Iron-containing proteins that are widely distributed in animals, plants, and microorganisms. Their major function is to store IRON in a nontoxic bioavailable form. Each ferritin molecule consists of ferric iron in a hollow protein shell (APOFERRITINS) made of 24 subunits of various sequences depending on the species and tissue types.
The protein components of ferritins. Apoferritins are shell-like structures containing nanocavities and ferroxidase activities. Apoferritin shells are composed of 24 subunits, heteropolymers in vertebrates and homopolymers in bacteria. In vertebrates, there are two types of subunits, light chain and heavy chain. The heavy chain contains the ferroxidase activity.
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.
Hemosiderin is an iron-containing pigment that originates from the breakdown of hemoglobin and accumulates in tissues, primarily in macrophages, as a result of various pathological conditions such as hemorrhage, inflammation, or certain storage diseases.
An iron-binding beta1-globulin that is synthesized in the LIVER and secreted into the blood. It plays a central role in the transport of IRON throughout the circulation. A variety of transferrin isoforms exist in humans, including some that are considered markers for specific disease states.
Anemia characterized by decreased or absent iron stores, low serum iron concentration, low transferrin saturation, and low hemoglobin concentration or hematocrit value. The erythrocytes are hypochromic and microcytic and the iron binding capacity is increased.
Disorders in the processing of iron in the body: its absorption, transport, storage, and utilization. (From Mosby's Medical, Nursing, & Allied Health Dictionary, 4th ed)
Proteins that regulate cellular and organismal iron homeostasis. They play an important biological role by maintaining iron levels that are adequate for metabolic need, but below the toxicity threshold.
An excessive accumulation of iron in the body due to a greater than normal absorption of iron from the gastrointestinal tract or from parenteral injection. This may arise from idiopathic hemochromatosis, excessive iron intake, chronic alcoholism, certain types of refractory anemia, or transfusional hemosiderosis. (From Churchill's Illustrated Medical Dictionary, 1989)
Membrane glycoproteins found in high concentrations on iron-utilizing cells. They specifically bind iron-bearing transferrin, are endocytosed with its ligand and then returned to the cell surface where transferrin without its iron is released.
Unstable isotopes of iron that decay or disintegrate emitting radiation. Fe atoms with atomic weights 52, 53, 55, and 59-61 are radioactive iron isotopes.
Natural product isolated from Streptomyces pilosus. It forms iron complexes and is used as a chelating agent, particularly in the mesylate form.
A disorder of iron metabolism characterized by a triad of HEMOSIDEROSIS; LIVER CIRRHOSIS; and DIABETES MELLITUS. It is caused by massive iron deposits in parenchymal cells that may develop after a prolonged increase of iron absorption. (Jablonski's Dictionary of Syndromes & Eponymic Diseases, 2d ed)
A form of pneumoconiosis resulting from inhalation of iron in the mining dust or welding fumes.
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.
Anemia characterized by a decrease in the ratio of the weight of hemoglobin to the volume of the erythrocyte, i.e., the mean corpuscular hemoglobin concentration is less than normal. The individual cells contain less hemoglobin than they could have under optimal conditions. Hypochromic anemia may be caused by iron deficiency from a low iron intake, diminished iron absorption, or excessive iron loss. It can also be caused by infections or other diseases, therapeutic drugs, lead poisoning, and other conditions. (Stedman, 25th ed; from Miale, Laboratory Medicine: Hematology, 6th ed, p393)
Organic chemicals that form two or more coordination links with an iron ion. Once coordination has occurred, the complex formed is called a chelate. The iron-binding porphyrin group of hemoglobin is an example of a metal chelate found in biological systems.
Inorganic or organic compounds that contain divalent iron.
Inorganic or organic compounds containing trivalent iron.
A multifunctional iron-sulfur protein that is both an iron regulatory protein and cytoplasmic form of aconitate hydratase. It binds to iron regulatory elements found on mRNAs involved in iron metabolism and regulates their translation. Its RNA binding ability and its aconitate hydrolase activity are dependent upon availability of IRON.
Ceruloplasmin is a blue copper-containing protein primarily synthesized in the liver, functioning as a ferroxidase enzyme involved in iron homeostasis and contributing to copper transportation in the body.
ERYTHROCYTE size and HEMOGLOBIN content or concentration, usually derived from ERYTHROCYTE COUNT; BLOOD hemoglobin concentration; and HEMATOCRIT. The indices include the mean corpuscular volume (MCV), the mean corpuscular hemoglobin (MCH), and the mean corpuscular hemoglobin concentration (MCHC).
A ferroin compound that forms a stable magenta-colored solution with the ferrous ion. The complex has an absorption peak at 562 nm and is used as a reagent and indicator for iron.
Proteins that specifically bind to IRON.
The techniques used to draw blood from a vein for diagnostic purposes or for treatment of certain blood disorders such as erythrocytosis, hemochromatosis, polycythemia vera, and porphyria cutanea tarda.
Large, hoofed mammals of the family EQUIDAE. Horses are active day and night with most of the day spent seeking and consuming food. Feeding peaks occur in the early morning and late afternoon, and there are several daily periods of rest.
A multifunctional iron-sulfur protein that is both an iron regulatory protein and cytoplasmic form of aconitate hydratase. It binds to iron regulatory elements found on mRNAs involved in iron metabolism and regulates their translation. Its rate of degradation is increased in the presence of IRON.
Puncture of a vein to draw blood for therapeutic purposes. Bloodletting therapy has been used in Talmudic and Indian medicine since the medieval time, and was still practiced widely in the 18th and 19th centuries. Its modern counterpart is PHLEBOTOMY.
A complex of ferric oxyhydroxide with dextrans of 5000 to 7000 daltons in a viscous solution containing 50 mg/ml of iron. It is supplied as a parenteral preparation and is used as a hematinic. (Goodman and Gilman's The Pharmacological Basis of Therapeutics, 8th ed, p1292)
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A disorder characterized by reduced synthesis of the beta chains of hemoglobin. There is retardation of hemoglobin A synthesis in the heterozygous form (thalassemia minor), which is asymptomatic, while in the homozygous form (thalassemia major, Cooley's anemia, Mediterranean anemia, erythroblastic anemia), which can result in severe complications and even death, hemoglobin A synthesis is absent.
Forms of hepcidin, a cationic amphipathic peptide synthesized in the liver as a prepropeptide which is first processed into prohepcidin and then into the biologically active hepcidin forms, including in human the 20-, 22-, and 25-amino acid residue peptide forms. Hepcidin acts as a homeostatic regulators of iron metabolism and also possesses antimicrobial activity.
Conditions in which there is a generalized increase in the iron stores of body tissues, particularly of liver and the MONONUCLEAR PHAGOCYTE SYSTEM, without demonstrable tissue damage. The name refers to the presence of stainable iron in the tissue in the form of hemosiderin.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)

