Hemin: Chloro(7,12-diethenyl-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-dipropanoato(4-)-N(21),N(22),N(23),N(24)) ferrate(2-) dihydrogen.Heme: The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.Protoporphyrins: Porphyrins with four methyl, two vinyl, and two propionic acid side chains attached to the pyrrole rings. Protoporphyrin IX occurs in hemoglobin, myoglobin, and most of the cytochromes.Heme Oxygenase (Decyclizing): A mixed function oxidase enzyme which during hemoglobin catabolism catalyzes the degradation of heme to ferrous iron, carbon monoxide and biliverdin in the presence of molecular oxygen and reduced NADPH. The enzyme is induced by metals, particularly cobalt. EC Oxygenase-1: A ubiquitous stress-responsive enzyme that catalyzes the oxidative cleavage of HEME to yield IRON; CARBON MONOXIDE; and BILIVERDIN.Hemeproteins: Proteins that contain an iron-porphyrin, or heme, prosthetic group resembling that of hemoglobin. (From Lehninger, Principles of Biochemistry, 1982, p480)Heptanoates: Salts and esters of the 7-carbon saturated monocarboxylic acid heptanoic acid.Iron: A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN.Hemoglobins: The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements.Porphyrins: A group of compounds containing the porphin structure, four pyrrole rings connected by methine bridges in a cyclic configuration to which a variety of side chains are attached. The nature of the side chain is indicated by a prefix, as uroporphyrin, hematoporphyrin, etc. The porphyrins, in combination with iron, form the heme component in biologically significant compounds such as hemoglobin and myoglobin.Congo Red: An acid dye used in testing for hydrochloric acid in gastric contents. It is also used histologically to test for AMYLOIDOSIS.Corynebacterium diphtheriae: A species of gram-positive, asporogenous bacteria in which three cultural types are recognized. These types (gravis, intermedius, and mitis) were originally given in accordance with the clinical severity of the cases from which the different strains were most frequently isolated. This species is the causative agent of DIPHTHERIA.Reticulocytes: Immature ERYTHROCYTES. In humans, these are ERYTHROID CELLS that have just undergone extrusion of their CELL NUCLEUS. They still contain some organelles that gradually decrease in number as the cells mature. RIBOSOMES are last to disappear. Certain staining techniques cause components of the ribosomes to precipitate into characteristic "reticulum" (not the same as the ENDOPLASMIC RETICULUM), hence the name reticulocytes.Leukemia, Erythroblastic, Acute: A myeloproliferative disorder characterized by neoplastic proliferation of erythroblastic and myeloblastic elements with atypical erythroblasts and myeloblasts in the peripheral blood.Porphyromonas gingivalis: A species of gram-negative, anaerobic, rod-shaped bacteria originally classified within the BACTEROIDES genus. This bacterium produces a cell-bound, oxygen-sensitive collagenase and is isolated from the human mouth.5-Aminolevulinate Synthetase: An enzyme of the transferase class that catalyzes condensation of the succinyl group from succinyl coenzyme A with glycine to form delta-aminolevulinate. It is a pyridoxyal phosphate protein and the reaction occurs in mitochondria as the first step of the heme biosynthetic pathway. The enzyme is a key regulatory enzyme in heme biosynthesis. In liver feedback is inhibited by heme. EC Porphyrins which are combined with a metal ion. The metal is bound equally to all four nitrogen atoms of the pyrrole rings. They possess characteristic absorption spectra which can be utilized for identification or quantitative estimation of porphyrins and porphyrin-bound compounds.Globins: A superfamily of proteins containing the globin fold which is composed of 6-8 alpha helices arranged in a characterstic HEME enclosing structure.Porphyrias: