Heme Oxygenase (Decyclizing)
Leukemia, Erythroblastic, Acute
delta-Aminolevulinate synthetases in the liver cytosol fraction and mitochondria of mice treated with allylisopropylacetamide and 3,5-dicarbethoxyl-1,4-dihydrocollidine. (1/964)Hepatic delta-aminolevulinate (ALA) synthetase was induced in mice by the administration of allylisopropylacetamide (AIA) and 3,5-dicarbethoxy-1,4-dihydrocollidine (DDC). In both cases, a significant amount of ALA synthetase accumulated in the liver cytosol fraction as well as in the mitochondria. The apparent molecular weight of the cytosol ALA synthetase was estimated to be 320,000 by gel filtration, but when the cytosol ALA synthetase was subjected to sucrose density gradient centrifugation, it showed a molecular weight of 110,000. In the mitochondria, there were two different sizes of ALA synthetase with molecular weights of 150,000 and 110,000, respectively; the larger enzyme was predominant in DDC-treated mice, whereas in AIA-treated mice and normal mice the enzyme existed mostly in the smaller form. When hemin was injected into mice pretreated with DDC, the molecular size of the mitochondrial ALA synthetase changed from 150,000 to 110,000. The half-life of ALA synthetase in the liver cytosol fraction was about 30 min in both the AIA-treated and DDC-treated mice. The half-life of the mitochondrial ALA synthetase in AIA-treated mice and normal mice was about 60 min, but in DDC-treated mice the half-life was as long as 150 min. The data suggest that the cytosol ALA synthetase of mouse liver is a protein complex with properties very similar to those of the cytosol ALA synthetase of rat liver, which has been shown to be composed of the enzyme active protein and two catalytically inactive binding proteins, and that ALA synthetase may be transferred from the liver cytosol fraction to the mitochondria with a size of about 150,000 daltons, followed by its conversion to enzyme with a molecular weight of 110,000 within the mitochondria. The process of intramitochondrial enzyme degradation seems to be affected in DDC-treated animals. (+info)
8-Aminoquinolines active against blood stage Plasmodium falciparum in vitro inhibit hematin polymerization. (2/964)From the Walter Reed Army Institute of Research (WRAIR) inventory, thirteen 8-aminoquinoline analogs of primaquine were selected for screening against a panel of seven Plasmodium falciparum clones and isolates. Six of the 13 8-aminoquinolines had average 50% inhibitory concentrations between 50 and 100 nM against these P. falciparum clones and were thus an order of magnitude more potent than primaquine. However, excluding chloroquine-resistant clones and isolates, these 8-aminoquinolines were all an order of magnitude less potent than chloroquine. None of the 8-aminoquinolines was cross resistant with either chloroquine or mefloquine. In contrast to the inactive primaquine prototype, 8 of the 13 8-aminoquinolines inhibited hematin polymerization more efficiently than did chloroquine. Although alkoxy or aryloxy substituents at position 5 uniquely endowed these 13 8-aminoquinolines with impressive schizontocidal activity, the structural specificity of inhibition of both parasite growth and hematin polymerization was low. (+info)
Identification of quinone-binding and heme-ligating residues of the smallest membrane-anchoring subunit (QPs3) of bovine heart mitochondrial succinate:ubiquinone reductase. (3/964)The smallest membrane-anchoring subunit (QPs3) of bovine heart succinate:ubiquinone reductase was overexpressed in Escherichia coli JM109 as a glutathione S-transferase fusion protein using the expression vector pGEX2T/QPs3. The yield of soluble active recombinant glutathione S-transferase-QPs3 fusion protein was isopropyl-1-thio-beta-D-galactopyranoside concentration-, induction growth time-, temperature-, and medium-dependent. Maximum yield of soluble recombinant fusion protein was obtained from cells harvested 3.5 h post-isopropyl-1-thio-beta-D-galactopyranoside (0.4 mM)-induction growth at 25 degrees C in 2.0% tryptone, 0.5% yeast extract, 10 mM NaCl, 2.5 mM KCl, 10 mM MgCl2, 20 mM glucose (SOC medium) containing 440 mM sorbitol and 2.5 mM betaine. QPs3 was released from the fusion protein by proteolytic cleavage with thrombin. Isolated recombinant QPs3 shows one protein band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis that corresponds to subunit V of mitochondrial succinate:ubiquinone reductase. Although purified recombinant QPs3 is dispersed in 0.01% dodecylmaltoside, it is in a highly aggregated form, with an apparent molecular mass of more than 1 million. The recombinant QPs3 binds ubiquinone, causing a spectral blue shift. Upon titration of the recombinant protein with ubiquinone, a saturation behavior is observed, suggesting that the binding is specific and that recombinant QPs3 may be in the functionally active state. Two amino acid residues, serine 33 and tyrosine 37, in the putative ubiquinone binding domain of QPs3 are involved in ubiquinone binding because the S33A- or Y37A-substituted recombinant QPs3s do not cause the spectral blue shift of ubiquinone. Although recombinant QPs3 contains little cytochrome b560 heme, the spectral characteristics of cytochrome b560 are reconstituted upon addition of hemin chloride. Reconstituted cytochrome b560 in recombinant QPs3 shows a EPR signal at g = 2.92. Histidine residues at positions 46 and 60 are responsible for heme ligation because the H46N- or H60N-substituted QPs3 fail to restore cytochrome b560 upon addition of hemin chloride. (+info)
Urate synthesis in the blood-sucking insect rhodnius prolixus. Stimulation by hemin is mediated by protein kinase C. (4/964)Hemin is a catalyst of the formation of reactive oxygen species. We proposed that hematophagous insects are exposed to intense oxidative stress because of hemoglobin hydrolysis in their midgut (Petretsky, M. D., Ribeiro, J. M. C., Atella, G. C., Masuda, H., and Oliveira, P. L. (1995) J. Biol. Chem. 270, 10893-10896). We have shown that hemin stimulates urate synthesis in the blood-sucking insect Rhodnius prolixus (Graca-Souza, A. V., Petretsky, J. H., Demasi, M., Bechara, E. J. H., and Oliveira, P. L. (1997) Free Radical Biol. Med. 22, 209-214). Once released by fat body cells, urate accumulates in the hemolymph, where this radical scavenger constitutes an important defense against blood-feeding derived oxidative stress. Incubation of Rhodnius fat bodies with okadaic acid raises the level of urate synthesis, suggesting that urate production can be controlled by protein phosphorylation/dephosphorylation. Urate synthesis is stimulated by dibutyryl cAMP and inhibited by N(2((p-bromocinnamil)amino)ethyl)-5-isoquinolinesulfonamide (H-89), an inhibitor of protein kinase A, as well as activated by the protein kinase C activator phorbol 12-myristate 13-acetate. In the presence of hemin, however, inhibition of urate synthesis by H-89 does not occur, suggesting that the hemin stimulatory effect is not mediated by protein kinase A. Calphostin C completely inhibits the hemin-induced urate production, suggesting that the triggering of urate antioxidant response depends on protein kinase C activation. This conclusion is reinforced by the observation that in fat bodies exposed to hemin, both protein kinase C activity and phosphorylation of specific endogenous polypeptides are significantly increased. (+info)
Phosphatidylserine externalization during differentiation-triggered apoptosis of erythroleukemic cells. (5/964)K562 erythroleukemia cells undergo apoptosis when induced to differentiate along the erythroid lineage with hemin. This event, characterized by DNA fragmentation, correlated with downregulation of the survival protein, BCL-xL, and decrease in mitochondrial transmembrane potential (deltapsi[m]) that ultimately resulted in cell death. Reorientation of phosphatidylserine (PS) from the cells inner-to-outer plasma membrane leaflet and inhibition of the aminophospholipid translocase was observed upon hemin-treatment. Constitutive expression of BCL-2 did not inhibit hemin-induced alterations in lipid asymmetry or decrease in deltapsi[m], and only moderately prevented DNA fragmentation. BCL-2, on the other hand, effectively inhibited actinomycin D-induced DNA fragmentation, the appearance of PS at the cells outer leaflet and the decrease in deltapsi[m]. The caspase inhibitor, z.VAD.fmk, blocked DNA fragmentation by both hemin and actinomycin D, but inhibited PS externalization only in the actinomycin D-treated cells. These results suggest that, unlike pharmacologically-induced apoptosis, PS externalization triggered by differentiation-induced apoptosis occurs by a mechanism that is associated with a decrease in deltapsi[m], but independent of BCL-2 and caspases. (+info)