Coronary heart disease and iron status: meta-analyses of prospective studies. (1/3222)

BACKGROUND: Studies of iron status and coronary heart disease (CHD) have yielded conflicting results. In a systematic review ("meta-analysis"), we quantitatively assessed epidemiological associations reported in prospective studies. METHODS AND RESULTS: Studies were identified by computer-assisted searches of the published literature, scanning of relevant reference lists, hand searching of relevant journals, and discussions with relevant authors. The following was abstracted: size and type of cohort, mean age, mean duration of follow-up, assay methods, degree of adjustment for confounders, and relationship of CHD risk to the baseline assay results. Twelve studies were identified, involving a total of 7800 CHD cases, with several reporting on >1 marker of iron status. For serum ferritin, with 570 CHD cases in 5 studies, comparison of individuals with baseline values >/=200 versus <200 microg/L yielded a combined risk ratio of 1.0 (95% CI, 0.8 to 1.3). For transferrin saturation, with 6194 CHD cases in 5 studies, comparison of individuals in the top third with those in the bottom third of the baseline measurements yielded a combined risk ratio of 0.9 (95% CI, 0.7 to 1.1). Comparisons of individuals in top and bottom thirds of baseline measurements also yielded nonsignificant risk ratios in combined analyses of studies involving total iron-binding capacity (combined risk ratio, 1.0; 95% CI, 0.7 to 1.5), serum iron (0.8; 95% CI, 0.7 to 1.0), and total dietary iron (0.8; 95% CI, 0.7 to 1.1). CONCLUSIONS: Published prospective studies do not provide good evidence to support the existence of strong epidemiological associations between iron status and CHD.  (+info)

