Protoporphyrins
Porphyrins
Thiol-dependent degradation of protoporphyrin IX by plant peroxidases. (1/1018)
Protoporphyrin IX (PP) is the last porphyrin intermediate in common between heme and chlorophyll biosynthesis. This pigment normally does not accumulate in plants because its highly photodynamic nature makes it toxic. While the steps leading to heme and chlorophylls are well characterized, relatively little is known of the metabolic fate of excess PP in plants. We have discovered that plant peroxidases can rapidly degrade this pigment in the presence of thiol-containing substrates such as glutathione and cysteine. This thiol-dependent degradation of PP by horseradish peroxidase consumes oxygen and is inhibited by ascorbic acid. (+info)Mg-chelatase of tobacco: the role of the subunit CHL D in the chelation step of protoporphyrin IX. (2/1018)
The Mg-chelation is found to be a prerequisite to direct protoporphyrin IX into the chlorophyll (Chl)-synthesizing branch of the tetrapyrrol pathway. The ATP-dependent insertion of magnesium into protoporphyrin IX is catalyzed by the enzyme Mg-chelatase, which consists of three protein subunits (CHL D, CHL I, and CHL H). We have chosen the Mg-chelatase from tobacco to obtain more information about the mode of molecular action of this complex enzyme by elucidating the interactions in vitro and in vivo between the central subunit CHL D and subunits CHL I and CHL H. We dissected CHL D in defined peptide fragments and assayed for the essential part of CHL D for protein-protein interaction and enzyme activity. Surprisingly, only a small part of CHL D, i.e., 110 aa, was required for interaction with the partner subunits and maintenance of the enzyme activity. In addition, it could be demonstrated that CHL D is capable of forming homodimers. Moreover, it interacted with both CHL I and CHL H. Our data led to the outline of a two-step model based on the cooperation of the subunits for the chelation process. (+info)Timing of illumination is essential for effective and safe photodynamic therapy: a study in the normal rat oesophagus. (3/1018)
5-Aminolaevulinic acid (ALA)-induced, protoporphyrin IX (PpIX)-mediated photodynamic therapy (PDT) is an experimental treatment modality for (pre)malignant oesophageal lesions. This study aimed to optimize the time of illumination after ALA administration. Six groups of eight rats received 200 mg kg(-1) ALA orally, eight rats served as controls. Illumination was performed at 1, 2, 3, 4, 6 or 12 h after ALA administration with a 1-cm cylindrical diffuser placed in a balloon catheter (laser parameters: 633 nm, 25 J radiant energy, power output 100 mW). During illumination, fluorescence measurements and light dosimetry were performed. Animals were sacrificed at 48 h (n = 4) or 28 days (n = 4) after PDT. At day 28, an oesophagogram was performed. Largest PpIX fluorescence was found at 3 h after ALA administration. In vivo fluence rate was three times higher than the calculated incident fluence rate. At 48 h after PDT, major epithelial damage was found in all animals illuminated at 2 h, whereas less epithelial damage was found at 3-6 h and none at 1 and 12 h. In animals illuminated at 4, 6 and 12 h, but not at 2 h, oesophagograms showed severe dilatations and histology showed loss of Schwann cells. These results demonstrate that the choice of time interval between ALA administration and illumination is critical for achieving epithelial damage without oesophageal functional impairment. A short interval of 2-3 h seems to be most appropriate. (+info)Reaction of the microsomal heme oxygenase with cobaltic protoporphyrin IX, and extremely poor substrate. (4/1018)
A reconstituted heme oxygenase system which was composed of a purified heme oxygenase from pig spleen microsomes and a partially purified NADPH-cytochrome c reductase from pig liver microsomes could not catalyze the conversion of cobaltic protoporphyrin IX (Co-heme) to biliverdin, although Co-heme could bind with the heme oxygenase protein to form a complex. The heme oxygenase system in the microsomes from pig spleen, rat spleen, and rat kidney also failed to oxidize Co-heme to biliverdin. Properties of the complex of Co-heme and heme oxygenase closely resembled those of cobalt myoglobin and cobalt hemoglobin; the Co-heme bound to the heme oxygenase protein did not react with cyanide and azide, the Co-heme moiety was reduced but only slowly with sodium dithionite, and the reduced form of the Co-heme did not appear to bind carbon monoxide. The co-heme bound to heme oxygenase was not reduced with the NADPH-cytochrome c reductase system in air. These findings further support the views that heme oxygenase may have a heme-binding crevice similar to those of myoglobin and hemoglobin and that reduction of heme is the prerequisite for the oxidative degradation of heme in the heme oxygenase reaction. (+info)Hypoxia significantly reduces aminolaevulinic acid-induced protoporphyrin IX synthesis in EMT6 cells. (5/1018)
