Inorganic or organic salts and esters of arsenic acid.
Oxidoreductases that specifically reduce arsenate ion to arsenite ion. Reduction of arsenate is a critical step for its biotransformation into a form that can be transported by ARSENITE TRANSPORTING ATPASES or complexed by specific sulfhydryl-containing proteins for the purpose of detoxification (METABOLIC DETOXIFICATION, DRUG). Arsenate reductases require reducing equivalents such as GLUTAREDOXIN or AZURIN.
A general class of integral membrane proteins that transport ions across a membrane against an electrochemical gradient.
Efflux pumps that use the energy of ATP hydrolysis to pump arsenite across a membrane. They are primarily found in prokaryotic organisms, where they play a role in protection against excess intracellular levels of arsenite ions.
A shiny gray element with atomic symbol As, atomic number 33, and atomic weight 75. It occurs throughout the universe, mostly in the form of metallic arsenides. Most forms are toxic. According to the Fourth Annual Report on Carcinogens (NTP 85-002, 1985), arsenic and certain arsenic compounds have been listed as known carcinogens. (From Merck Index, 11th ed)
Inorganic salts or organic esters of arsenious acid.
A plant genus of the family PTERIDACEAE. Members contain entkaurane DITERPENES. The name is similar to bracken fern (PTERIDIUM).
Inorganic salts of phosphoric acid.
Inorganic or organic compounds that contain arsenic.
An arsenical that has been used as a dermatologic agent and as an herbicide.
A metallic element that has the atomic symbol Sb, atomic number 51, and atomic weight 121.75. It is used as a metal alloy and as medicinal and poisonous salts. It is toxic and an irritant to the skin and the mucous membranes.
A family of gram-negative, moderately halophilic bacteria in the order Oceanospirillales. Members of the family have been isolated from temperate and Antarctic saline lakes, solar salt facilities, saline soils, and marine environments.
Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.
A genus of gram-negative, facultatively anaerobic rods. It is a saprophytic, marine organism which is often isolated from spoiling fish.
A plant genus of the family BRASSICACEAE. Members contain crambin.
A subgroup of aquaporins that transport WATER; GLYCEROL; and other small solutes across CELL MEMBRANES.
Disorders associated with acute or chronic exposure to compounds containing ARSENIC (ARSENICALS) which may be fatal. Acute oral ingestion is associated with gastrointestinal symptoms and an encephalopathy which may manifest as SEIZURES, mental status changes, and COMA. Chronic exposure is associated with mucosal irritation, desquamating rash, myalgias, peripheral neuropathy, and white transverse (Mees) lines in the fingernails. (Adams et al., Principles of Neurology, 6th ed, p1212)
A genus of gram-negative, straight or slightly curved rods which are motile by polar flagella and which accumulate poly-beta-hydroxybutyrate within the cells.
A schistosomicide possibly useful against other parasites. It has irritant emetic properties and may cause lethal cardiac toxicity among other adverse effects.
The type species of gram-negative, anaerobic bacteria of the genus DESULFOVIBRIO. It is found in FRESHWATER; SOIL, and in marine or brackish water.
Membrane proteins that are involved in the active transport of phosphate.

Probing the function of the conserved tryptophan in the flexible loop of the Yersinia protein-tyrosine phosphatase. (1/405)

The involvement of the strictly conserved Trp354 residue in the catalysis of the Yersinia protein tyrosine phosphatase (PTPase) has been investigated by site-directed mutagenesis and kinetic studies. Crystallographic structural data have revealed that Trp354 interacts with the active site Arg409 and is located at one of the hinge positions of the flexible surface loop (WpD loop) which also harbors the general acid/base (Asp356) essential for catalysis [Schubert, H. L., Fauman, E. B., Stuckey, J. A., Dixon, J. E. & Saper, M. A. (1995) Protein Sci. 4, 1904-1913]. Two mutants were constructed and expressed that contained the Trp354-->Phe and Trp354-->Ala substitutions. The K(m) of the W354F and W354A mutants were not significantly different from that of the wild-type. However, a major decrease in the affinity for oxyanions was observed for the mutants, which is consistent with Trp354 playing a role in aligning Arg409 for oxyanion binding. In addition replacement of Trp354 with Phe or Ala caused a decrease in kcat of 200-fold and 480-fold, respectively, and impaired the ability of the mutant enzymes to stabilize the negative charge in the leaving group at the transition state. In fact, the W354F and W354A mutants exhibited catalytic efficiency and leaving group dependency similar to those observed for the general acid-deficient PTPase D356N. These results indicate that Trp354 is an important residue that keeps the WpD loop in a catalytically competent conformation and positions the general acid/base Asp356 in the correct orientation for proton transfer.  (+info)