The identification of ferritin in the nucleus of K562 cells, and investigation of a possible role in the transcriptional regulation of adult beta-globin gene expression. (2/3222)

We studied the subcellular distribution of ferritin in K562 cells by immunofluorescence techniques and have made a reappraisal of a direct binding interaction between ferritin and the proximal promoter region of the human beta-globin gene, as previously mentioned in the literature. Confocal microscopy indicates that ferritin, the iron-storage protein, is present in the nucleus of K562 cells, in addition to its expected cytoplasmic localisation. The stain distribution suggests that it is not directly associated with the nuclear matrix. Using a gel mobility shift assay, a protein that cross-reacts with monoclonal ferritin antibodies competitively binds to a double-stranded oligonucleotide spanning the region situated 150 base pairs upstream from the beta-globin transcription start site. Despite this antibody cross-reactivity, the protein is unlike cytosolic ferritin as it appears to be highly sensitive to both temperature and freeze-thaw cycles, and UV-crosslinking experiments indicate that the molecular mass of the protein factor lies between 90 and 100 kDa. In conclusion, while the intranuclear location of ferritin is described in the present study, ferritin is not in direct contact with the beta-globin promoter region.  (+info)

Ferritin mutants of Escherichia coli are iron deficient and growth impaired, and fur mutants are iron deficient. (3/3222)

Escherichia coli contains at least two iron storage proteins, a ferritin (FtnA) and a bacterioferritin (Bfr). To investigate their specific functions, the corresponding genes (ftnA and bfr) were inactivated by replacing the chromosomal ftnA and bfr genes with disrupted derivatives containing antibiotic resistance cassettes in place of internal segments of the corresponding coding regions. Single mutants (ftnA::spc and bfr::kan) and a double mutant (ftnA::spc bfr::kan) were generated and confirmed by Western and Southern blot analyses. The iron contents of the parental strain (W3110) and the bfr mutant increased by 1.5- to 2-fold during the transition from logarithmic to stationary phase in iron-rich media, whereas the iron contents of the ftnA and ftnA bfr mutants remained unchanged. The ftnA and ftnA bfr mutants were growth impaired in iron-deficient media, but this was apparent only after the mutant and parental strains had been precultured in iron-rich media. Surprisingly, ferric iron uptake regulation (fur) mutants also had very low iron contents (2.5-fold less iron than Fur+ strains) despite constitutive expression of the iron acquisition systems. The iron deficiencies of the ftnA and fur mutants were confirmed by Mossbauer spectroscopy, which further showed that the low iron contents of ftnA mutants are due to a lack of magnetically ordered ferric iron clusters likely to correspond to FtnA iron cores. In combination with the fur mutation, ftnA and bfr mutations produced an enhanced sensitivity to hydroperoxides, presumably due to an increase in production of "reactive ferrous iron." It is concluded that FtnA acts as an iron store accommodating up to 50% of the cellular iron during postexponential growth in iron-rich media and providing a source of iron that partially compensates for iron deficiency during iron-restricted growth. In addition to repressing the iron acquisition systems, Fur appears to regulate the demand for iron, probably by controlling the expression of iron-containing proteins. The role of Bfr remains unclear.  (+info)

Ferroxidase activity of ferritin: effects of pH, buffer and Fe(II) and Fe(III) concentrations on Fe(II) autoxidation and ferroxidation. (4/3222)

It is widely accepted that iron deposition in the iron storage protein ferritin in vitro involves Fe(II) oxidation, and that ferritin facilitates this oxidation at a ferroxidase site on the protein. However, these views have recently been questioned, with the protein ferroxidase activity instead being attributed to autoxidation from the buffer alone. Ligand exchange between another protein with ferroxidase activity and ferritin has been proposed as an alternative mechanism for iron incorporation into ferritin. In the present work, a pH stat apparatus is used to eliminate the influence of buffers on iron(II) oxidation. Here we show that the recent experiments questioning the ferroxidase activity of ferritin were flawed by inadequate pH control, that buffers actually retard rather than facilitate iron(II) oxidation, and that horse spleen ferritin has ferroxidase activity when measured under proper experimental conditions. Furthermore, high pH (7.0), a high Fe(II) concentration and the presence of Fe(III) all favour Fe(II) autoxidation in the presence or absence of ferritin.  (+info)