The haemin storage (Hms+) phenotype of Yersinia pestis is not essential for the pathogenesis of bubonic plague in mammals. (6/964)The haemin storage (Hms+) phenotype of Yersinia pestis enables this bacillus to form greenish/brown or red colonies on haemin or Congo Red agar plates, respectively, at 26 but not 37 degrees C. Escherichia coli strains that contain mutations in genes essential for siderophore biosynthesis, porphyrin generation and/or haemin transport remain unable to utilize exogenous haemin as a nutritional iron or porphyrin source when transformed with the cloned Y. pestis hmsHFRS locus. Further physiological analysis of the Hms+ phenotype of Y. pestis strain KIM6+ suggests that the haemin and inorganic iron stored by the Hms system was not used nutritionally under subsequent iron-deficient conditions. In vitro analysis of the bactericidal effects of hydrogen peroxide, superoxide and nitric oxide showed that Hms- Y. pestis cells, in certain cases, were more susceptible than the Hms+ parent cells to these reactive oxygen species at 26 and/or 37 degrees C. In adherence assays, a higher percentage of Hms+ cells were associated with HeLa cells and normal human neutrophils, compared to Hms- cells. However, the Hms+ phenotype did not provide any additional protection against the killing effects of neutrophils. Finally, LD50 analysis in subcutaneously infected mice showed that an Hms- strain was slightly more virulent than Hms+, indicating that the Hms phenotype is not essential for the pathogenesis of bubonic plague in mammals. (+info)
Cellular uptake of chloroquine is dependent on binding to ferriprotoporphyrin IX and is independent of NHE activity in Plasmodium falciparum. (7/964)Here we provide definitive evidence that chloroquine (CQ) uptake in Plasmodium falciparum is determined by binding to ferriprotoporphyrin IX (FPIX). Specific proteinase inhibitors that block the degradation of hemoglobin and stop the generation of FPIX also inhibit CQ uptake. Food vacuole enzymes can generate cell-free binding, using human hemoglobin as a substrate. This binding accounts for CQ uptake into intact cells and is subject to identical inhibitor specificity. Inhibition of CQ uptake by amiloride derivatives occurs because of inhibition of CQ-FPIX binding rather than inhibition of the Na+/H+ exchanger (NHE). Inhibition of parasite NHE using a sodium-free medium does not inhibit CQ uptake nor does it alter the ability of amilorides to inhibit uptake. CQ resistance is characterized by a reduced affinity of CQ-FPIX binding that is reversible by verapamil. Diverse compounds that are known to disrupt lysosomal pH can mimic the verapamil effect. These effects are seen in sodium-free medium and are not due to stimulation of the NHE. We propose that these compounds increase CQ accumulation and overcome CQ resistance by increasing the pH of lysosomes and endosomes, thereby causing an increased affinity of binding of CQ to FPIX. (+info)
Peroxynitrite induces haem oxygenase-1 in vascular endothelial cells: a link to apoptosis. (8/964)Peroxynitrite (ONOO-) is a potent oxidizing agent generated by the interaction of nitric oxide (NO) and the superoxide anion. In physiological solution, ONOO- rapidly decomposes to a hydroxyl radical, one of the most reactive free radicals, and nitrogen dioxide, another species able to cause oxidative damage. In the present study we investigated the effect of ONOO- on the expression of haem oxygenase-1 (HO-1), an inducible protein that is highly up-regulated by oxidative stress. Exposure of bovine aortic endothelial cells to