Sulfurospirillum barnesii sp. nov. and Sulfurospirillum arsenophilum sp. nov., new members of the Sulfurospirillum clade of the epsilon Proteobacteria. (2/405)

Two strains of dissimilatory arsenate-reducing vibrio-shaped bacteria are assigned to the genus Sulfurospirillum. These two new species, Sulfurospirillum barnesii strain SES-3T and Sulfurospirillum arsenophilum strain MIT-13T, in addition to Sulfurospirillum sp. SM-5, two strains of Sulfurospirillum deleyianum, and Sulfurospirillum arcachonense, form a distinct clade within the epsilon subclass of the Proteobacteria based on 16S rRNA analysis.  (+info)

Enhanced transcription factor DNA binding and gene expression induced by arsenite or arsenate in renal slices. (3/405)

Although the kidney represents a target for the accumulation and toxicity of arsenic, little is known about the molecular targets of arsenic in this organ. Therefore, these studies were designed to examine the molecular impact of arsenite [As(III)] and arsenate [As(V)] at low (nanomolar) concentrations. Precision-cut rabbit renal cortical slices were challenged with As(III) or As(V) for up to 8 h. Neither form of the metal induced overt cytotoxicity as assessed by intracellular K+ levels over this time period at concentrations from 0.01-10 microM. In addition, no alterations in the expression of Hsp 60, 70, or 90 were observed. However, induction of heme oxygenase-1 (Hsp 32) was seen following a 4-h challenge with As(III), but not with As(V). As(III) and As(V) induced DNA binding of AP-1 at 2- and 4-h exposure; following a 6-h exposure there was no difference. Although no alteration in the DNA binding activity of ATF-2 was induced by As(III) or As(V), both forms enhanced the DNA binding activity of Elk-1. Enhanced DNA binding activity of AP-1 and Elk-1 correlated with increased gene expression of c-fos, but not c-jun, at 2 h. c-myc gene expression was also induced by As(III) and As(V), albeit at a later time point (6 h). These results suggest that acute arsenic challenge, by either As(III) or As(V), is associated with discrete alterations in the activity of signaling pathways and gene expression in renal tissue.  (+info)

N-acetylneuraminic acid transport by Streptococcus oralis strain AR3. (4/405)

Streptococcus oralis has emerged as one of the most important organisms of the viridans streptococcus group in terms of infections and is recognised as an agent of infective endocarditis and, in immunocompromised patients, septicaemia. The mechanisms by which this organism proliferates in vivo are unknown. However, host-derived sialic acids -- including N-acetylneuraminic acid (NeuNAc) which is present in serum and cell-associated glycoproteins -- are a potential source of fermentable carbohydrate for bacterial proliferation, especially for sialidase-producing bacteria, including S. oralis. To further elucidate the role of NeuNAc in supporting growth, this study determined the ability of S. oralis strain AR3 (isolated from a patient with infective endocarditis) to transport NeuNAc and characterised the transport system. The transport of [14C]-labelled NeuNAc into S. oralis was monitored and this transport system was induced by growth of the bacteria in the presence of the N-acetylated sugars NeuNAc, N-acetylglucosamine and N-acetylmannosamine. The transport system followed typical Michaelis-Menten kinetics, with a Km of 21.0 microM and a Vmax of 2.65 nmoles of NeuNAc transported/min/mg of dry cell mass. NeuNAc transport was inhibited by the presence of exogenous N-glycolylneuraminic acid, a related sialic acid. Chlorhexidine, NaF and 2,4-dinitrophenol were potent inhibitors of the transport system, suggesting that the uptake of NeuNAc occurs via a proton motive force-dependent permease system. This is the first report of the mechanism by which NeuNAc transport occurs in pathogenic streptococci. This transport process may have relevance to the acquisition of a source of fermentable carbohydrate and thus bacterial proliferation in vivo.  (+info)