Streptavidin facilitates internalization and pulmonary targeting of an anti-endothelial cell antibody (platelet-endothelial cell adhesion molecule 1): a strategy for vascular immunotargeting of drugs. (5/3222)

Conjugation of drugs with antibodies to surface endothelial antigens is a potential strategy for drug delivery to endothelium. We studied antibodies to platelet-endothelial adhesion molecule 1 (PECAM-1, a stably expressed endothelial antigen) as carriers for vascular immunotargeting. Although 125I-labeled anti-PECAM bound to endothelial cells in culture, the antibody was poorly internalized by the cells and accumulated poorly after intravenous administration in mice and rats. However, conjugation of biotinylated anti-PECAM (b-anti-PECAM) with streptavidin (SA) markedly stimulated uptake and internalization of anti-PECAM by endothelial cells and by cells expressing PECAM. In addition, conjugation with streptavidin markedly stimulated uptake of 125I-labeled b-anti-PECAM in perfused rat lungs and in the lungs of intact animals after either intravenous or intraarterial injection. The antioxidant enzyme catalase conjugated with b-anti-PECAM/SA bound to endothelial cells in culture, entered the cells, escaped intracellular degradation, and protected the cells against H2O2-induced injury. Anti-PECAM/SA/125I-catalase accumulated in the lungs after intravenous injection or in the perfused rat lungs and protected these lungs against H2O2-induced injury. Thus, modification of a poor carrier antibody with biotin and SA provides an approach for facilitation of antibody-mediated drug targeting. Anti-PECAM/SA is a promising candidate for vascular immunotargeting of bioactive drugs.  (+info)

Transcriptional regulation of the mouse ferritin H gene. Involvement of p300/CBP adaptor proteins in FER-1 enhancer activity. (6/3222)

We previously identified a major enhancer of the mouse ferritin H gene (FER-1) that is central to repression of the ferritin H gene by the adenovirus E1A oncogene (Tsuji, Y., Akebi, N., Lam, T. K., Nakabeppu, Y., Torti, S. V., and Torti, F. M. (1995) Mol. Cell. Biol. 15, 5152-5164). To dissect the molecular mechanism of transcriptional regulation of ferritin H, E1A mutants were tested for their ability to repress FER-1 enhancer activity using cotransfection with ferritin H-chloramphenicol acetyltransferase (CAT) reporter constructs. Here we report that p300/CBP transcriptional adaptor proteins are involved in the regulation of ferritin H transcription through the FER-1 enhancer element. Thus, E1A mutants that failed to bind p300/CBP lost the ability to repress FER-1, whereas mutants of E1A that abrogated its interaction with Rb, p107, or p130 were fully functional in transcriptional repression. Transfection with E1A did not affect endogenous p300/CBP levels, suggesting that repression of FER-1 by E1A is not due to repression of p300/CBP synthesis, but to E1A and p300/CBP interaction. In addition, we have demonstrated that transfection of a p300 expression plasmid significantly activated ferritin H-CAT containing the FER-1 enhancer, but had a marginal effect on ferritin H-CAT with FER-1 deleted. Furthermore, both wild-type p300 and a p300 mutant that failed to bind E1A but retained an adaptor function restored FER-1 enhancer activity repressed by E1A. Sodium butyrate, an inhibitor of histone deacetylase, mimicked p300/CBP function in activation of ferritin H-CAT and elevation of endogenous ferritin H mRNA, suggesting that the histone acetyltransferase activity of p300/CBP or its associated proteins may contribute to the activation of ferritin H transcription. Recruitment of these broadly active transcriptional adaptor proteins for ferritin H synthesis may represent an important mechanism by which changes in iron metabolism are coordinated with other cellular responses mediated by p300/CBP.  (+info)

Iron-deficient diet reduces atherosclerotic lesions in apoE-deficient mice. (7/3222)