We have studied the effects of hypoxia on aminolaevulinic acid (ALA)-induced protoporphyrin IX (PpIX) synthesis in EMT6 monolayer cultures characterized by different cell densities and proliferation rates. Specifically, after ALA incubation under hypoxic or normoxic conditions, we detected spectrofluorometrically the PpIX content of the following populations: (a) low-density exponentially growing cells; (b) high-density fed-plateau cells; and (c) high-density unfed-plateau cells. These populations were selected either for the purpose of comparison with other in vitro studies (low-density exponentially growing cells) or as representatives of tumour regions adjacent to (high-density fed-plateau cells) and further away from (high-density unfed-plateau cells) capillaries. The amount of PpIX per cell produced by each one of these populations was higher after normoxic ALA incubation. The magnitude of the effect of hypoxia on PpIX synthesis was dependent on cell density and proliferation rate. A 42-fold decrease in PpIX fluorescence was observed for the high-density unfed-plateau cells. PpIX production by the low-density exponential cells was affected the least by ALA incubation under hypoxic conditions (1.4-fold decrease), whereas the effect on the high-density fed-plateau population was intermediate (20-fold decrease). (+info)The iron regulatory protein can determine the effectiveness of 5-aminolevulinic acid in inducing protoporphyrin IX in human primary skin fibroblasts. (6/1018)
The level of endogenous photosensitiser, protoporphyrin IX (PPIX), can be enhanced in the cells by 5-aminolevulinic acid (ALA). We investigated the effect of critical parameters such as growth state of the cells and availability of intracellular iron in modulating the level of PPIX, in human primary cultured skin fibroblasts (FEK4) maintained either in exponentially growing or growth-arrested phase, following treatment with ALA. The addition of ALA to exponentially growing cells increased the level of PPIX 6-fold relative to control cells; however, in growth-arrested cells the same treatment increased the level of PPIX up to 34-fold. The simultaneous addition of the hydrophilic iron-chelator Desferal with ALA, boosted the level of PPIX up to 47-fold in growing cells and up to 42-fold in growth-arrested cells, suggesting that iron is limiting under the latter conditions. The strict dependence of PPIX enhancement on free available iron levels was examined by the level of activation of iron regulatory protein in band shift assays. This analysis revealed that the basal level of iron regulatory protein in growth-arrested cells was 6-fold higher than in growing cells, reflecting the influence of the free available iron pool in exponentially growing cells. Interestingly, the same ratio was found between the basal level concentration of PPIX in growing and growth-arrested cells. We propose that iron regulatory protein activation could serve as a marker for developing photodynamic therapy protocols because it identifies cells and tissues with a propensity to accumulate PPIX and it is therefore likely to predict the effectiveness of such therapies. (+info)Peroxynitrite induces haem oxygenase-1 in vascular endothelial cells: a link to apoptosis. (7/1018)
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)Active and higher intracellular uptake of 5-aminolevulinic acid in tumors may be inhibited by glycine. (8/1018)
Topical 5-aminolevulinic acid is used for the fluorescence-based diagnosis and photodynamic treatment of superficial precancerous and cancerous lesions of the skin. Thus, we investigated the kinetics of 5-aminolevulinic acid-induced fluorescence and the mechanisms responsible for the selective formation of porphyrins in tumors in vivo. Using amelanotic melanomas (A-Mel-3) grown in dorsal skinfold chambers of Syrian golden hamsters fluorescence kinetics were measured up to 24 h after topical application of 5-aminolevulinic acid (1%, 3%, or 10%) for 1 h, 4 h, or 8 h by intravital microscopy (n = 54). Maximal fluorescence intensity in tumors after 1 h application (3% 5-aminolevulinic acid) occurred 150 min and after 4 h application (3% 5-aminolevulinic acid) directly thereafter. Increasing either concentration of 5-aminolevulinic acid or application time did not yield a higher fluorescence intensity. The selectivity of the fluorescence in tumors decreased with increasing application time. Fluorescence