Sodium arsenate induces overproduction of interleukin-1alpha in murine keratinocytes: role of mitochondria. (5/405)

It has recently been demonstrated that arsenic induces overexpression of keratinocyte-derived growth factors, which are likely to have a significant role in arsenic-induced skin hyperkeratoses and cancer. The mechanism(s) involved in this induction are, however, still elusive. The purpose of this study was to investigate the early intracellular events that follow in vitro treatment with sodium arsenate in a murine keratinocyte cell line (HEL30), which leads to cytokine overproduction. First, we observed that sodium arsenate induced a concentration-dependent production of interleukin-1alpha and a significant increase in cell proliferation, that could be suppressed by the addition of a neutralizing antibody against murine interleukin-1alpha, confirming the ability of arsenic to induce keratinocyte growth-promoting cytokines. Electron microscopic analysis revealed that arsenate induced a dramatic alteration in keratinocyte mitochondria. This effect could be prevented by rotenone pretreatment, which suggests the possible involvement of mitochondria-derived reactive oxygen species. Arsenic induced a concentration- and time-dependent increase in cellular oxidative activity, which was followed by activation of redox-sensitive transcription factors such as nuclear factor-kappaB and activator protein-1, that are essential for interleukin-1alpha synthesis. Prior treatment with rotenone or prolonged treatment with ethidium bromide, an inhibitor of mitochondrial DNA and RNA synthesis, to deplete cells of functional mitochondria, completely prevented sodium arsenate-induced interleukin-1alpha production, this indicates the pivotal role of these organelles in sodium arsenate-induced keratinocyte growth factors.  (+info)

Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction. (6/405)

In Escherichia coli ArsC catalyzes the reduction of arsenate to arsenite using GSH with glutaredoxin as electron donors. E. coli has three glutaredoxins: 1, 2, and 3, each with a classical -Cys-Pro-Tyr-Cys- active site. Glutaredoxin 2 is the major glutathione disulfide oxidoreductase in E. coli, but its function remains unknown. In this report glutaredoxin 2 is shown to be the most effective hydrogen donor for the reduction of arsenate by ArsC. Analysis of single or double cysteine-to-serine substitutions in the active site of the three glutaredoxins indicated that only the N-terminal cysteine residue is essential for activity. This suggests that, during the catalytic cycle, ArsC forms a mixed disulfide with GSH before being reduced by glutaredoxin to regenerate the active ArsC reductase.  (+info)

Signal transduction pathways regulated by arsenate and arsenite. (7/405)

Arsenate and arsenite activate c-Jun N-terminal kinase (JNK), however, the mechanism by which this occurs is not known. By expressing inhibitory mutant small GTP-binding proteins, p21-activated kinase (PAK) and mitogen-activated protein kinase/extracellular signal-regulated kinase kinase kinases (MEKKs), we have identified specific proteins that are involved in arsenate- and arsenite-mediated activation of JNK. We observe a distinct difference between arsenate and arsenite signaling, which demonstrates that arsenate and arsenite are capable of activating unique proteins. Both arsenate and arsenite activation of JNK requires Rac and Rho. Neither arsenate nor arsenite signaling was inhibited by a dominant-negative mutant of Cdc42 or Ras. Arsenite stimulation of JNK requires PAK, whereas arsenate-mediated activation of JNK was unaffected by inhibitory mutant PAK. Of the four MEKKs tested, only MEKK3 and MEKK4 are involved in arsenate-mediated activation of JNK. In contrast, arsenite-mediated JNK activation requires MEKK2, MEKK3 and MEKK4. These results better define the mechanisms by which arsenate and arsenite activate JNK and demonstrate differences in the regulation of signal transduction pathways by these inorganic arsenic species.  (+info)

