. Poor wound healing and scarring.
5. Eye problems such as cataracts, glaucoma, and poor vision.
6. Neurological problems such as intellectual disability, seizures, and difficulty with coordination and balance.
XP is usually inherited in an autosomal recessive pattern, which means that a child must inherit two copies of the mutated gene, one from each parent, to develop the condition. The diagnosis of XP is based on clinical features, family history, and genetic testing. There is no cure for XP, but treatment options include:
1. Avoiding UV radiation by staying out of the sun, using protective clothing, and using sunscreens with high SPF.
2. Regular monitoring and early detection of skin cancers.
3. Chemoprevention with drugs that inhibit DNA replication.
4. Photoprotection with antioxidants and other compounds that protect against UV damage.
5. Managing neurological problems with medications and therapy.
The prognosis for XP is poor, with most patients dying from skin cancer or other complications before the age of 20. However, with early diagnosis and appropriate treatment, some patients may be able to survive into their 30s or 40s. There is currently no cure for XP, but research is ongoing to develop new treatments and improve the quality of life for affected individuals.
There are several types of erythema, including:
1. Erythema migrans (Lyme disease): A rash that occurs due to an infection with the bacteria Borrelia burgdorferi and is characterized by a red, expanding rash with a central clearing.
2. Erythema multiforme: A condition that causes small, flat or raised red lesions on the skin, often triggered by an allergic reaction to medication or infection.
3. Erythema nodosum: A condition that causes small, painful lumps under the skin, usually due to an allergic reaction to medication or infection.
4. Erythema infectiosum (Fifth disease): A viral infection that causes a red rash on the face, arms, and legs.
5. Erythema annulare centrifugum: A condition that causes a ring-shaped rash with raised borders, often seen in people with autoimmune disorders or taking certain medications.
Treatment for erythema depends on the underlying cause, and may include topical creams or ointments, oral medications, or antibiotics. It is important to seek medical attention if you experience any unusual skin changes or symptoms, as some types of erythema can be a sign of a more serious underlying condition.
Without this enzyme, the medications build up in the body and can cause severe side effects, including nausea, vomiting, diarrhea, and a low white blood cell count. In severe cases, DPD deficiency can lead to life-threatening complications, such as sepsis and organ failure.
DPD deficiency is usually diagnosed through a genetic test that measures the presence and function of the dihydropyrimidine dehydrogenase enzyme. Treatment for DPD deficiency typically involves avoiding medications that trigger the condition and using alternative treatments that do not require the presence of the enzyme. In some cases, medications may be given to help reduce the risk of complications.
The exact prevalence of DPD deficiency is not well established, but it is estimated to affect about 1 in 300 people of European ancestry and a higher percentage of people with certain genetic conditions, such as hereditary colon cancer syndromes. The condition is usually diagnosed in adulthood, although it can sometimes be detected in children who have a family history of DPD deficiency.
Overall, dihydropyrimidine dehydrogenase deficiency is a rare genetic disorder that can cause severe side effects from certain medications used to treat cancer and other conditions. It is important for healthcare providers to be aware of this condition and to test for it in individuals who are being prescribed these medications.
Favism is characterized by a sudden and severe anemia, often triggered by exposure to certain foods or medications that contain a chemical called quinine. Quinine is found in the bark of the cinchona tree, which is used to make antimalarial drugs. In individuals with favism, quinine can cause red blood cells to rupture and die prematurely, leading to anemia and other complications.
Symptoms of favism usually begin within 24 hours of exposure to quinine and may include fatigue, jaundice, dark urine, and a low platelet count. In severe cases, favism can lead to life-threatening complications such as kidney failure and cardiac arrest.
Favism is most commonly found in individuals of Mediterranean or African descent, particularly those from Greece, Italy, Turkey, and the Middle East. It is estimated that approximately 10% of these populations carry the G6PD deficiency that causes favism.
There is no cure for favism, but certain medications and dietary changes can help manage symptoms and prevent complications. Individuals with favism are advised to avoid consuming foods or medications containing quinine, and may require regular monitoring of their red blood cell count and other clinical parameters.
In conclusion, favism is a rare genetic disorder that affects the metabolism of hemoglobin and can cause sudden and severe anemia in certain populations. It is important to be aware of this condition and take necessary precautions to prevent complications, particularly when consuming certain foods or medications containing quinine.
Symptoms of hemolytic anemia may include fatigue, weakness, shortness of breath, dizziness, headaches, and pale or yellowish skin. Treatment options depend on the underlying cause but may include blood transfusions, medication to suppress the immune system, antibiotics for infections, and removal of the spleen (splenectomy) in severe cases.