spectra indicated the formation of protoporphyrin IX (3% 5-aminolevulinic acid, 4 h; n = 3). The simultaneous application of 5-aminolevulinic acid (3%, 4 h) and glycine (20 microM or 200 microM; n = 10) reduced fluorescence in tumor and surrounding host tissue significantly. In contrast, neither decreasing iron concentration by desferrioxamine (1% and 3%; n = 10) nor inducing tetrapyrrole accumulation using 1, 10-phenanthroline (7.5 mM; n = 5) increased fluorescence in tumors. The saturation and faster increase of fluorescence in the tumor together with a reduction of fluorescence by the application of glycine suggests an active and higher intracellular uptake of 5-aminolevulinic acid in tumor as compared with the surrounding tissue. Shorter application (1 h) yields a better contrast between tumor and surrounding tissue for fluorescence diagnosis. The additional topical application of modifiers of the heme biosynthesis, desferrioxamine or 1,10-phenanthroline, however, is unlikely to enhance the efficacy of topical 5-aminolevulinic acid-photodynamic therapy at least in our model. (+info)Protoporphyrins are organic compounds that are the immediate precursors to heme in the porphyrin synthesis pathway. They are composed of a porphyrin ring, which is a large, complex ring made up of four pyrrole rings joined together, with an acetate and a propionate side chain at each pyrrole. Protoporphyrins are commonly found in nature and are important components of many biological systems, including hemoglobin, the protein in red blood cells that carries oxygen throughout the body.
There are several different types of protoporphyrins, including protoporphyrin IX, which is the most common form found in humans and other animals. Protoporphyrins can be measured in the blood or other tissues as a way to diagnose or monitor certain medical conditions, such as lead poisoning or porphyrias, which are rare genetic disorders that affect the production of heme. Elevated levels of protoporphyrins in the blood or tissues can indicate the presence of these conditions and may require further evaluation and treatment.
Griseofulvin is an antifungal medication used to treat various fungal infections, including those affecting the skin, hair, and nails. It works by inhibiting the growth of fungi, particularly dermatophytes, which cause these infections. Griseofulvin can be obtained through a prescription and is available in oral (by mouth) and topical (on the skin) forms.
The primary mechanism of action for griseofulvin involves binding to tubulin, a protein necessary for fungal cell division. This interaction disrupts the formation of microtubules, which are crucial for the fungal cell's structural integrity and growth. As a result, the fungi cannot grow and multiply, allowing the infected tissue to heal and the infection to resolve.
Common side effects associated with griseofulvin use include gastrointestinal symptoms (e.g., nausea, vomiting, diarrhea), headache, dizziness, and skin rashes. It is essential to follow the prescribing physician's instructions carefully when taking griseofulvin, as improper usage may lead to reduced effectiveness or increased risk of side effects.
It is important to note that griseofulvin has limited use in modern medicine due to the development of newer and more effective antifungal agents. However, it remains a valuable option for specific fungal infections, particularly those resistant to other treatments.
Porphyrins are complex organic compounds that contain four pyrrole rings joined together by methine bridges (=CH-). They play a crucial role in the biochemistry of many organisms, as they form the core structure of various heme proteins and other metalloproteins. Some examples of these proteins include hemoglobin, myoglobin, cytochromes, and catalases, which are involved in essential processes such as oxygen transport, electron transfer, and oxidative metabolism.
In the human body, porphyrins are synthesized through a series of enzymatic reactions known as the heme biosynthesis pathway. Disruptions in this pathway can lead to an accumulation of porphyrins or their precursors, resulting in various medical conditions called porphyrias. These disorders can manifest as neurological symptoms, skin lesions, and gastrointestinal issues, depending on the specific type of porphyria and the site of enzyme deficiency.
It is important to note that while porphyrins are essential for life, their accumulation in excessive amounts or at inappropriate locations can result in pathological conditions. Therefore, understanding the regulation and function of porphyrin metabolism is crucial for diagnosing and managing porphyrias and other related disorders.