Interactions of arsenate, sulfate and phosphate with yeast mitochondria. (8/405)

In the presence of K(+), addition of ATP or ethanol to yeast mitochondria triggers the depletion of the transmembrane potential (DeltaPsi) and this is prevented by millimolar concentrations of phosphate (PO(4)). Different monovalent and polyvalent anions were tested for their protective effects on mitochondria from Saccharomyces cerevisiae. Only arsenate (AsO(4)) and sulfate (SO(4)) were as efficient as PO(4) to protect mitochondria against the K(+) mediated swelling, depletion of the DeltaPsi, and decrease in the ratio of uncoupled state to state 4 respiration rates. Protection by PO(4), SO(4) or AsO(4) was inhibited by mersalyl, suggesting that these anions interact with a site located in the matrix side. In addition, the effects of SO(4) and AsO(4) on the F(1)F(0)-ATPase were tested: both SO(4) and AsO(4) inhibited the synthesis of ATP following competitive kinetics against PO(4) and non-competitive kinetics against ADP. The mersalyl sensitive uptake of (32)PO(4) was not inhibited by SO(4) or AsO(4), suggesting that the synthesis of ATP was inhibited at the F(1)F(0)-ATPase. The hydrolysis of ATP was not inhibited, only a stimulation was observed when AsO(4) or sulfite (SO(3)) were added. It is suggested that the structure and charge similarities of PO(4), AsO(4) and SO(4) result in undiscriminated binding to at least two sites located in the mitochondrial matrix: at one site, occupation by any of these three anions results in protection against uncoupling by K(+); at the second site, in the F(1)F(0)-ATPase, AsO(4) and SO(4) compete for binding against PO(4) leading to inhibition of the synthesis of ATP.  (+info)

Arsenates are salts or esters of arsenic acid (AsO4). They contain the anion AsO4(3-), which consists of an arsenic atom bonded to four oxygen atoms in a tetrahedral arrangement. Arsenates can be found in various minerals, and they have been used in pesticides, wood preservatives, and other industrial applications. However, arsenic is highly toxic to humans and animals, so exposure to arsenates should be limited. Long-term exposure to arsenic can cause skin lesions, cancer, and damage to the nervous system, among other health problems.

Arsenate reductases are enzymes that catalyze the reduction of arsenate (As(V)) to arsenite (As(III)). This reaction is a critical step in the detoxification process of arsenic compounds in many organisms, including bacteria, fungi, and plants. The enzyme typically uses thioredoxin or glutaredoxin as an electron donor to reduce arsenate.

The medical significance of arsenate reductases lies in their role in arsenic detoxification and resistance. Exposure to high levels of arsenic can lead to a variety of health issues, including skin lesions, cancer, and neurological disorders. Understanding the mechanisms of arsenate reduction and detoxification may provide insights into new strategies for treating arsenic poisoning and developing environmental remediation technologies.

Ion pumps, also known as ion transporters, are membrane-bound proteins that actively transport ions across a biological membrane against their electrochemical gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate), and allows cells to maintain resting potentials, regulate intracellular ion concentrations, and facilitate various physiological processes such as nerve impulse transmission, muscle contraction, and cell volume regulation.

Ion pumps can transport one or more types of ions, including sodium (Na+), potassium (K+), chloride (Cl-), calcium (Ca2+), and protons (H+). A well-known example of an ion pump is the Na+/K+ ATPase, which transports three sodium ions out of the cell and two potassium ions into the cell for each ATP molecule hydrolyzed. This creates a concentration gradient that drives the passive transport of Na+ and K+ ions through other channels, contributing to the resting membrane potential.

Arsenite transporting ATPases are a type of membrane-bound enzyme complexes that use the energy from ATP hydrolysis to actively transport arsenic compounds across cell membranes. They are part of the P-type ATPase family and play a crucial role in detoxifying cells by removing arsenite (AsIII) ions, which are highly toxic even at low concentrations.