A diverse group of metabolic diseases characterized by errors in the biosynthetic pathway of HEME in the LIVER, the BONE MARROW, or both. They are classified by the deficiency of specific enzymes, the tissue site of enzyme defect, or the clinical features that include neurological (acute) or cutaneous (skin lesions). Porphyrias can be hereditary or acquired as a result of toxicity to the hepatic or erythropoietic marrow tissues.Menstrual Cycle: The period from onset of one menstrual bleeding (MENSTRUATION) to the next in an ovulating woman or female primate. The menstrual cycle is regulated by endocrine interactions of the HYPOTHALAMUS; the PITUITARY GLAND; the ovaries; and the genital tract. The menstrual cycle is divided by OVULATION into two phases. Based on the endocrine status of the OVARY, there is a FOLLICULAR PHASE and a LUTEAL PHASE. Based on the response in the ENDOMETRIUM, the menstrual cycle is divided into a proliferative and a secretory phase.Porphyria, Acute Intermittent: An autosomal dominant porphyria that is due to a deficiency of HYDROXYMETHYLBILANE SYNTHASE in the LIVER, the third enzyme in the 8-enzyme biosynthetic pathway of HEME. Clinical features are recurrent and life-threatening neurologic disturbances, ABDOMINAL PAIN, and elevated level of AMINOLEVULINIC ACID and PORPHOBILINOGEN in the urine.Porphyrias, Hepatic: A group of metabolic diseases due to deficiency of one of a number of LIVER enzymes in the biosynthetic pathway of HEME. They are characterized by the accumulation and increased excretion of PORPHYRINS or its precursors. Clinical features include neurological symptoms (PORPHYRIA, ACUTE INTERMITTENT), cutaneous lesions due to photosensitivity (PORPHYRIA CUTANEA TARDA), or both (HEREDITARY COPROPORPHYRIA). Hepatic porphyrias can be hereditary or acquired as a result of toxicity to the hepatic tissues.Heart Rate: The number of times the HEART VENTRICLES contract per unit of time, usually per minute.PubMed: A bibliographic database that includes MEDLINE as its primary subset. It is produced by the National Center for Biotechnology Information (NCBI), part of the NATIONAL LIBRARY OF MEDICINE. PubMed, which is searchable through NLM's Web site, also includes access to additional citations to selected life sciences journals not in MEDLINE, and links to other resources such as the full-text of articles at participating publishers' Web sites, NCBI's molecular biology databases, and PubMed Central.Bacteroidaceae Infections: Infections with bacteria of the family BACTEROIDACEAE.Periodicals as Topic: A publication issued at stated, more or less regular, intervals.Bartonella quintana: A species of gram-negative bacteria in which man is the primary host and the human body louse, Pediculus humanus, the principal vector. It is the etiological agent of TRENCH FEVER.Gastroparesis: Chronic delayed gastric emptying. Gastroparesis may be caused by motor dysfunction or paralysis of STOMACH muscles or may be associated with other systemic diseases such as DIABETES MELLITUS.Gastric Emptying: The evacuation of food from the stomach into the duodenum.Diabetes Mellitus, Type 1: A subtype of DIABETES MELLITUS that is characterized by INSULIN deficiency. It is manifested by the sudden onset of severe HYPERGLYCEMIA, rapid progression to DIABETIC KETOACIDOSIS, and DEATH unless treated with insulin. The disease may occur at any age, but is most common in childhood or adolescence.Interstitial Cells of Cajal: c-Kit positive cells related to SMOOTH MUSCLE CELLS that are intercalated between the autonomic nerves and the effector smooth muscle cells of the GASTROINTESTINAL TRACT. Different phenotypic classes play roles as pacemakers, mediators of neural inputs, and mechanosensors.Tin Compounds: Inorganic compounds that contain tin as an integral part of the molecule.Rats, Inbred SHR: A strain of Rattus norvegicus with elevated blood pressure used as a model