Protoporphyrin IX
Zinc protoporphyrin
Magnesium protoporphyrin IX methyltransferase
Magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase
Urine test strip
Porphyrinogen
Chlorophyll b
Magnesium chelatase
Coproporphyrinogen III oxidase
Chlorophyllide-a oxygenase
Protochlorophyllide reductase
Chlorophyll synthase
Protochlorophyllide
Chlorophyll
Chlorophyllide a reductase
Chlorophyll a
Chlorophyllide
Bacteriochlorophyll
Divinyl chlorophyllide a 8-vinyl-reductase
Erythropoietic porphyria
Protoporphyrinogen IX
Porphyrin
Porphine
Carol Remmer Angle
Parent structure
Liquid biopsy
Heme oxygenase
Ferrochelatase
Methyl aminolevulinate
Pulse generator
Protoporphyrin IX - Wikipedia
NHANES 2001-2002: Erythrocyte Protoporphyrin Data Documentation, Codebook, and Frequencies
White light-informed optical properties improve ultrasound-guided fluorescence tomography of photoactive protoporphyrin IX
Intracellular Localization is a Cofactor for the Phototoxicity of Protoporphyrin IX in the Gastrointestinal Tract: In Vitro...
On the Role of Iron and one of its Chelating Agents in the Production of Protoporphyrin IX Generated by 5-Aminolevulinic Acid...
Kinetic and localization properties of protoporphyrin dimethyl ester in fibrosarcoma cells | (1994) | Wessels | Publications |...
Sequential Evaluation of Erythrocyte Zinc Protoporphyrin in a Dog with Polycythemia Submitted to Phlebotomies - WSAVA2009 - VIN
An enzyme-coupled continuous spectrophotometric assay for magnesium protoporphyrin IX methyltransferases - IRep - Nottingham...
Monitoring mitochondrial oxygen levels via protoporphyrin-IX triplet state lifetime technique: assessment of factors reducing...
Zinc Protoporphyrin - Lab Doctor
Superoxide dismutase is upregulated in Staphylococcus aureus following protoporphyrin-mediated photodynamic inactivation and...
Cu(II) Protoporphyrin IX - Echelon Biosciences
Sn(IV) Protoporphyrin IX Archives - Echelon Biosciences
Synthetic antimicrobial and LPS-neutralising peptides suppress inflammatory and immune responses in skin cells and promote...
Preventing Lead Poisoning in Young Children
Zinc Protoporphyrin or ZPP is a blood test for lead poisoning
2008 Nutrition Report Executive Summary | CDC
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Adult Blood Lead Epidemiology and Surveillance --- United States, 1998--2001
Acute Porphyria: Practice Essentials, Background, Pathophysiology
Protoporphyrin IX-loaded magnetoliposomes as a potential drug delivery system for photodynamic therapy: Fabrication,...
Near-infrared autofluorescence induced by intraplaque hemorrhage and heme degradation as marker for high-risk atherosclerotic...
heme b (CHEBI:26355)
Chester Porphyria Treatment & Management: Approach Considerations
RCSB PDB - 4U9J: Crystal structure of an H-NOX protein from S. oneidensis in the Mn(II) ligation state, Q154A/Q155A/K156A mutant
Synthesis of divinyl protochlorophyllide. Enzymological properties of the Mg-protoporphyrin IX monomethyl ester oxidative...
Comparison of minimal detectable protoporphyrin IX concentrations with a loupe device and conventional 5-ALA fluorescence...