BACKGROUND: Iron deposition is evident in human atherosclerotic lesions, suggesting that iron may play a role in the development of atherosclerosis. To test this idea, the correlation between the extent of iron deposition and the severity of atherosclerosis in apolipoprotein E (apoE)-deficient mice was investigated. Furthermore, the effect of a low-iron diet on the progression of atherosclerotic lesions in these animals was evaluated. METHODS AND RESULTS: Iron deposition in tissues of apoE-deficient mice was examined by Perls' staining method. The results clearly demonstrated that iron deposits are present in atherosclerotic lesions and tissue sections of heart and liver in an age-dependent manner. When the young mice received a low-iron diet for 3 months, the hematocrit, serum iron, hemoglobin, and cholesterol concentrations were not significantly altered compared with those of littermates placed on a chow diet. However, the serum ferritin level of animals in the iron-restricted group was 27% to 30% lower than that of the control group in either sex. Furthermore, the lipoproteins isolated from the iron-restricted group exhibited greater resistance to copper-induced oxidation. Histological examination revealed that atherosclerotic lesions developed in mice fed a low-iron diet were significantly smaller than those found in control littermates. Likewise, the iron deposition as well as tissue iron content was much less in aortic tissues of the iron-restricted animals. Circulating autoantibodies to oxidized LDL and immunostains for epitopes of malondialdehyde-modified LDL detected on lesions were also significantly lower in mice fed a low-iron diet. CONCLUSIONS: Iron deposition is closely associated with the progression of atherosclerosis in apoE-deficient mice. Restriction in dietary iron intake leads to significant inhibition of lesion formation in these animals. These results suggest that the beneficial effect of a low-iron diet may be mediated, at least in part, by the reduction of iron deposition as well as LDL oxidation in vascular lesions.  (+info)

Effect of iron-, iodine-, and beta-carotene-fortified biscuits on the micronutrient status of primary school children: a randomized controlled trial. (8/3222)

BACKGROUND: Deficiencies of iron, iodine, and vitamin A are prevalent worldwide and can affect the mental development and learning ability of schoolchildren. OBJECTIVE: The aim of this study was to determine the effect of micronutrient-fortified biscuits on the micronutrient status of primary school children. DESIGN: Micronutrient status was assessed in 115 children aged 6-11 y before and after consumption of biscuits (fortified with iron, iodine, and beta-carotene) for 43 wk over a 12-mo period and was compared with that in a control group (n = 113) who consumed nonfortified biscuits. Cognitive function, growth, and morbidity were assessed as secondary outcomes. RESULTS: There was a significant between-group treatment effect on serum retinol, serum ferritin, serum iron, transferrin saturation, and urinary iodine (P <0.0001) and in hemoglobin and hematocrit (P <0.05). The prevalence of low serum retinol concentrations (<0.70 micromol/L) decreased from 39.1% to 12.2%, of low serum ferritin concentrations (<20 microg/L) from 27.8% to 13.9%, of anemia (hemoglobin <120 g/L) from 29.6% to 15.6%, and of low urinary iodine concentrations (<100 microg/L) from 97.5% to 5.4%. There was a significant between-group treatment effect (P <0.05) in cognitive function with the digit span forward task (short-term memory). Fewer school days were missed in the intervention than in the control group because of respiratory- (P = 0.097) and diarrhea-related (P = 0.013) illnesses. The intervention had no effect on anthropometric status [corrected]. CONCLUSIONS: Fortified biscuits resulted in a significant improvement in the micronutrient status of primary school children from a poor rural community and also appeared to have a favorable effect on morbidity and cognitive function [corrected].  (+info)

Ferritin is a protein in iron-metabolizing cells that stores iron in a water-soluble form. It is found inside the cells (intracellular) and is released into the bloodstream when the cells break down or die. Measuring the level of ferritin in the blood can help determine the amount of iron stored in the body. High levels of ferritin may indicate hemochromatosis, inflammation, liver disease, or other conditions. Low levels of ferritin may indicate anemia, iron deficiency, or other conditions.

Apoferritins are the protein shells or apoproteins of ferritin molecules that are devoid of iron. Ferritin is a protein in cells that stores iron and releases it in a form that can be used by the body. Apoferritin can bind with iron ions to form ferritin. It has a hollow, spherical structure and is often used as a model for studying protein folding and assembly.

In the context of medicine, iron is an essential micromineral and key component of various proteins and enzymes. It plays a crucial role in oxygen transport, DNA synthesis, and energy production within the body. Iron exists in two main forms: heme and non-heme. Heme iron is derived from hemoglobin and myoglobin in animal products, while non-heme iron comes from plant sources and supplements.