Prevention strategies for hemolytic anemia include avoiding triggers such as certain medications or infections, maintaining good hygiene practices, and seeking early medical attention if symptoms persist or worsen over time.
It is important to note that while hemolytic anemia can be managed with proper treatment, it may not be curable in all cases, and ongoing monitoring and care are necessary to prevent complications and improve quality of life.
Prevalence: Anemia, hemolytic, congenital is a rare disorder, affecting approximately 1 in 100,000 to 1 in 200,000 births.
Causes: The condition is caused by mutations in genes that code for proteins involved in hemoglobin synthesis or red blood cell membrane structure. These mutations can lead to abnormal hemoglobin formation, red blood cell membrane instability, and increased susceptibility to oxidative stress, which can result in hemolytic anemia.
Symptoms: Symptoms of anemia, hemolytic, congenital may include jaundice (yellowing of the skin and eyes), fatigue, weakness, pale skin, and shortness of breath. In severe cases, the condition can lead to life-threatening complications such as anemia, infections, and kidney failure.
Diagnosis: Anemia, hemolytic, congenital is typically diagnosed through a combination of physical examination, medical history, and laboratory tests, including blood smear examination, hemoglobin electrophoresis, and mutation analysis.
Treatment: Treatment for anemia, hemolytic, congenital depends on the specific underlying genetic cause and may include blood transfusions, folic acid supplements, antibiotics, and/or surgery to remove the spleen. In some cases, bone marrow transplantation may be necessary.
Prognosis: The prognosis for anemia, hemolytic, congenital varies depending on the specific underlying genetic cause and the severity of the condition. With appropriate treatment, many individuals with this condition can lead relatively normal lives, but in severe cases, the condition can be life-threatening.
1. Rabies: A deadly viral disease that affects the central nervous system and is transmitted through the saliva of infected animals, usually through bites.
2. Distemper: A highly contagious viral disease that affects dogs, raccoons, and other carnivorous animals, causing symptoms such as seizures, vomiting, and diarrhea.
3. Parvo: A highly contagious viral disease that affects dogs and other animals, causing severe gastrointestinal symptoms and dehydration.
4. Heartworm: A parasitic infection caused by a worm that infects the heart and blood vessels of animals, particularly dogs and cats.
5. Feline immunodeficiency virus (FIV): A viral disease that weakens the immune system of cats, making them more susceptible to other infections and diseases.
6. Avian influenza: A type of flu that affects birds, including chickens and other domesticated fowl, as well as wild birds.
7. Tuberculosis: A bacterial infection that can affect a wide range of animals, including cattle, pigs, and dogs.
8. Leptospirosis: A bacterial infection that can affect a wide range of animals, including dogs, cats, and wildlife, and can cause symptoms such as fever, kidney failure, and death.
9. Lyme disease: A bacterial infection transmitted through the bite of an infected tick, primarily affecting dogs and humans.
10. Fungal infections: Fungal infections can affect a wide range of animals, including dogs, cats, and livestock, and can cause symptoms such as skin lesions, respiratory problems, and death.
Animal diseases can have a significant impact on animal health and welfare, as well as human health and the economy. They can also be transmitted between animals and humans, making it important to monitor and control animal disease outbreaks to prevent their spread.
Vaccination is an effective way to prevent animal diseases in pets and livestock. Regular vaccinations can help protect against common diseases such as distemper, hepatitis, parvovirus, and rabies, among others. Vaccines can be administered orally, through injection, or through a nasal spray.
Preventative care is key in avoiding animal disease outbreaks. Some of the best ways to prevent animal diseases include:
1. Regular vaccinations: Keeping pets and livestock up to date on their vaccinations can help protect against common diseases.
2. Proper sanitation and hygiene: Keeping living areas clean and free of waste can help prevent the spread of disease-causing bacteria and viruses.
3. Avoiding contact with wild animals: Wild animals can carry a wide range of diseases that can be transmitted to domesticated animals, so it's best to avoid contact with them whenever possible.
4. Proper nutrition: Providing pets and livestock with a balanced diet can help keep their immune systems strong and better able to fight off disease.
5. Monitoring for signs of illness: Regularly monitoring pets and livestock for signs of illness, such as fever, vomiting, or diarrhea, can help identify and treat diseases early on.
6. Quarantine and isolation: Isolating animals that are showing signs of illness can help prevent the spread of disease to other animals and humans.
7. Proper disposal of animal waste: Properly disposing of animal waste can help prevent the spread of disease-causing bacteria and viruses.
8. Avoiding overcrowding: Overcrowding can contribute to the spread of disease, so it's important to provide adequate living space for pets and livestock.