PPIX11
- An alternative name for heme is iron protoporphyrin IX (iron PPIX). (wikipedia.org)
- Protoporphyrin IX reacts with iron salts in air to give the complex FeCl(PPIX). (wikipedia.org)
- Subsurface fluorescence imaging is desirable for medical applications, including protoporphyrin-IX (PpIX)-based skin tumor diagnosis, surgical guidance, and dosimetry in photodynamic therapy. (nih.gov)
- Although the use of 5-aminolevulinic acid-induced protoporphyrin IX (PPIX) shows important advantages over other photosensitizers, the main mechanisms of phototoxicity induced are still poorly understood. (bioone.org)
- Photodynamic therapy (PDT) with 5-aminolevulinic acid (ALA) or its derivatives as precursors of protoporphyrin IX (PPIX) is routinely used in dermatology for the treatment of various pathologies. (bioone.org)
- In the samples with the highest fluorescence intensity, a modified fluorescence spectrum was observed after 10 h, with the emergence of a peak at 590 nm, which is attributed to zinc protoporphyrin IX (Zn PPIX). (bioone.org)
- Accordingly, the protoporphyrin-IX triplet state lifetime technique (PpIX-TSLT) measures oxygen pressure levels in mitochondria (mitoPO2) via porphyrin excitation which produce 630nm delayed fluorescence (DF). (utwente.nl)
- METHODS To overcome the shallow tissue penetration of blue light, which maximally excites the ALA-induced fluorophore protoporphyrin IX (PpIX) but is also strongly absorbed by hemoglobin and oxyhemoglobin, a system was developed to illuminate the surgical field with red light (620-640 nm) matching a secondary, smaller absorption peak of PpIX and detecting the fluorescence emission through a 650-nm longpass filter. (neurosurgery-blog.com)
- Background: Protoporphyrin IX (PpIX) is a well-known photosensitizer that has great potential for use in photodynamic therapy (PDT). (bezmialem.edu.tr)
- Previous technical implementations of this technique have relied on specifically modified surgical microscopes to visualize intratumoral fluorescent protoporphyrin (PpIX). (bvsalud.org)
- Erythropoietic protoporphyria (EPP), a metabolic disorder, leads to the accumulation of protoporphyrin (PPIX). (researchgate.net)
Erythrocyte8
- Also, see the documentation for the primary exam data for Laboratory 39 (Erythrocyte Protoporphyrin). (cdc.gov)
- Note: Erythrocyte Protoporphyrin was performed at Centers for Disease Control and Prevention in 2001 and the State of New York Department of Health in 2002. (cdc.gov)
- Free erythrocyte protoporphyrin (FEP) is measured by a modification of the method of Sassa et al. (cdc.gov)
- thus, iron depletion may develop and then erythrocyte zinc protoporphyrin (ZPP) is formed during the final step of heme synthesis. (vin.com)
- Erythrocyte total protoporphyrin is the initial screening exam to diagnose EPP and XLP, if the total is elevated with metal-free protoporphyrin it is suggestive of EPP or XLP. (medscape.com)
- Initial testing includes porphobilinogen (PBG) measurement, urine porphyrin fractionation, and erythrocyte protoporphyrin measurements. (arupconsult.com)
- Free erythrocyte protoporphyrin was markedly elevated in all cases. (cdc.gov)
- Biochemical assessment of iron status relies on serum-based indicators, such as serum ferritin (SF), transferrin saturation, and soluble transferrin receptor (sTfR), as well as erythrocyte protoporphyrin. (cdc.gov)
Zinc1
- Zinc protoporphyrin (ZPP) is a normal metabolite that accumulates in trace amounts in erythrocytes during hemoglobin synthesis. (clinlabnavigator.com)
Heme7
- Protoporphyrin IX is an organic compound, classified as a porphyrin, that plays an important role in living organisms as a precursor to other critical compounds like heme (hemoglobin) and chlorophyll. (wikipedia.org)
- Protoporphyrin IX is an important precursor to biologically essential prosthetic groups such as heme, cytochrome c, and chlorophylls. (wikipedia.org)
- Cu (II) Protoporphyrin IX does not inhibit heme oxygenase (the enzyme that catalyzes the conversion of heme to biliverdin in the heme degradation pathway) and is used as a negative control for Zn (II) Protoporphyrin (an inihibitor of heme oxygenase). (echelon-inc.com)