ONOO- (250-1000 microM) produced a concentration-dependent increase in haem oxygenase activity and HO-1 protein expression. This effect was completely abolished by the ONOO- scavengers uric acid and N-acetylcysteine, and partly attenuated by 1,3-dimethyl-2-thiourea, a scavenger of hydroxyl radicals. ONOO- also produced a concentration-dependent increase in apoptosis and cytotoxicity, which were considerably decreased by uric acid and N-acetylcysteine. A 70% decrease in apoptosis was observed when cells were exposed to ONOO- in the presence of 10 microM tin protoporphyrin IX (SnPPIX), an inhibitor of haem oxygenase activity. When SnPPIX was added 5 min after ONOO-, apoptosis decreased by only 40%, which suggests that an interaction between ONOO- and the protoporphyrin occurs in our system. Increased haem oxygenase activity by pretreatment of cells with haemin resulted in elevated bilirubin production and was associated with a substantial decrease (35%) in ONOO--mediated apoptosis. These results indicate the ability of ONOO- to modulate the expression of the stress protein HO-1 and suggest that the haem oxygenase pathway contributes to protection against the cytotoxic action of ONOO-. (+info)
Hemin is a naturally occurring iron-containing porphyrin compound that is found in red blood cells. It is the primary component of hemoglobin, the protein responsible for carrying oxygen from the lungs to the body's tissues and carbon dioxide from the tissues back to the lungs. In the medical field, hemin is used as a medication to treat a rare genetic disorder called porphyria, which is characterized by the accumulation of toxic byproducts of heme metabolism in the body. Hemin is also used in the treatment of certain types of anemia, such as acute intermittent porphyria, and as a supplement to increase iron levels in people with iron deficiency anemia. Hemin has also been studied for its potential therapeutic effects in other conditions, such as cancer, neurodegenerative diseases, and infectious diseases. However, more research is needed to fully understand its potential uses and side effects.
Heme is a complex organic molecule that contains iron and is a vital component of hemoglobin, myoglobin, and other proteins involved in oxygen transport and storage in living organisms. It is also a component of various enzymes involved in metabolism and detoxification processes. In the medical field, heme is often used as a diagnostic tool to detect and monitor certain medical conditions, such as anemia (a deficiency of red blood cells or hemoglobin), liver disease (which can affect heme synthesis), and certain types of cancer (which can produce abnormal heme molecules). Heme is also used in the production of certain medications, such as heme-based oxygen carriers for use in patients with sickle cell disease or other conditions that affect oxygen transport. Additionally, heme is a component of some dietary supplements and is sometimes used to treat certain types of anemia.
Protoporphyrins are a group of pigments that are synthesized in the body as part of the heme biosynthesis pathway. Heme is a vital component of hemoglobin, which is responsible for carrying oxygen in red blood cells. Protoporphyrins are also found in other proteins, such as cytochromes, which are involved in cellular respiration. In the medical field, protoporphyrins are often measured in blood tests as a marker of iron metabolism. Elevated levels of protoporphyrins can indicate a deficiency in iron or other nutrients involved in heme synthesis, such as vitamin B12 or folate. On the other hand, low levels of protoporphyrins can be a sign of excessive iron stores or other medical conditions, such as liver disease or kidney failure. Protoporphyrins are also used as a diagnostic tool in the detection of certain types of cancer, such as bladder cancer and lung cancer. In these cases, elevated levels of protoporphyrins in the urine or blood can indicate the presence of cancer cells. Additionally, protoporphyrins have been studied as potential therapeutic agents for various diseases, including cancer, anemia, and neurological disorders.