9. Regular veterinary care: Regular check-ups with a veterinarian can help identify and treat diseases early on, and also provide guidance on how to prevent animal diseases.
10. Emergency preparedness: Having an emergency plan in place for natural disasters or other unexpected events can help protect pets and livestock from disease outbreaks.
Hemoglobinuria can be caused by a variety of factors, including:
1. Blood disorders such as sickle cell disease, thalassemia, and von Willebrand disease.
2. Inherited genetic disorders such as hemophilia.
3. Autoimmune disorders such as autoimmune hemolytic anemia.
4. Infections such as septicemia or meningococcemia.
5. Toxins such as lead, which can damage red blood cells and cause hemoglobinuria.
6. Certain medications such as antibiotics and nonsteroidal anti-inflammatory drugs (NSAIDs).
7. Kidney disease or failure.
8. Transfusion-related acute lung injury (TRALI), which can occur after blood transfusions.
9. Hemolytic uremic syndrome (HUS), a condition that occurs when red blood cells are damaged and broken down, leading to kidney failure.
The symptoms of hemoglobinuria may include:
1. Red or brown-colored urine
2. Frequent urination
3. Pale or yellowish skin
5. Shortness of breath
6. Nausea and vomiting
8. Dizziness or lightheadedness
9. Confusion or loss of consciousness in severe cases.
Diagnosis of hemoglobinuria is typically made through urine testing, such as a urinalysis, which can detect the presence of hemoglobin in the urine. Additional tests may be ordered to determine the underlying cause of hemoglobinuria, such as blood tests, imaging studies, or biopsies.
Treatment of hemoglobinuria depends on the underlying cause and severity of the condition. In some cases, treatment may involve addressing the underlying condition that is causing the hemoglobinuria, such as managing an infection or stopping certain medications. Other treatments may include:
1. Fluid and electrolyte replacement to prevent dehydration and maintain proper fluid balance.
2. Medications to help remove excess iron from the body.
3. Blood transfusions to increase the number of red blood cells in the body and improve oxygen delivery.
4. Dialysis to filter waste products from the blood when the kidneys are unable to do so.
5. Supportive care, such as oxygen therapy and pain management.
In severe cases of hemoglobinuria, complications can include:
1. Kidney damage or failure
2. Septicemia (blood infection)
3. Respiratory failure
4. Heart problems
5. Increased risk of infections and other complications.
Prevention of hemoglobinuria involves managing any underlying medical conditions, such as diabetes or infections, and avoiding certain medications that can cause the condition. It is also important to seek medical attention if symptoms of hemoglobinuria develop, as early treatment can help prevent complications and improve outcomes.
There are several types of skin neoplasms, including:
1. Basal cell carcinoma (BCC): This is the most common type of skin cancer, and it usually appears as a small, fleshy bump or a flat, scaly patch. BCC is highly treatable, but if left untreated, it can grow and invade surrounding tissue.
2. Squamous cell carcinoma (SCC): This type of skin cancer is less common than BCC but more aggressive. It typically appears as a firm, flat, or raised bump on sun-exposed areas. SCC can spread to other parts of the body if left untreated.
3. Melanoma: This is the most serious type of skin cancer, accounting for only 1% of all skin neoplasms but responsible for the majority of skin cancer deaths. Melanoma can appear as a new or changing mole, and it's essential to recognize the ABCDE signs (Asymmetry, Border irregularity, Color variation, Diameter >6mm, Evolving size, shape, or color) to detect it early.
4. Sebaceous gland carcinoma: This rare type of skin cancer originates in the oil-producing glands of the skin and can appear as a firm, painless nodule on the forehead, nose, or other oily areas.
5. Merkel cell carcinoma: This is a rare and aggressive skin cancer that typically appears as a firm, shiny bump on the skin. It's more common in older adults and those with a history of sun exposure.
6. Cutaneous lymphoma: This type of cancer affects the immune system and can appear as a rash, nodules, or tumors on the skin.
7. Kaposi sarcoma: This is a rare type of skin cancer that affects people with weakened immune systems, such as those with HIV/AIDS. It typically appears as a flat, red or purple lesion on the skin.
While skin cancers are generally curable when detected early, it's important to be aware of your skin and notice any changes or unusual spots, especially if you have a history of sun exposure or other risk factors. If you suspect anything suspicious, see a dermatologist for an evaluation and potential biopsy. Remember, prevention is key to avoiding the harmful effects of UV radiation and reducing your risk of developing skin cancer.