for studying hypertension and stroke.Hypertension: Persistently high systemic arterial BLOOD PRESSURE. Based on multiple readings (BLOOD PRESSURE DETERMINATION), hypertension is currently defined as when SYSTOLIC PRESSURE is consistently greater than 140 mm Hg or when DIASTOLIC PRESSURE is consistently 90 mm Hg or more.Rats, Inbred WKY: A strain of Rattus norvegicus used as a normotensive control for the spontaneous hypertensive rats (SHR).Blood Pressure: PRESSURE of the BLOOD on the ARTERIES and other BLOOD VESSELS.Tin: A trace element that is required in bone formation. It has the atomic symbol Sn, atomic number 50, and atomic weight 118.71.Mice, Inbred NOD: A strain of non-obese diabetic mice developed in Japan that has been widely studied as a model for T-cell-dependent autoimmune insulin-dependent diabetes mellitus in which insulitis is a major histopathologic feature, and in which genetic susceptibility is strongly MHC-linked.HIV-1: The type species of LENTIVIRUS and the etiologic agent of AIDS. It is characterized by its cytopathic effect and affinity for the T4-lymphocyte.Mice, SCID: Mice homozygous for the mutant autosomal recessive gene "scid" which is located on the centromeric end of chromosome 16. These mice lack mature, functional lymphocytes and are thus highly susceptible to lethal opportunistic infections if not chronically treated with antibiotics. The lack of B- and T-cell immunity resembles severe combined immunodeficiency (SCID) syndrome in human infants. SCID mice are useful as animal models since they are receptive to implantation of a human immune system producing SCID-human (SCID-hu) hematochimeric mice.HIV Infections: Includes the spectrum of human immunodeficiency virus infections that range from asymptomatic seropositivity, thru AIDS-related complex (ARC), to acquired immunodeficiency syndrome (AIDS).Curcumin: A yellow-orange dye obtained from tumeric, the powdered root of CURCUMA longa. It is used in the preparation of curcuma paper and the detection of boron. Curcumin appears to possess a spectrum of pharmacological properties, due primarily to its inhibitory effects on metabolic enzymes.Curcuma: A plant genus of the family ZINGIBERACEAE that contains CURCUMIN and curcuminoids.Buthionine Sulfoximine: A synthetic amino acid that depletes glutathione by irreversibly inhibiting gamma-glutamylcysteine synthetase. Inhibition of this enzyme is a critical step in glutathione biosynthesis. It has been shown to inhibit the proliferative response in human T-lymphocytes and inhibit macrophage activation. (J Biol Chem 1995;270(33):1945-7)Glutathione Disulfide: A GLUTATHIONE dimer formed by a disulfide bond between the cysteine sulfhydryl side chains during the course of being oxidized.Luminescent Measurements: Techniques used for determining the values of photometric parameters of light resulting from LUMINESCENCE.Antibodies, Immobilized: Antibodies that are chemically bound to a substrate material which renders their location fixed.Nanowires: Nanometer-scale wires made of materials that conduct electricity. They can be coated with molecules such as antibodies that will bind to proteins and other substances.Luminol: 5-Amino-2,3-dihydro-1,4-phthalazinedione. Substance that emits light on oxidation. It is used in chemical determinations.Electrochemistry: The study of chemical changes resulting from electrical action and electrical activity resulting from chemical changes.Luminescence: Emission of LIGHT when ELECTRONS return to the electronic ground state from an excited state and lose the energy as PHOTONS. It is sometimes called cool light in contrast to INCANDESCENCE. LUMINESCENT MEASUREMENTS take advantage of this type of light emitted from LUMINESCENT AGENTS.Graphite: An allotropic form of carbon that is used in pencils, as a lubricant, and in matches and explosives. It is obtained by mining and its dust can cause lung irritation.