- The final biochemical reaction in the heme pathway is the chelation of ferrous iron with protoporphyrin IX by the enzyme, ferrochelatase. (clinlabnavigator.com)
- The techniques are based on the application of the heme biomolecule precursor 5-aminolevulinic acid which induces the endogenous accumulation of the photosensitizer protoporphyrin IX in designated tissues. (thieme-connect.de)
- Binds 1 heme B (iron-protoporphyrin IX) group covalently and 1 calcium ion per heterodimer. (lu.se)
- Ferrochelatase catalyses iron insertion into protoporphyrin IX at the terminal step of heme biosynthesis, while IscU assists in the formation of iron-sulphur clusters. (lu.se)
Fluorescence1
- Comparison of minimal detectable protoporphyrin IX concentrations with a loupe device and conventional 5-ALA fluorescence microscopy: an experimental study. (bvsalud.org)
Excess protoporphyrin2
- This excess protoporphyrin leads to incapacitating phototoxic burns in sunlight exposed skin. (researchgate.net)
- Patients with liver failure may need liver transplantation, but liver transplantation is not curative because the predominant source of excess protoporphyrin production is the bone marrow. (msdmanuals.com)
Ester5
- Pascal Uehlinger , Jean-Pierre Ballini , Hubert van den Bergh , and Georges Wagnières "On the Role of Iron and one of its Chelating Agents in the Production of Protoporphyrin IX Generated by 5-Aminolevulinic Acid and its Hexyl Ester Derivative Tested on an Epidermal Equivalent of Human Skin," Photochemistry and Photobiology 82(4), 1069-1076, (1 July 2006). (bioone.org)
- Enzymological properties of the Mg-protoporphyrin IX monomethyl ester oxidative cyclase system. (docksci.com)
- Caroline J. WALKER,* Paul A. CASTELFRANCOt and Barry J. WHYTE Department of Botany, University of California at Davis, Davis, CA 95616, U.S.A. The resolution and reconstitution of the Mg-protoporphyrin IX monomethyl ester oxidative cyclase system into a supernatant and a pellet fraction was accomplished by a procedure involving salt treatment followed by osmotic shock. (docksci.com)
- This restoration effect could be demonstrated using either Mg-protoporphyrin IX or Mg-protoporphyrin IX monomethyl ester as the cyclase substrate in the presence or absence of S-adenosylmethionine. (docksci.com)
- INTRODUCTION The Mg-protoporphyrin IX monomethyl ester (MgProtoMe) oxidative cyclase system (or cyclase) catalyses the conversion of MgProtoMe to protochlorophyllide (Pchlide) in the chlorophyll (Chl) synthesis pathway. (docksci.com)
Photodynamic1
- Protoporphyrin-dimethylester (PP) is an amphiphilic porphyrin which shows a fast clearance and is therefore of interest for photodynamic therapy. (spie.org)
Excitation1
- The protoporphyrin in the aqueous phase is measured fluorometrically at excitation and emission wavelengths of 404 and 658 nm, respectively. (cdc.gov)
Biosynthesis2
- In the biosynthesis of those molecules, the metal cation is inserted into protoporphyrin IX by enzymes called chelatases. (wikipedia.org)
- In chlorophyll biosynthesis, the enzyme magnesium chelatase converts it into Mg-protoporphyrin IX. (wikipedia.org)
Acid2
Magnesium1
- We conclude that ATP hydrolysis by BchI+D is required for an activation step in the magnesium chelatase reaction, whereas ATPase activity of BchH and the phosphate exchange activity of BchI participate in subsequent reactions leading to the insertion of Mg2+ into protoporphyrin IX. (lu.se)
Micrograms1
- After a correction for the individual hematocrit is made, the final concentration of protoporphyrin in a specimen is expressed as micrograms per deciliter (ug/dL) of packed red blood cells (RBC). (cdc.gov)
Accumulates1
- Protoporphyrin accumulates in bone marrow and red blood cells, enters the plasma, and is deposited in the skin or excreted by the liver into bile. (msdmanuals.com)
Protoheme1
- Fe-protoporphyrin IX or protoheme IX). (wikipedia.org)
Porphyrins1
- The prefix proto often means 'first' in science nomenclature (such as carbon protoxide), hence Hans Fischer is thought to have coined the name protoporphyrin as the first class of porphyrins. (wikipedia.org)
Porphyrias1
- Stool studies: The ratio of fecal coproporphyrin to fecal protoporphyrin varies among the porphyrias. (medscape.com)
Diagnosis1
- Diagnosis is based on symptoms and increased levels of protoporphyrin in red blood cells and plasma. (msdmanuals.com)