Heme Oxygenase-1 (HO-1) is an enzyme that plays a crucial role in the metabolism of heme, a component of hemoglobin found in red blood cells. HO-1 is induced in response to various stressors, including inflammation, oxidative stress, and exposure to toxins. The primary function of HO-1 is to break down heme into biliverdin, carbon monoxide (CO), and iron (Fe). Biliverdin is then converted into bilirubin, which is excreted from the body. CO has several biological effects, including vasodilation and anti-inflammatory properties. Fe is recycled and used for the synthesis of new heme. HO-1 has been shown to have a number of beneficial effects in the body, including protection against oxidative stress, inflammation, and tissue damage. It has been implicated in the prevention and treatment of a variety of diseases, including cardiovascular disease, neurodegenerative disorders, and cancer. In the medical field, HO-1 is often studied as a potential therapeutic target for the treatment of various diseases. For example, drugs that induce HO-1 activity have been shown to have anti-inflammatory and anti-cancer effects in preclinical studies. However, more research is needed to fully understand the role of HO-1 in disease and to develop effective therapies that target this enzyme.
Hemeproteins are a class of proteins that contain a heme group, which is a complex of iron and porphyrin. Hemeproteins are found in many organisms and play important roles in a variety of biological processes, including oxygen transport, energy metabolism, and detoxification. The most well-known hemeprotein is hemoglobin, which is found in red blood cells and is responsible for carrying oxygen from the lungs to the body's tissues. Hemoglobin is composed of four subunits, each of which contains a heme group. The iron atom in the heme group can bind to oxygen molecules, allowing hemoglobin to transport oxygen throughout the body. Other examples of hemeproteins include myoglobin, which is found in muscle tissue and stores oxygen for use during periods of high physical activity, and cytochrome P450 enzymes, which are involved in the metabolism of drugs and other xenobiotics. Hemeproteins are important for many biological processes and are the subject of ongoing research in the medical field.
In the medical field, "heptanoates" refers to a group of compounds that contain a heptanoic acid functional group. Heptanoic acid is a seven-carbon carboxylic acid, and its derivatives are known as heptanoates. Heptanoates are commonly used in the production of pharmaceuticals, cosmetics, and personal care products. They can also be used as intermediates in the synthesis of other compounds. In some cases, heptanoates may be used as a source of energy for the body. For example, heptanoic acid is a component of medium-chain triglycerides (MCTs), which are a type of dietary fat that can be easily metabolized by the body for energy. It is worth noting that the use of heptanoates in medicine and other fields is typically limited to specific applications and may require careful consideration of potential risks and side effects.
In the medical field, "iron" refers to a mineral that is essential for the production of red blood cells, which carry oxygen throughout the body. Iron is also important for the proper functioning of the immune system, metabolism, and energy production. Iron deficiency is a common condition that can lead to anemia, a condition in which the body does not have enough red blood cells to carry oxygen to the body's tissues. Symptoms of iron deficiency anemia may include fatigue, weakness, shortness of breath, and pale skin. Iron supplements are often prescribed to treat iron deficiency anemia, and dietary changes may also be recommended to increase iron intake. However, it is important to note that excessive iron intake can also be harmful, so it is important to follow the recommended dosage and consult with a healthcare provider before taking any iron supplements.
Hemoglobins are a group of proteins found in red blood cells (erythrocytes) that are responsible for carrying oxygen from the lungs to the body's tissues and carbon dioxide from the tissues back to the lungs. Hemoglobin is composed of four subunits, each of which contains a heme group that binds to oxygen. The oxygen binds to the iron atom in the heme group, allowing the hemoglobin to transport oxygen throughout the body. Hemoglobin also plays a role in regulating the pH of the blood and in the immune response. Abnormalities in hemoglobin can lead to various medical conditions, such as anemia, sickle cell disease, and thalassemia.