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)

  • The obtained results open good perspectives to apply FeIII-TAML activator 1a in CL analytical methods instead of hemin, traditionally used peroxidase mimetic. (ac.ru)
  • Bombicini RL, Schmitt TH, Frezzati Junior WA, Schreier S. Effect of hemin upon structure, permeability and peroxidation of membranes. (usp.br)
  • Moreover, 15 μ M curcumin attenuated by 55% the increase in reactive oxygen species (ROS) production, by 94% the reduction of GSH/glutathione disulfide (GSSG) ratio, and by 49% the cell death induced by hemin. (hindawi.com)
  • Herein we describe the oxidation of luminol with hydrogen peroxide catalyzed by commercial available FeIII-TAML activator 1a, which was showed to be more active catalyst than hemin. (ac.ru)
  • Hemin is used to treat the symptoms of occasional attacks of porphyria related to the menstrual cycle in women. (peacehealth.org)
  • Hemin should not be used to treat porphyria that affects the skin, also called porphyria cutanea tarda. (peacehealth.org)
  • Hemin is usually given after other medicines to treat porphyria have been given for a certain amount of time. (peacehealth.org)
  • These findings suggest an important role of hemin-induced HO-1 activity as a host defense mechanism against HIV-1 infection. (jimmunol.org)
  • The present study investigated the role of hemin-induced HO-1 as a putative protection factor against HIV infection. (jimmunol.org)
  • The role of hemin or HO-1 in the pancreas and their potential modulation of pancreatic injury are unknown. (jci.org)
  • In this study we wanted to determine the role of hemin and various growth media on the fluorescing properties of S. mutans under planktonic (total biomass) and biofilm (biofilm mass) growth conditions. (iupui.edu)
  • The role of hemin and porphyrin-related compounds in the metabolism of S. mutans should be elucidated. (iupui.edu)
  • Recently, researchers have witnessed major advances in our understanding of the physiological role of hemin. (springeropen.com)
  • It is very important that your doctor check your progress at regular visits to make sure hemin is working properly. (drugs.com)
  • Hemin is a heme-oxygenase inducer, which can confer anti-inflammatory, cytoprotective, and antiapoptotic effects. (dovepress.com)
  • Here, we assessed heme oxygenase-1 (HO-1), which is a crucial antioxidative, antiapoptotic molecule against intracellular stresses, for its therapeutic potential via its inducer, hemin. (aspetjournals.org)
  • Taken together, our data show that hemin inhibits mitoBKCa and partially abolishes some of the cytoprotective properties of potassium channel opening. (sigmaaldrich.com)
  • We now show that hemin blocks cyclic AMP binding because it itself binds specifically to the regulatory subunit. (ias.ac.in)
  • Considering the role of the mitoBKCa in cytoprotection, it can be presumed that its inhibition by hemin may be a novel mechanism contributing to the severity of the ICH symptoms. (sigmaaldrich.com)
  • Datta, K. (1986) Affinity purification and properties of rat liver mitochondrial L-alanine:4,5-dioxovalerate transaminase and its inhibition by hemin Archives of Biochemistry and Biophysics, 248 (2). (ias.ac.in)
  • A. The experiment involved sequential addition of the fluorescent LDV-FITC probe (25 nM), and different concentrations of hemin (6-100 μM) or DMSO (vehicle). (nih.gov)
  • Tra nsmission electron microscopic images showed that hemin nanoparticles with different initial concentrations of hemin (0.1 and 0.5 mg/mL) were tadpole-shaped (head of approximately 200 nm and tail of 100 nm) and sphere-shaped (50-100 nm), respectively. (springeropen.com)
  • Male CD-1 mice with TNBS-induced colitis were treated with a daily dose of hemin 5 mg/kg body weight/day and 10 mg/kg body weight/day intraperitoneal, during 4 days. (dovepress.com)