Iron1
- A metalloprotoporphyrin in which the four pyrrole nitrogens of the protoporphyrin moiety are coordinated to iron. (ebi.ac.uk)
Includes1
- Fischer also generated the Roman numeral naming system which includes 15 protoporphyrin analogs, the naming system is not systematic however. (wikipedia.org)
Aminolevulinic Acid3
- Of these enzymes, it has been considered that the inhibition of o-aminolevulinic acid dehydratase (ALAD) catalyzing the step from 0aminolevulinic acid (ALA) to porphobilinogen (PBG) and that of heme synthetase catalyzing the step from protoporphyrin IX to heme are of particular interest. (docksci.com)
- 14. Protoporphyrin IX fluorescence photobleaching and the response of rat Barrett's esophagus following 5-aminolevulinic acid photodynamic therapy. (nih.gov)
- 15. Phenytoin reduces 5-aminolevulinic acid-induced protoporphyrin IX accumulation in malignant glioma cells. (nih.gov)
Zinc Protoporphyrin11
- Zinc protoporphyrin (ZPP) testing has been studied previously as a substitute for ferritin (fer) testing of blood donors in determining iron stores. (medscape.com)
- Zinc protoporphyrin (ZPP) is the main form of nonheme protoporphyrin present in red blood cells (RBCs) with iron depletion. (medscape.com)
- Hemoglobin, serum iron, and zinc protoporphyrin in lead-exposed workers. (nih.gov)
- a statistically significant negative correlation between hemoglobin and zinc protoporphyrin was also detected. (nih.gov)
- There was no significant correlation between blood lead or zinc protoporphyrin and serum iron, TIBC and Fe/TIBC. (nih.gov)
- the correlation between hemoglobin and zinc protoporphyrin reached a much higher level of significance. (nih.gov)
- TY - JOUR T1 - Comparative analysis of zinc protoporphyrin and blood lead levels in lead-exposed Andean children. (unboundmedicine.com)
- Inhibition of HO by zinc protoporphyrin-IX led to inhibition of MCP-1 and increased expression of CCR2, its cognate receptor. (nih.gov)
- Pretreatment with zinc protoporphyrin-IX, an HO inhibitor, but not copper protoporphyrin-IX, which does not block the enzyme, attenuated the CdCl 2 -induced apoptosis. (jci.org)
- Such antiapoptotic effects of zinc protoporphyrin-IX were repressed by supplementation of dichloromethane, a CO donor. (jci.org)
- this event was also suppressed by zinc protoporphyrin-IX and restored by dichloromethane. (jci.org)
Accumulation of protoporphyrin IX1
- Brazilian Green Propolis Extract Synergizes with Protoporphyrin IX-mediated Photodynamic Therapy via Enhancement of Intracellular Accumulation of Protoporphyrin IX and Attenuation of NF-κB and COX-2. (propolisscience.org)
Erythrocyte protoporphyrin levels1
- Determination of erythrocyte protoporphyrin levels was performed in workers who are occupationally exposed to lead. (docksci.com)
Biliverdin4
- The colours come from the way that two pigments in the shell - biliverdin and protoporphyrin - blend with each other and with the calcium carbonate that makes most of the shell. (newscientist.com)
- Sander's student, Jasmina Wiemann, found the oviraptor eggs contained both biliverdin and protoporphyrin. (newscientist.com)
- Protoporphyrin (PP) and biliverdin (BV) give rise to the enormous diversity in avian egg coloration. (peerj.com)
- Using a double-checking liquid chromatography ESI-Q-TOF mass spectrometry routine, we traced the origin of colored eggs to their non-avian dinosaur ancestors by providing the first record of the avian eggshell pigments protoporphyrin and biliverdin in the eggshells of Late Cretaceous oviraptorid dinosaurs. (peerj.com)
Photodynamic Therapy3
- 1. Catechin reduces phototoxic effects induced by protoporphyrin IX-based photodynamic therapy in the chick embryo chorioallantoic membrane. (nih.gov)
- 4. Stimulation and homogenization of the protoporphyrin IX endogenous production by photobiomodulation to increase the potency of photodynamic therapy. (nih.gov)
- 18. Protoporphyrin IX photodynamic therapy for synovitis. (nih.gov)
Micrograms per deciliter1
- After a correction for the individual hematocrit is made, the final concentration of protoporphyrin in a specimen is expressed as micrograms per deciliter (ug/dL) of packed red blood cells (RBC). (cdc.gov)
Pigments1