Symptoms of argininosuccinic aciduria typically appear during infancy or early childhood and may include seizures, developmental delays, intellectual disability, vision loss, and poor muscle tone. Treatment for this condition involves a strict diet that limits the intake of certain amino acids, as well as medication to manage seizures and other symptoms. In some cases, liver transplantation may be necessary.
Argininosuccinic aciduria is diagnosed through a combination of clinical evaluation, laboratory tests, and genetic analysis. Treatment is usually coordinated by a multidisciplinary team of healthcare professionals, including pediatricians, neurologists, metabolism specialists, dietitians, and psychologists. With appropriate treatment and management, many individuals with argininosuccinic aciduria are able to lead active and fulfilling lives.
Overall, argininosuccinic aciduria is a rare and complex genetic disorder that requires careful management and monitoring to prevent complications and improve quality of life for affected individuals.
The term "Sarcoma 180" was coined by a German surgeon named Otto Kunkel in the early 20th century. He described this type of cancer as a highly malignant tumor that grows slowly but is resistant to treatment with surgery, radiation therapy, and chemotherapy.
The exact cause of Sarcoma 180 is not known, but it is believed to be linked to genetic mutations and exposure to certain chemicals or radiation. The disease typically affects middle-aged adults and is more common in men than women.
The symptoms of Sarcoma 180 can vary depending on the location of the tumor, but they may include pain, swelling, redness, and limited mobility in the affected area. If left untreated, the cancer can spread to other parts of the body and be fatal.
Treatment for Sarcoma 180 usually involves a combination of surgery, radiation therapy, and chemotherapy. In some cases, amputation of the affected limb may be necessary. The prognosis for this disease is generally poor, with a five-year survival rate of less than 50%.
In summary, Sarcoma 180 is a rare and aggressive form of cancer that affects connective tissue and has a poor prognosis. It is important for medical professionals to be aware of this condition and its symptoms in order to provide proper diagnosis and treatment.
Deoxyribonuclease (pyrimidine dimer)
Inborn errors of purine-pyrimidine metabolism
Treat Baldwin Johnson
Dihydrouracil dehydrogenase (NAD+)
Complementarity (molecular biology)
Nucleic acid metabolism
Browsing by Subject "Pyrimidines"
Discovery of novel pyrimidine and malonamide derivatives as TGR5 agonists
5-Bromo-4-(2,5-dimethylphenyl)pyrimidine | C12H11BrN2 | CID 26369947 - PubChem
"New pyrimidine-N-ß-D-glucosides: synthesis, biological evaluation, and" by NURAN KAHRİMAN, KIVANÇ PEKER et al.
147972-27-8], MFCD09834966, 4-Chloro-2-(trifluoromethyl)thieno[3,2-d]pyrimidine
7-Chloro-2,5-dimethyl-3-thiophen-2-ylpyrazolo[1,5-a]pyrimidine | VWR
Methyl 5,7-Dichloropyrazolo[1,5-a]Pyrimidine-3-Carboxylate Properties, Molecular Formula, Applications - WorldOfChemicals
biosynthesis of purine and pyrimidine nucleotides slideshare
Mayr's Database Of Reactivity Parameters - Molecule5-methoxyfuroxano[3,4-d]pyrimidine
Network Portal - Function pyrimidine deoxyribonucleoside monophosphate metabolic process
5.14B: Purine and Pyrimidine Synthesis - Biology LibreTexts
Antiproliferative activities of halogenated pyrrolo[3,2-d]pyrimidines<...
Purine Bases, Pyrimidine Bases and Nucleosides (1) (DE-613) - Shodex
Pyrimidine homeostasis is accomplished by directed overflow metabolism. | Lewis-Sigler Institute
4-Chloro-7H-pyrrolo[2,3-d]pyrimidine-5-carbaldehyde | Atuka Inc.
4-(1H-1,2,3,4-Tetrazol-5-yl)pyrimidine - Doron Scientific
pKa Archives - ACD/Labs
Immunosuppression: Practice Essentials, History, Drugs
Synthesis, characterization and cytotoxicity studies of 1,2,3-triazoles and 1,2,4-triazolo 1,5-a pyrimidines in human breast...
The cspA mRNA Is a Thermosensor that Modulates Translation of the Cold-Shock Protein CspA: Molecular Cell
1H-Thieno[3,2-d]pyrimidine-2,4-dione [16233-51-5] glixxlabs.com High quality biochemicals supplier
Immunosuppression: Practice Essentials, History, Drugs
Design, synthesis and biological evaluation of nitric oxide-releasing 5-cyano-6-phenyl-2, 4-disubstituted pyrimidine...