  • Intraperitoneal hemin administration dramatically increases peritoneal and pancreas macrophages that overexpress HO-1 in association with pancreatic induction of the chemoattractants monocyte chemotactic protein-1 and macrophage inflammatory protein-1α but not RANTES or macrophage inflammatory protein-2. (jci.org)
  • 1) group C: non-anesthesia, (2) group H: intraperitoneal hemin (50 mg kg-1) treatment on days 5 and 6, (3) group S: 3% sevoflurane exposure for 4 h, and (4) group SH: hemin treatment + sevoflurane exposure. (smarttots.org)
  • The hemin-treated mice presented a decrease in fecal hemoglobin, ALP, and proinflammatory cytokine concentrations compared to the TNBS group. (dovepress.com)
  • Hemin, a critical component of hemoglobin, is an active ingredient of a biologic therapeutic approved by the Food and Drug Administration for the treatment of acute porphyries. (jimmunol.org)
  • Hemin is a product of hemoglobin degradation, which has strong toxicity and can induce reactive oxygen species (ROS). (frontiersin.org)
  • Neena Singh and Ajai Tripathi's recent research from Case Western Reserve University School of Medicine (OH, USA) may offer exciting new insights into prion protein's (PrP) binding motif and its interactions with hemin, a toxic byproduct of hemoglobin. (neuro-central.com)
  • In both cell lines, deletion of the hemin-binding octapeptide repeat domain inhibited PrP C -mediated increases in hemoglobin synthesis and PrP C internalization. (neuro-central.com)
  • Pharmaceutical inhibition of PrP C -hemin elicited increases in hemoglobin synthesis and also limited the propagation of pathological PrP sc , for example in CJD. (neuro-central.com)
  • Conversely, outcomes in cerebral hemorrhage may be improved by inhibiting hemin-induced endocytosis of PrP C . The downstream effects of such inhibition would preclude the upregulation of hemoglobin and improve neuronal viability by clearing extracellular hemin and increasing respiratory potential. (neuro-central.com)
  • Collectively, these results implicate PrP C in promoting neuronal survival in physiological conditions and in cerebral hemorrhage by clearing hemin from the neuronal microenvironment and upregulating the synthesis of hemoglobin. (neuro-central.com)
  • Tripathi AK, Singh N. Prion Protein-Hemin Interaction Upregulates Hemoglobin Synthesis: Implications for Cerebral Hemorrhage and Sporadic Creutzfeldt-Jakob Disease. (neuro-central.com)
  • Brain tissue loss, microglial activation, and neuronal death were significantly higher in rats receiving QA plus hemin (H-QA) versus QA and controls. (hindawi.com)
  • PEG-hemin showed higher solubility in water and significantly prolonged plasma half-life than free hemin, which resulted from its micellar nature with molecular mass of 126 kDa in aqueous media. (aspetjournals.org)
  • Moreover, hemin nanoparticles exhibited higher solubility than free hemin. (springeropen.com)
  • We postulated that the solubility of hemin nanoparticles could be increased compared to free hemin, which could have valuable applications. (springeropen.com)
  • We further show that extracellular hemin concentration correlates closely with changes in RBC deformability and we confirm that this biophysical change correlates with other indicators of cell stress. (rsc.org)
  • These data suggest that the pretreatment with curcumin induces Nrf2 and an antioxidant response that may play an important role in the protective effect of this antioxidant against hemin-induced neuronal death. (hindawi.com)
  • Hemin reduced neuronal apoptosis, improved mitochondrial dynamics and protected against cognitive deficits induced by sevoflurane in neonatal rats. (smarttots.org)
  • In order to do so, we have used a patch-clamp technique and shown that hemin inhibits mitoBKCa in human astrocytoma U-87 MG cell line mitochondria. (sigmaaldrich.com)
  • C. The experiment was conducted using U937 cells stably transfected with the FPR ΔST receptor, and involved sequential addition of the fluorescent LDV-FITC probe (4 nM), the high affinity FPR ligand N-formyl-Met-Leu-Phe-Phe (100 nM), hemin (1.5-100 μM) or DMSO (control), and LDV (2 μM). (nih.gov)