These enzymes consist of two main domains: a cytoplasmic domain responsible for ATP binding and hydrolysis, and a transmembrane domain that contains the ion transport pathway. The transport process involves several conformational changes in the protein structure, driven by ATP hydrolysis, which ultimately result in the movement of arsenite ions against their concentration gradient from the cytoplasm to the extracellular space or into organelles like vacuoles and endosomes.

In humans, there are two main isoforms of arsenite transporting ATPases: ACR3 (also known as ARS-A) and ACR2 (or ARS-B). Both isoforms have been identified in various tissues, including the liver, kidney, and intestine. Mutations in these genes can lead to impaired arsenic detoxification and increased susceptibility to arsenic toxicity.

Overall, arsenite transporting ATPases are essential for maintaining cellular homeostasis and protecting organisms from the harmful effects of environmental arsenic exposure.

Arsenic is a naturally occurring semi-metal element that can be found in the earth's crust. It has the symbol "As" and atomic number 33 on the periodic table. Arsenic can exist in several forms, including inorganic and organic compounds. In its pure form, arsenic is a steel-gray, shiny solid that is brittle and easily pulverized.

Arsenic is well known for its toxicity to living organisms, including humans. Exposure to high levels of arsenic can cause various health problems, such as skin lesions, neurological damage, and an increased risk of cancer. Arsenic can enter the body through contaminated food, water, or air, and it can also be absorbed through the skin.

In medicine, arsenic has been used historically in the treatment of various diseases, including syphilis and parasitic infections. However, its use as a therapeutic agent is limited due to its toxicity. Today, arsenic trioxide is still used as a chemotherapeutic agent for the treatment of acute promyelocytic leukemia (APL), a type of blood cancer. The drug works by inducing differentiation and apoptosis (programmed cell death) in APL cells, which contain a specific genetic abnormality. However, its use is closely monitored due to the potential for severe side effects and toxicity.

Arsenites are inorganic compounds that contain arsenic in the trivalent state (arsenic-III). They are formed by the reaction of arsenic trioxide (As2O3) or other trivalent arsenic compounds with bases such as sodium hydroxide, potassium hydroxide, or ammonia.

The most common and well-known arsenite is sodium arsenite (NaAsO2), which has been used in the past as a wood preservative and pesticide. However, due to its high toxicity and carcinogenicity, its use has been largely discontinued. Other examples of arsenites include potassium arsenite (KAsO2) and calcium arsenite (Ca3(AsO3)2).

Arsenites are highly toxic and can cause a range of health effects, including skin irritation, nausea, vomiting, diarrhea, abdominal pain, and death in severe cases. Long-term exposure to arsenites has been linked to an increased risk of cancer, particularly lung, bladder, and skin cancer.

I apologize for any confusion, but "Pteris" is not a medical term. It is the name of a genus of ferns, commonly known as brake ferns or table ferns. If you have any questions about a medical term or concept, please provide it, and I would be happy to help define it for you.

Phosphates, in a medical context, refer to the salts or esters of phosphoric acid. Phosphates play crucial roles in various biological processes within the human body. They are essential components of bones and teeth, where they combine with calcium to form hydroxyapatite crystals. Phosphates also participate in energy transfer reactions as phosphate groups attached to adenosine diphosphate (ADP) and adenosine triphosphate (ATP). Additionally, they contribute to buffer systems that help maintain normal pH levels in the body.

Abnormal levels of phosphates in the blood can indicate certain medical conditions. High phosphate levels (hyperphosphatemia) may be associated with kidney dysfunction, hyperparathyroidism, or excessive intake of phosphate-containing products. Low phosphate levels (hypophosphatemia) might result from malnutrition, vitamin D deficiency, or certain diseases affecting the small intestine or kidneys. Both hypophosphatemia and hyperphosphatemia can have significant impacts on various organ systems and may require medical intervention.

Arsenicals are a group of chemicals that contain arsenic, a naturally occurring element that is toxic to humans and animals. Arsenic can combine with other elements such as chlorine, sulfur, or carbon to form various inorganic and organic compounds known as arsenicals. These compounds have been used in a variety of industrial and agricultural applications, including wood preservatives, pesticides, and herbicides.