The recommended daily allowance (RDA) for iron varies depending on age, sex, and life stage:

* For men aged 19-50 years, the RDA is 8 mg/day
* For women aged 19-50 years, the RDA is 18 mg/day
* During pregnancy, the RDA increases to 27 mg/day
* During lactation, the RDA for breastfeeding mothers is 9 mg/day

Iron deficiency can lead to anemia, characterized by fatigue, weakness, and shortness of breath. Excessive iron intake may result in iron overload, causing damage to organs such as the liver and heart. Balanced iron levels are essential for maintaining optimal health.

Hemosiderin is a golden-brown pigment that consists of iron-containing protein complexes called ferritin and ferrikinase. It is insoluble in water and forms as a result of the breakdown of hemoglobin in the reticuloendothelial system, primarily in macrophages. Hemosiderin deposits can be found in various tissues and organs, such as the spleen, liver, and brain, under conditions of increased red blood cell destruction or impaired iron metabolism. These deposits are often associated with diseases such as hemochromatosis, thalassemia, and chronic inflammation.

Transferrin is a glycoprotein that plays a crucial role in the transport and homeostasis of iron in the body. It's produced mainly in the liver and has the ability to bind two ferric (Fe3+) ions in its N-lobe and C-lobe, thus creating transferrin saturation.

This protein is essential for delivering iron to cells while preventing the harmful effects of free iron, which can catalyze the formation of reactive oxygen species through Fenton reactions. Transferrin interacts with specific transferrin receptors on the surface of cells, particularly in erythroid precursors and brain endothelial cells, to facilitate iron uptake via receptor-mediated endocytosis.

In addition to its role in iron transport, transferrin also has antimicrobial properties due to its ability to sequester free iron, making it less available for bacterial growth and survival. Transferrin levels can be used as a clinical marker of iron status, with decreased levels indicating iron deficiency anemia and increased levels potentially signaling inflammation or liver disease.

Iron-deficiency anemia is a condition characterized by a decrease in the total amount of hemoglobin or red blood cells in the blood, caused by insufficient iron levels in the body. Hemoglobin is a protein in red blood cells that carries oxygen from the lungs to the rest of the body. When iron levels are low, the body cannot produce enough hemoglobin, leading to the production of smaller and fewer red blood cells, known as microcytic hypochromic anemia.

Iron is essential for the production of hemoglobin, and a deficiency in iron can result from inadequate dietary intake, chronic blood loss, or impaired absorption. In addition to fatigue and weakness, symptoms of iron-deficiency anemia may include shortness of breath, headaches, dizziness, pale skin, and brittle nails. Treatment typically involves iron supplementation and addressing the underlying cause of the iron deficiency.

Iron metabolism disorders are a group of medical conditions that affect the body's ability to absorb, transport, store, or utilize iron properly. Iron is an essential nutrient that plays a crucial role in various bodily functions, including oxygen transportation and energy production. However, imbalances in iron levels can lead to several health issues.

There are two main types of iron metabolism disorders:

1. Iron deficiency anemia (IDA): This condition occurs when the body lacks adequate iron to produce sufficient amounts of hemoglobin, a protein in red blood cells responsible for carrying oxygen throughout the body. Causes of IDA may include inadequate dietary iron intake, blood loss, or impaired iron absorption due to conditions like celiac disease or inflammatory bowel disease.
2. Hemochromatosis: This is a genetic disorder characterized by excessive absorption and accumulation of iron in various organs, including the liver, heart, and pancreas. Over time, this excess iron can lead to organ damage and diseases such as cirrhosis, heart failure, diabetes, and arthritis. Hemochromatosis is typically caused by mutations in the HFE gene, which regulates iron absorption in the intestines.

Other iron metabolism disorders include:

* Anemia of chronic disease (ACD): A type of anemia that occurs in individuals with chronic inflammation or infection, where iron is not efficiently used for hemoglobin production due to altered regulation.
* Sideroblastic anemias: These are rare disorders characterized by the abnormal formation of ringed sideroblasts (immature red blood cells containing iron-laden mitochondria) in the bone marrow, leading to anemia and other symptoms.
* Iron-refractory iron deficiency anemia (IRIDA): A rare inherited disorder caused by mutations in the TMPRSS6 gene, resulting in impaired regulation of hepcidin, a hormone that controls iron absorption and distribution in the body. This leads to both iron deficiency and iron overload.