  • Complementation analyses with Escherichia coli hemA show that HutA functions as a hemin receptor, and complementation analyses with E. coli hemA tonB indicate that HutA is TonB dependent. (umt.edu)
  • Liu, X., Zhang, X., Li, N. Study of a Magnetic Photocatalyst Based on Hemin with Axial Ligand and its Degradation under Visible Light. (ac.ir)
  • In addition, hemin treatment significantly suppressed infection of both monocytes and T cells inoculated with R5, X4, R5X4 tropic strains, and reverse transcriptase-resistant, azidothymidine-resistant, ddC/ddI-resistant, nivirapine-resistant, and other clinical HIV isolates. (jimmunol.org)
  • In a rat I/R model, administration of PEG-hemin significantly elevated HO-1 expression and enzymatic activity. (aspetjournals.org)
  • Dietary hemin significantly reduced colonic carcinogenesis. (biomedcentral.com)
  • In contrast, hemin treatment of MCT-administered animals, which led to a further increase in pulmonary HO-1 mRNA expression, significantly ameliorated MCT-induced PH as well as tissue inflammation. (eurekaselect.com)
  • The data showed that the fastest growing cells were significantly more virulent than those grown more slowly, irrespective of haemin concentration. (microbiologyresearch.org)
  • Oxygen quenching agents in media such as hemin and charcoal as well as a microaerobic atmosphere and preenrichment can significantly improve recovery (2,14-16,21,25,28). (fda.gov)
  • Subinhibitory concentrations of haemin were found to significantly reduce transcription of the haemolysin genes hlb (encoding β-haemolysin) and hlgA (encoding the S-class component of γ-haemolysin), while hla (encoding α-haemolysin) and RNAIII (encoding δ-haemolysin) transcription did not appear to be affected. (microbiologyresearch.org)
  • In contrast, hemin, also in a dose-dependent manner, significantly attenuated the lipopolysaccharide-induced NF-κB activation, CAT-2 expression, and l-arginine transport. (elsevier.com)
  • Several proteins in human blood bind to hemin, such as hemopexin and serum albumin. (wikipedia.org)
  • Hemin is the prosthetic moiety for a large number of proteins that play essential roles in the transport of oxygen, mitochondrial functions, and a variety of signal transduction pathways. (jimmunol.org)
  • We propose a model of haemin utilization in Y. enterocolitica in which HemT, HemU and HemV proteins transport haemin into the cytoplasm where it is degraded by HemS thereby liberating the iron. (nih.gov)
  • Hemin, as one of the iron porphyrin derivatives, is the active center of heme-proteins, having abilities to mimic the active site of various enzymes. (biomedcentral.com)
  • 7 ] reported that hemin could combine with β-cyclodextrin by a cyclic oligosaccharide of seven α- linked glucose units [ 1 , 4 ], leading to a significant improvement in hemin solubility. (springeropen.com)
  • Tumor cells were exposed to different ALA concentrations and ALA-S activity repressed conditions, produced by hemin or glucose addition to the medium. (biomedcentral.com)
  • After 24 h of culture, ALA (0.5-5 mM), Hemin (8-24 μg/ml) or D-glucose (2-3 mg/ml) dissolved in PBS immediately prior to use, were added to the medium. (biomedcentral.com)
  • Only hemin among the intermediate compounds of heme metabolism tested was shown to be an inhibitor of purified alanine:4,5-dioxovalerate transaminase. (ias.ac.in)
  • Hemin was further shown as an uncompetitive inhibitor of both alanine and dioxovalerate. (ias.ac.in)
  • Significant increase of ROS production in H-QA rat brain was inhibited by the specific HO-1 inhibitor ZnPP which supports the idea that ROS level augmentation in hemin-treated animals is a direct consequence of HO-1 induction. (hindawi.com)
  • Spontaneous mutation to a Pgm- phenotype results in the loss of a number of divergent physiological characteristics, including the ability to store hemin and to bind Congo red at 26 degrees C. In this study, we generated and isolated transposon insertion mutants that are hemin storage negative (Hms-) and therefore unable to form pigmented colonies. (asm.org)