Exposure to high levels of arsenic can cause serious health effects, including skin damage, circulatory problems, and increased risk of cancer. Long-term exposure to lower levels of arsenic can also lead to chronic health issues, such as neurological damage and diabetes. Therefore, the use of arsenicals is regulated in many countries to minimize human and environmental exposure.

Cacodylic acid is an organic compound with the formula (CH3)2AsO2. It is the simplest dialkyl arsenic acid and is classified as a toxic organoarsenic compound. Cacodylic acid was once used in various medical applications, but its use has been largely discontinued due to its high toxicity and environmental concerns.

It's important to note that cacodylic acid is not commonly encountered in modern medicine or clinical practice. Its historical medical uses included as a treatment for some parasitic infections, but it has since been replaced by safer and more effective alternatives. Nowadays, cacodylic acid is primarily used in research and industrial settings, where it serves as a precursor for the synthesis of other organoarsenic compounds.

Antimony is a toxic metallic element with the symbol Sb and atomic number 51. It exists in several allotropic forms and can be found naturally as the mineral stibnite. Antimony has been used for centuries in various applications, including medicinal ones, although its use in medicine has largely fallen out of favor due to its toxicity.

In a medical context, antimony may still be encountered in certain medications used to treat parasitic infections, such as pentavalent antimony compounds (e.g., sodium stibogluconate and meglumine antimoniate) for the treatment of leishmaniasis. However, these drugs can have significant side effects and their use is typically reserved for severe cases that cannot be treated with other medications.

It's important to note that exposure to antimony in high concentrations or over prolonged periods can lead to serious health issues, including respiratory problems, skin irritation, gastrointestinal symptoms, and even neurological damage. Therefore, handling antimony-containing substances should be done with caution and appropriate safety measures.

Halomonadaceae is a family of halophilic (salt-loving) bacteria within the order Oceanospirillales. These bacteria are commonly found in saline environments such as salt lakes, marine solar salterns, and salted foods. They have the ability to grow in media with a wide range of salinities, from around 0.5% to saturated salt concentrations. Some members of this family can also tolerate or even require the presence of organic solvents. The type genus of Halomonadaceae is Halomonas.

Multienzyme complexes are specialized protein structures that consist of multiple enzymes closely associated or bound together, often with other cofactors and regulatory subunits. These complexes facilitate the sequential transfer of substrates along a series of enzymatic reactions, also known as a metabolic pathway. By keeping the enzymes in close proximity, multienzyme complexes enhance reaction efficiency, improve substrate specificity, and maintain proper stoichiometry between different enzymes involved in the pathway. Examples of multienzyme complexes include the pyruvate dehydrogenase complex, the citrate synthase complex, and the fatty acid synthetase complex.

Shewanella is a genus of gram-negative, facultatively anaerobic bacteria that are widely distributed in various environments such as aquatic habitats, sediments, and occasionally in association with animals or humans. The bacteria are known for their ability to reduce a variety of substances, including metals, which can have implications in bioremediation and corrosion processes. Some species of Shewanella have been associated with human infections, typically occurring in individuals with underlying health conditions or compromised immune systems. However, these cases are relatively rare.

A Crambe plant, also known as Crambe abyssinica, is a species of plant in the mustard family (Brassicaceae). It is native to the Mediterranean region and parts of Africa. The plant can grow up to several feet tall and has large, lobed leaves and clusters of small white flowers.

Crambe plants are not commonly used in medical contexts, but they do have some potential uses in the field of medicine. For example, the seeds of the plant contain a high level of erucic acid, which has been studied for its potential to lower cholesterol levels and improve heart health. However, more research is needed to confirm these potential benefits and to determine the safety and effectiveness of using crambe seeds or extracts as a medical treatment.

It's important to note that crambe plants and their seeds should not be consumed without first consulting a healthcare professional, as they can have toxic effects if not prepared properly.

Aquaglyceroporins are a subfamily of aquaporin water channels that also transport glycerol and other small solutes across biological membranes. They play important roles in various physiological processes, including osmoregulation, skin hydration, and fat metabolism. In humans, there are three known aquaglyceroporins: AQP3, AQP7, and AQP9.