- These pigments possess an isocyclic E ring formed by the Mg-protoporphyrin IX monomethylester cyclase (MgPME-cyclase). (whiterose.ac.uk)
Pigment1
- The pink color results from a high concentration of brown protoporphyrin pigment being deposited on the eggshell. (colorwithleo.com)
Markedly increased1
- The diagnosis of EPP is established by detection of markedly increased free erythrocyte protoporphyrin and/or by the identification of biallelic pathogenic variants in FECH on molecular genetic testing . (nih.gov)
Fluorescent1
- The level of erythrocyte protoporphyrin was easily measured with microsamples of blood by utilizing a fluorescent assay. (docksci.com)
Genetics1
- For an olive egger to lay pink eggs, both parents must not only have brown egg laying heritage, but also the specific genetics for heavy protoporphyrin deposition causing dark brown or pink eggs. (colorwithleo.com)
Excretion1
- Severe liver complications are difficult to treat: cholestyramine and other porphyrin absorbents (to interrupt the enterohepatic circulation of protoporphyrin and promote its fecal excretion) and plasmapheresis and intravenous hemin are sometimes beneficial. (nih.gov)
Enzyme2
- In chlorophyll biosynthesis, the enzyme magnesium chelatase converts it into Mg-protoporphyrin IX. (wikipedia.org)
- On the other hand, because of the enzyme inhibition described above, the measurement of erythrocyte protoporphyrin (EP) can also be expected to be more useful for the evaluation of the degree of lead effects in occupational exposure. (docksci.com)
Levels3
- Both of these protoporphyrias cause increased protoporphyrin levels that cause photosensitivity and may lead to hepatopathy and further increases in erythrocyte and plasma porphyrin levels. (nih.gov)
- We evaluated erythrocyte protoporphyrin and plasma porphyrin levels in all subjects with EPP (83 subjects) or XLP (9 subjects) without evidence of liver disease tested repeatedly at a single laboratory over 25 years. (nih.gov)
- Diagnosis is based on symptoms and increased levels of protoporphyrin in red blood cells and plasma. (msdmanuals.com)
PROTEIN1
- Most protoporphyrin came from the protein layer or cuticle still coating the fossil egg, as it does in modern bird eggs. (newscientist.com)
Detection1
- The erythrocyte protoporphyrin test is especially useful in the detection of mild increases in blood lead concentration under conditions of occupational exposure. (docksci.com)
Lead2
- Erythrocyte protoporphyrin test for occupational lead exposure. (docksci.com)
- The log of erythrocyte protoporphyrin level was closely correlated to blood lead level (r=.72) in leadexposed workers. (docksci.com)
Free2
Production1
- Patients with liver failure may need liver transplantation, but liver transplantation is not curative because the predominant source of excess protoporphyrin production is the bone marrow. (msdmanuals.com)
Formation1
- 10. Protoporphyrin IX formation and photobleaching in different layers of normal human skin: methyl- and hexylaminolevulinate and different light sources. (nih.gov)
Cells1
- Protoporphyrin accumulates in bone marrow and red blood cells, enters the plasma, and is deposited in the skin or excreted by the liver into bile. (msdmanuals.com)
Important1
- 8. Subcellular localization pattern of protoporphyrin IX is an important determinant for its photodynamic efficiency of human carcinoma and normal cell lines. (nih.gov)
Total1
- Variation of erythrocyte total protoporphyrin up to 25% is expected in patients with protoporphyria, whereas greater increases might raise concern for protoporphyric hepatopathy. (nih.gov)
Higher1
- Despite the wide range of organisms that synthesize protoporphyrin IX, the process is largely conserved from bacteria to mammals with a few distinct exceptions in higher plants. (wikipedia.org)
Disease1
- Note: Erythrocyte Protoporphyrin was performed at Centers for Disease Control and Prevention in 2001 and the State of New York Department of Health in 2002. (cdc.gov)
Alpha1
- In this case, the resulting bilin carries the suffix IXα which indicates the parent molecule was protoporphyrin IX cleaved at the alpha position. (wikipedia.org)
Layers1
- Brown egg layers have genes controlling protoporphyrin deposition. (colorwithleo.com)