  • Liu J, Xin XY, Zhou H, Zhang SS (2015) A ternary composite based on graphene, hemin, and gold nanorods with high catalytic activity for the detection of cell-surface glycan expression. (springer.com)
  • The reduced graphene oxide-hemin-cysteine (rGO-H-Cys) composite and Au-PtNWs acted not only as amplification labels to amplify signals via synergetic catalysis, but also as an ideal nanocarrier to accelerate electron transfer. (rsc.org)
  • Herein, we reported a simple colorimetric strategy for label-free quantification of human telomerase activity in urine by using hemin-graphene nanomaterial (H-GNs). (selleckchem.com)
  • 6 ] indicated that crystalline hemin and L-arginate could prepare water-soluble hemin-arginate coacervation, which could be used as a new heme iron supplement in food additives, functional foods, and pharmaceuticals. (springeropen.com)
  • Engaged in the research and development of biological products with animal and vegetable as main materials, we now have successfully developed a series of products such as Soybean Extract Cu/Zn-Superoxide Dismutase (SOD), Heme Iron, Hemin, Thrombin, Bilirubin and Food grade plasma Albumen powder, etc. (lasvegasgoers.com)
  • Identification and cloning of a hemin storage locus involved in the pigmentation phenotype of Yersinia pestis. (asm.org)
  • Restriction site analysis of eight mutants identified a minimum of six potentially different insertion sites spanning an approximately 10-kb hemin storage (hms) locus. (asm.org)
  • mini-kan mutations and cloned wild-type hms locus generated in this study will greatly aid in identifying the function of hemin storage in Y. pestis. (asm.org)
  • Irr functions as a transcriptional repressor of the hut locus at all hemin concentrations tested. (umt.edu)
  • Hemin was diluted in 25% albumin to obtain a concentration of 2.4 mg/mL and administered at a dose of 1.25 mL/Kg and at a rate of 60 mL/hour. (clinicaltrials.gov)
  • B. The span of the single exponential fits for the dissociation curves (from panel A after LDV addition) plotted versus logarithm of hemin concentration. (nih.gov)
  • LDV-FITC dissociation rates (koff) were determined as described for panel A. D. The span of the single exponential fits for the dissociation curves (from panel C, after LDV addition) plotted versus logarithm of hemin concentration. (nih.gov)
  • Results indicated that exposure to a pathologically-representative concentration (10-30 μM) of hemin induced rapid endocytosis of PrP C in neuroblastoma cells. (neuro-central.com)
  • Y. enterocolitica strains mutated in hemU or hemV genes were unable to use haemin as an iron source whereas those mutated in the hemT gene were able to use haemin as an iron source. (nih.gov)
  • Acquisition of heat shock factor 2 (HSF2) DNA binding activity is accompanied by induced transcription of heat shock genes in hemin-treated K562 cells undergoing erythroid differentiation. (abo.fi)
  • In contrast, when HSF2-beta is expressed at levels exceeding those of endogenous HSF2-alpha, the hemin-induced DNA binding activity and transcription of heat shock genes are repressed, whereas overexpression of HSF2-alpha results in an enhanced hemin response. (abo.fi)
  • Moreover, cell treatment with hemin, a natural source of CO, resulted in comparable VLA-4 ligand dissociation. (nih.gov)
  • An investigation was conducted on hemin modified with axial ligand loaded onto magnetic carriers which created a kind of visible-light activated photocatalyst with good magnetic property. (ac.ir)
  • In mouse studies, hemin, a biological product of red blood cells, has been shown to boost the production of HO-1, thereby reducing oxidative stress, allowing repair of the ICC network and normalizing gastric function. (emilysstomach.com)
  • These effects may be mediated by direct interactions of hemin with DNA and perhaps other cellular constituents or by molecular complex formation between hemin and anthracyclines at intracellular sites. (aacrjournals.org)