Porphyrins are a group of organic compounds that are essential for the production of hemoglobin, a protein found in red blood cells that carries oxygen throughout the body. Porphyrins are also involved in the metabolism of other substances, such as bile pigments and vitamin B12. In the medical field, porphyrins are often used as diagnostic tools for certain diseases. For example, elevated levels of porphyrins in the blood or urine can be a sign of liver disease, kidney disease, or anemia. Porphyrins can also accumulate in the skin and other tissues in conditions such as porphyria, a group of rare genetic disorders that affect the metabolism of porphyrins. In addition, porphyrins have been studied for their potential therapeutic applications. Some porphyrins have been shown to have anti-cancer properties, while others have been used to treat certain types of infections and to deliver drugs to specific cells in the body.
Congo Red is a dye that is commonly used in the medical field to stain certain types of tissue samples, particularly those containing amyloid proteins. Amyloid proteins are abnormal proteins that can accumulate in tissues and cause a variety of diseases, including Alzheimer's disease, Parkinson's disease, and amyloidosis. When Congo Red is applied to a tissue sample containing amyloid proteins, it binds to the proteins and causes them to appear bright red under a microscope. This makes it easier for doctors and researchers to identify and study the amyloid proteins, which can help them better understand the underlying causes of the disease and develop new treatments. Congo Red is also used to stain other types of tissue samples, such as those containing collagen fibers or certain types of bacteria. However, its primary use in the medical field is to stain amyloid proteins.
Acute Erythroblastic Leukemia (AEL) is a rare type of acute myeloid leukemia (AML) that is characterized by the overproduction of immature red blood cells (erythroblasts) in the bone marrow. This leads to a decrease in the production of mature red blood cells, which can cause anemia, fatigue, weakness, and shortness of breath. AEL is typically diagnosed in adults and is more common in males than females. The symptoms of AEL can be similar to those of other types of AML, so a bone marrow biopsy is usually performed to confirm the diagnosis. Treatment for AEL typically involves chemotherapy and/or radiation therapy to kill the cancer cells and restore normal blood cell production. In some cases, a stem cell transplant may also be recommended. The prognosis for AEL depends on various factors, including the patient's age, overall health, and the specific type and stage of the disease.
5-Aminolevulinate synthetase is an enzyme that plays a crucial role in the biosynthesis of heme, a pigment found in red blood cells and other cells throughout the body. This enzyme catalyzes the conversion of glycine and succinyl-CoA to 5-aminolevulinic acid (ALA), which is the first and rate-limiting step in the heme biosynthetic pathway. In the medical field, 5-aminolevulinate synthetase is of particular interest because it is involved in the production of porphyrins, a group of pigments that are the building blocks of heme. Porphyrin metabolism disorders, such as porphyria, can result from mutations in the gene encoding 5-aminolevulinate synthetase or other enzymes in the heme biosynthetic pathway. These disorders can cause a range of symptoms, including abdominal pain, neurological problems, and skin sensitivity to light. In addition to its role in heme biosynthesis, 5-aminolevulinate synthetase has also been studied for its potential use in cancer therapy. ALA is a precursor to porphyrins, which can be converted to photodynamic therapy agents that can selectively kill cancer cells when exposed to light. This approach, known as photodynamic therapy, is being investigated as a treatment for various types of cancer, including skin cancer, lung cancer, and head and neck cancer.
Metalloporphyrins are a class of compounds that consist of a porphyrin ring with a metal ion (such as iron, cobalt, or manganese) at its center. They are often used in the medical field as a diagnostic tool for certain diseases, such as anemia, and as a treatment for others, such as certain types of cancer. Metalloporphyrins are also being studied for their potential use in the development of new drugs and therapies.