Proper diagnosis and management of iron metabolism disorders are essential to prevent complications and maintain overall health. Treatment options may include dietary modifications, iron supplementation, phlebotomy (bloodletting), or chelation therapy, depending on the specific disorder and its severity.

Iron-regulatory proteins (IRPs) are specialized RNA-binding proteins that play a crucial role in the post-transcriptional regulation of iron homeostasis in mammalian cells. They are named as such because they regulate the expression of genes involved in iron metabolism, primarily by binding to specific cis-acting elements known as iron-responsive elements (IREs) located within the untranslated regions (UTRs) of target mRNAs.

There are two main IRPs: IRP1 and IRP2. Both proteins contain an N-terminal RNA-binding domain that recognizes and binds to IREs, as well as a C-terminal region involved in protein-protein interactions and other regulatory functions. Under conditions of iron deficiency or oxidative stress, IRPs become activated and bind to IREs, leading to changes in mRNA stability, translation, or both.

IRP1 can exist in two distinct conformational states: an active RNA-binding form (when iron levels are low) and an inactive aconitase form (when iron levels are sufficient). In contrast, IRP2 is primarily regulated by protein degradation, with its stability being modulated by the presence or absence of iron.

By binding to IREs within mRNAs encoding proteins involved in iron uptake, storage, and utilization, IRPs help maintain cellular iron homeostasis through a variety of mechanisms, including:

1. Promoting translation of transferrin receptor 1 (TfR1) mRNA to increase iron import when iron levels are low.
2. Inhibiting translation of ferritin heavy chain and light chain mRNAs to reduce iron storage when iron levels are low.
3. Stabilizing the mRNA encoding divalent metal transporter 1 (DMT1) to enhance iron uptake under conditions of iron deficiency.
4. Promoting degradation of transferrin receptor 2 (TfR2) and ferroportin mRNAs to limit iron import and export, respectively, when iron levels are high.

Overall, the regulation of iron metabolism by IRPs is crucial for maintaining proper cellular function and preventing the accumulation of toxic free radicals generated by iron-catalyzed reactions.

Iron overload is a condition characterized by an excessive accumulation of iron in the body's tissues and organs, particularly in the liver, heart, and pancreas. This occurs when the body absorbs more iron than it can use or eliminate, leading to iron levels that are higher than normal.

Iron overload can result from various factors, including hereditary hemochromatosis, a genetic disorder that affects how the body absorbs iron from food; frequent blood transfusions, which can cause iron buildup in people with certain chronic diseases such as sickle cell anemia or thalassemia; and excessive consumption of iron supplements or iron-rich foods.

Symptoms of iron overload may include fatigue, joint pain, abdominal discomfort, irregular heartbeat, and liver dysfunction. If left untreated, it can lead to serious complications such as cirrhosis, liver failure, diabetes, heart problems, and even certain types of cancer. Treatment typically involves regular phlebotomy (removal of blood) to reduce iron levels in the body, along with dietary modifications and monitoring by a healthcare professional.

Transferrin receptors are membrane-bound proteins found on the surface of many cell types, including red and white blood cells, as well as various tissues such as the liver, brain, and placenta. These receptors play a crucial role in iron homeostasis by regulating the uptake of transferrin, an iron-binding protein, into the cells.

Transferrin binds to two ferric ions (Fe3+) in the bloodstream, forming a complex known as holo-transferrin. This complex then interacts with the transferrin receptors on the cell surface, leading to endocytosis of the transferrin-receptor complex into the cell. Once inside the cell, the acidic environment within the endosome causes the release of iron ions from the transferrin molecule, which can then be transported into the cytoplasm for use in various metabolic processes.

After releasing the iron, the apo-transferrin (iron-free transferrin) is recycled back to the cell surface and released back into the bloodstream, where it can bind to more ferric ions and repeat the cycle. This process helps maintain appropriate iron levels within the body and ensures that cells have access to the iron they need for essential functions such as DNA synthesis, energy production, and oxygen transport.

In summary, transferrin receptors are membrane-bound proteins responsible for recognizing and facilitating the uptake of transferrin-bound iron into cells, playing a critical role in maintaining iron homeostasis within the body.