Arsenic poisoning is a condition that occurs when a person ingests or comes into contact with a toxic amount of arsenic, a naturally occurring element found in the earth's crust. Arsenic has no smell or taste, making it difficult to detect in food, water, or air.

Acute arsenic poisoning can occur after a single large exposure to arsenic, while chronic arsenic poisoning occurs after repeated or long-term exposure to lower levels of arsenic. The symptoms of acute arsenic poisoning include vomiting, diarrhea, abdominal pain, and muscle cramps. In severe cases, it can lead to death due to heart failure or respiratory failure.

Chronic arsenic poisoning can cause a range of health problems, including skin changes such as pigmentation and hard patches on the palms and soles, weakness, peripheral neuropathy, and an increased risk of cancer, particularly skin, lung, bladder, and kidney cancer. It can also affect cognitive development in children.

Arsenic poisoning is treated by removing the source of exposure and providing supportive care to manage symptoms. Chelation therapy may be used to remove arsenic from the body in cases of severe acute poisoning or chronic poisoning with high levels of arsenic. Prevention measures include monitoring and reducing exposure to arsenic in food, water, and air, as well as proper handling and disposal of arsenic-containing products.

'Comamonas' is a genus of gram-negative, aerobic, motile bacteria that are commonly found in various environments such as soil, water, and clinical specimens. The cells are typically rod-shaped and may be straight or curved. Comamonas species are capable of utilizing a wide range of organic compounds as carbon and energy sources. Some species have been associated with human infections, although they are generally considered to be of low pathogenicity.

It's worth noting that while some strains of Comamonas have been found to cause infections in humans, they are relatively rare and often occur in individuals with compromised immune systems or underlying medical conditions. Further research is needed to fully understand the role of Comamonas species in human health and disease.

Antimony potassium tartrate is an inorganic compound with the chemical formula KSbC4H4O7. It is a white crystalline solid that is soluble in water and has been used historically in medical treatments, most notably in the treatment of leishmaniasis, a parasitic disease. However, due to its potential toxicity and the availability of safer alternatives, it is no longer commonly used in modern medicine.

'Desulfovibrio desulfuricans' is a species of gram-negative, sulfate-reducing bacteria that is commonly found in aquatic environments, sediments, and the gastrointestinal tracts of animals. These bacteria are capable of reducing sulfates to sulfides, which can be toxic to other organisms and contribute to the corrosion of metals. They are also able to use a variety of organic compounds as electron donors, making them important players in the carbon and sulfur cycles in nature.

The medical relevance of 'Desulfovibrio desulfuricans' is limited, but there have been some reports of infections associated with these bacteria, particularly in individuals with compromised immune systems or underlying medical conditions. For example, they have been implicated in cases of bacteremia (bacteria in the blood), endocarditis (inflammation of the heart valves), and wound infections. However, such infections are rare and not well-studied.

It is worth noting that while 'Desulfovibrio desulfuricans' has been associated with some human diseases, it is generally considered to be a commensal organism in the gut microbiome of healthy individuals. Further research is needed to better understand the role of these bacteria in health and disease.

Phosphate transport proteins are membrane-bound proteins responsible for the active transport of phosphate ions across cell membranes. They play a crucial role in maintaining appropriate phosphate concentrations within cells and between intracellular compartments, which is essential for various biological processes such as energy metabolism, signal transduction, and bone formation.

These proteins utilize the energy derived from ATP hydrolysis or other sources to move phosphate ions against their concentration gradient, thereby facilitating cellular uptake of phosphate even when extracellular concentrations are low. Phosphate transport proteins can be classified based on their structure, function, and localization into different types, including sodium-dependent and sodium-independent transporters, secondary active transporters, and channels.

Dysregulation of phosphate transport proteins has been implicated in several pathological conditions, such as renal Fanconi syndrome, tumoral calcinosis, and hypophosphatemic rickets. Therefore, understanding the molecular mechanisms underlying phosphate transport protein function is essential for developing targeted therapies to treat these disorders.

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