Adrucil - Side Effects, Uses, Dosage, Overdose, Pregnancy, Alcohol | RxWiki
Ronoxidil - Side Effects, Uses, Dosage, Overdose, Pregnancy, Alcohol | RxWiki
- A series of 4-(2,5-dichlorophenoxy)pyrimidine and cyclopropylmalonamide derivatives were synthesized as potent agonists of TGR5 based on a bioisosteric replacement strategy. (nih.gov)
- In this study, syntheses of new pyrimidine-coupled N-ß-glucosides and tetra-O-acetyl derivatives were carried out. (tubitak.gov.tr)
- Humans synthesize the nucleic acids and their derivatives ATP, NAD +, coenzyme A, etc, from amphibolic intermediates.However, injected purine or pyrimidine analogs, including potential anticancer drugs, may nevertheless be incorporated into DNA. (myinfo.la)
- In the present work, we report the synthesis of 1,4-disubstituted 1,2,3-triazoles and 1,2,4-triazolo[1, 5-a]pyrimidine derivatives via copper (I)-catalyzed azide-alkyne cycloaddition (CuAAC) reaction and screened for their anticancer activity against MCF7 cells. (uni-mysore.ac.in)
- Ronoxidil is a brand name medication included in a group of medications called Pyrimidine derivatives . (rxwiki.com)
- Design, synthesis and biological evaluation of nitric oxide-releasing 5-cyano-6-phenyl-2, 4-disubstituted pyrimidine derivatives. (bvsalud.org)
- In this study, a series of nitric oxide (NO) -releasing 5-cyano-6-phenyl-2, 4-disubstituted pyrimidine derivatives were designed and synthesized. (bvsalud.org)
Purine and pyrimidine1
- There are two major synthetic pathways, for purine and pyrimidine bases, respectively, both of which diverge towards their ends to produce the different variants. (myinfo.la)
- No article was found for Purine-Pyrimidine Metabolism, Inborn Errors and UMOD[original query] . (cdc.gov)
- The biosynthesis of pyrimidines is simpler than that of purines. (myinfo.la)
- Pyrimidine homeostasis is accomplished by directed overflow metabolism. (princeton.edu)
- Thus, pyrimidine homeostasis involves dual regulatory strategies, with classical feedback inhibition enhancing metabolic efficiency and directed overflow metabolism ensuring end-product homeostasis. (princeton.edu)
- Detoxification is also mediated by CYP450s, forming a pyridinol (TCP) and a pyrimidine (IMHP), respectively. (cdc.gov)
- Plants possess metabolic pathways for the de novo synthesis of purine nucleotides generating AMP, as well as pyrimidine nucleotides yielding UMP. (myinfo.la)
- The chemical reactions and pathways involving pyrimidine deoxynucleoside monophosphate, a compound consisting of a pyrimidine base linked to a deoxyribose sugar esterified with phosphate on the sugar. (systemsbiology.net)
- In vitro evaluation of the halogenated pyrrolo[3,2-d]pyrimidines identified antiproliferative activities in compounds 1 and 2 against four different cancer cell lines. (johnshopkins.edu)
- UMP, which is also the precursor of CMP, is synthesized in a six-reaction pathway However, in contrast to purine catabolism, the pyrimidine bases in most organisms are subjected to reduction rather than oxidation. (myinfo.la)
- Welco Free pyrimidine bases without sugar residues cannot be recovered. (myinfo.la)
- Upon screening of a series of pyrrolo[3,2-d]pyrimidines, the 2,4-Cl compound 1 was found to exhibit antiproliferative activity at low micromolar concentrations. (johnshopkins.edu)
- New pyrimidine-N-ß-D-glucosides: synthesis, biological evaluation, and" by NURAN KAHRİMAN, KIVANÇ PEKER et al. (tubitak.gov.tr)
- The pyrimidine analogues, used as antineoplastic agents, are a diverse group of agents with similar structures but somewhat different mechanisms of action, activities and spectra of activity. (nih.gov)
- All of the pyrimidine analogues have some degree of direct hepatotoxic potential. (nih.gov)
- Two pyrimidine analogues have been linked to unique forms of liver injury. (nih.gov)
- Review Intracellular Pharmacokinetics of Pyrimidine Analogues used in Oncology and the Correlation with Drug Action. (nih.gov)
- Fluorouracil is a fluorinated pyrimidine analog used in topical form to treat actinic keratoses. (medscape.com)
- Identification of 2-Sulfonyl/Sulfonamide Pyrimidines as Covalent Inhibitors of WRN Using a Multiplexed High-Throughput Screening Assay. (bvsalud.org)
- This screening campaign led to the discovery of 2-sulfonyl/ sulfonamide pyrimidine derivatives as novel covalent inhibitors of WRN helicase activity. (bvsalud.org)