  • Therefore, hemin-like compounds or hemin-activated macrophages may offer novel therapeutic approaches for preventing acute pancreatitis and its pulmonary complication via upregulation of HO-1. (jci.org)
  • In such pharmacological contexts, hemin is typically formulated with human albumin prior to administration by a medical professional, to reduce the risk of phlebitis and to stabilise the compound, which is potentially reactive if allowed to circulate in free-form. (wikipedia.org)
  • Hemin, the oxidized form of heme, is a highly reactive compound that induces cellular injury. (hindawi.com)
  • Moreover, 15 μ M curcumin attenuated by 55% the increase in reactive oxygen species (ROS) production, by 94% the reduction of GSH/glutathione disulfide (GSSG) ratio, and by 49% the cell death induced by hemin. (hindawi.com)
  • The mechanism for the decomposition of the LbL film was considered to involve a more reactive oxygen species (ROS) that was formed by the reaction of hemin and H2O2, which then caused nonspecific DNA cleavage. (preprints.org)
  • Normosang injection contains human hemin, which is a substance derived from human blood. (netdoctor.co.uk)
  • In mice with diabetes and slow gastric emptying, hemin increases HO-1 activity and improves gastric emptying. (clinicaltrials.gov)
  • Hemin administration before CDD feeding protected 8 of 8 mice from lethality while 7 of 16 controls died. (jci.org)
  • Protection is mediated by HO-1-overexpressing macrophages since hemin-primed macrophages home to the pancreas after transfer to naive mice and protect from CDD-induced pancreatitis. (jci.org)
  • It may therefore be concluded that Daidzein in combination with hemin may enhance the level of renal nitric oxide by decreasing the expression of caveolin. (eurekaselect.com)
  • Since the 1970s, when it was approved by the Food and Drug Administration, hemin has been used to successfully treat a variety of disorders, such as acute porphyries, control of liver allograft failure due to recurrence of erythopoietic protophoria, and thalassemia intermedia ( 10 , 11 , 12 ) with minimal side effects. (jimmunol.org)
  • Hemin injection may increase iron levels in the blood. (drugs.com)
  • A strong hemin-binding function was found by LDS-PAGE and TMBZ staining when cells were grown under hemin (iron)-limited conditions. (nih.gov)
  • Bovine source hemin powder HEMIN IRON Appearance black powder CAS No. 16009-13-5 Purity 99% EINECS No. (lookchem.com)
  • 2,3 Heme or its Fe(III) oxidation product hemin is catalytically broken down by HO to yield CO, bilirubin, and iron. (ahajournals.org)
  • Hemin is a potent iron supplement. (springeropen.com)
  • These results suggested that hemin nanoparticles could serve as a potential iron supplement with potential applications in the food, biomedical, and photodynamic-photothermal therapy fields. (springeropen.com)
  • The advantage of the mutant in colonizing the iron-limited light-organ tissues is caused, at least in part, by its greater ability to acquire host-derived hemin. (pnas.org)
  • Bartonella quintana , the agent of trench fever and a cause of endocarditis and bacillary angiomatosis in humans, has the highest reported in vitro hemin requirement for any bacterium. (asm.org)
  • One variant showed auxotrophy for hemin with a deletion of 20 365 nucleotides, dosC-ydiK-mmuP-mmuM-tauA-tauB-tauC-tauD-hemB-yaiT-yaiV-ampH-yddQ-sbmA-yaiW-yaiY-yaiZ , including hemB , and was more resistant to aminoglycosides and carbapenems, but more susceptible to aztreonam, than the parent strain. (microbiologyresearch.org)
  • As predicted, in the presence of NO, wild-type V. fischeri grew more slowly on hemin than a hnoX deletion mutant. (pnas.org)
  • 0.004) dose-dependent decrease in hemin binding relative to controls, suggesting that HbpA plays an active role in hemin acquisition and therefore pathogenesis. (asm.org)
  • In a dose-dependent manner, hemin enhanced the lipopolysaccharide-induced Nrf2 activation and HO-1 expression. (elsevier.com)