Globins are a family of proteins that are found in red blood cells and are responsible for carrying oxygen throughout the body. There are several different types of globins, including hemoglobin, myoglobin, and cytoglobin. Hemoglobin is the most well-known globin and is responsible for binding to oxygen in the lungs and transporting it to the body's tissues. Myoglobin is found in muscle tissue and is responsible for storing oxygen for use during periods of high physical activity. Cytoglobin is found in the cytoplasm of cells and is thought to play a role in the regulation of cellular respiration. Abnormalities in globin levels or function can lead to a variety of medical conditions, including anemia, sickle cell disease, and thalassemia.
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- Hemin (plasma-derived intravenous heme) is the definitive treatment and mainstay of management. (medscape.com)
- Reconstitute it with human serum albumin 25% (132 mL of 25% human serum albumin to 1 vial of hemin [301 mg heme]) and infuse it into large vein to reduce the risk of thrombophlebitis. (medscape.com)
- Role of the Yersinia pestis hemin storage (hms) locus in the transmission of plague by fleas. (medscape.com)
- In agreement with the minimal reorganization between the apo-and holo-structures, the hemin on-rate is too fast to detect by conventional stopped-flow measurements. (ku.edu)
- It was previously known as hematin, a term used to describe the chemical reaction product of hemin and sodium carbonate solution. (medscape.com)
- Here, we performed volumetric analyses of formation of the complex between an oligonucleotide with the sequence of human telomeric DNA (h-telo) and hemin . (bvsalud.org)
- Interestingly, the pressure effect on the destabilization of the h-telo- hemin complex in the presence of poly( ethylene glycol )200 (PEG200) was repressed compared to that in the absence of PEG200. (bvsalud.org)
- PANHEMATIN is a hemin for injection indicated for amelioration of recurrent attacks of acute intermittent porphyria temporally related to the menstrual cycle in susceptible women, after initial carbohydrate therapy is known or suspected to be inadequate. (nih.gov)
- Injectable hemin (Panhematin) is now approved by the FDA for women with catamenial patterns of exacerbation. (medscape.com)
- Zhang Hemin, who is head of the breeding facility, says Xiang Xiang's habitat training began in a five-acre (two-hectare) open enclosure. (nationalgeographic.com)
- The roads leading to the base from Ya'an are inaccessible because of the quake," said Zhang Hemin, chief of the administrative bureau of Wolong. (chinadaily.com.cn)
- Hemin Chin, Ph.D. (nih.gov)
- A total of 372 patients were treated with hemin for acute attacks of porphyria in the studies. (hpfb-dgpsa.ca)
- After acute attacks are aborted, the hemin can be administered again, either weekly or monthly in the more refractory individuals, when pain complaints initiate a recurring attack. (medscape.com)
- Two medical therapies are effective in aborting porphyric attacks: IV 10% dextrose in water (D10W) and IV hemin (ie, hematin). (medscape.com)
- Staphylococcus aureus menadione and hemin auxotrophs, generated by in vitro gentamicin selection, demonstrated reduced hemolytic activity and enhanced intracellular survival within cultured bovine aortic endothelial cells relative to their hemolytic parent. (nih.gov)
- H. influenzae , a fastidious, pleomorphic, gram-negative coccobacillus, requires hemin (X factor) and nicotinamide-adenine-dinucleotide (NAD, also known as V factor) for in vitro growth. (cdc.gov)
- If therapeutic control lost, the patient is switched to IV hemin. (medscape.com)
- Supplementation of the auxotrophs with exogenous menadione or hemin resulted in rapid growth, increased hemolytic activity, and reduced intracellular persistence to the level found for the hemolytic clinical parent. (nih.gov)
- C-14 binding to globin, hemin, and erythrocyte cell debris in the blood and hepatic DNA was determined. (cdc.gov)
- Pharmacodynamic evaluation of the activity of antibiotics against hemin- and menadione-dependent small-colony variants of Staphylococcus aureus in models of extracellular (broth) and intracellular (THP-1 monocytes) infections. (nih.gov)