"Iron radioisotopes" refer to specific forms of the element iron that have unstable nuclei and emit radiation. These isotopes are often used in medical imaging and treatment procedures due to their ability to be detected by specialized equipment. Common iron radioisotopes include Iron-52, Iron-55, Iron-59, and Iron-60. They can be used as tracers to study the distribution, metabolism, or excretion of iron in the body, or for targeted radiation therapy in conditions such as cancer.

Deferoxamine is a medication used to treat iron overload, which can occur due to various reasons such as frequent blood transfusions or excessive iron intake. It works by binding to excess iron in the body and promoting its excretion through urine. This helps to prevent damage to organs such as the heart and liver that can be caused by high levels of iron.

Deferoxamine is an injectable medication that is typically administered intravenously or subcutaneously, depending on the specific regimen prescribed by a healthcare professional. It may also be used in combination with other medications to manage iron overload more effectively.

It's important to note that deferoxamine should only be used under the guidance of a medical professional, as improper use or dosing can lead to serious side effects or complications.

Hemochromatosis is a medical condition characterized by excessive absorption and accumulation of iron in the body, resulting in damage to various organs. It's often referred to as "iron overload" disorder. There are two main types: primary (hereditary) and secondary (acquired). Primary hemochromatosis is caused by genetic mutations that lead to increased intestinal iron absorption, while secondary hemochromatosis can be the result of various conditions such as multiple blood transfusions, chronic liver disease, or certain types of anemia.

In both cases, the excess iron gets stored in body tissues, particularly in the liver, heart, and pancreas, which can cause organ damage and lead to complications like cirrhosis, liver failure, diabetes, heart problems, and skin discoloration. Early diagnosis and treatment through regular phlebotomy (blood removal) or chelation therapy can help manage the condition and prevent severe complications.

Siderosis is a medical condition characterized by the abnormal accumulation of iron in various tissues and organs, most commonly in the lungs. This occurs due to the repeated inhalation of iron-containing dusts or fumes, which can result from certain industrial processes such as welding, mining, or smelting.

In the lungs, this iron deposit can lead to inflammation and fibrosis, potentially causing symptoms like coughing, shortness of breath, and decreased lung function. It is important to note that siderosis itself is not contagious or cancerous, but there may be an increased risk for lung cancer in individuals with severe and prolonged exposure to iron-containing particles.

While siderosis is generally non-reversible, the progression of symptoms can often be managed through medical interventions and environmental modifications to reduce further exposure to iron-containing dusts or fumes.

Hemoglobin (Hb or Hgb) is the main oxygen-carrying protein in the red blood cells, which are responsible for delivering oxygen throughout the body. It is a complex molecule made up of four globin proteins and four heme groups. Each heme group contains an iron atom that binds to one molecule of oxygen. Hemoglobin plays a crucial role in the transport of oxygen from the lungs to the body's tissues, and also helps to carry carbon dioxide back to the lungs for exhalation.

There are several types of hemoglobin present in the human body, including:

* Hemoglobin A (HbA): This is the most common type of hemoglobin, making up about 95-98% of total hemoglobin in adults. It consists of two alpha and two beta globin chains.
* Hemoglobin A2 (HbA2): This makes up about 1.5-3.5% of total hemoglobin in adults. It consists of two alpha and two delta globin chains.
* Hemoglobin F (HbF): This is the main type of hemoglobin present in fetal life, but it persists at low levels in adults. It consists of two alpha and two gamma globin chains.
* Hemoglobin S (HbS): This is an abnormal form of hemoglobin that can cause sickle cell disease when it occurs in the homozygous state (i.e., both copies of the gene are affected). It results from a single amino acid substitution in the beta globin chain.
* Hemoglobin C (HbC): This is another abnormal form of hemoglobin that can cause mild to moderate hemolytic anemia when it occurs in the homozygous state. It results from a different single amino acid substitution in the beta globin chain than HbS.

Abnormal forms of hemoglobin, such as HbS and HbC, can lead to various clinical disorders, including sickle cell disease, thalassemia, and other hemoglobinopathies.

Hypochromic anemia is a type of anemia characterized by the presence of red blood cells that have lower than normal levels of hemoglobin and appear paler in color than normal. Hemoglobin is a protein in red blood cells that carries oxygen from the lungs to the rest of the body. In hypochromic anemia, there may be a decrease in the production or increased destruction of red blood cells, leading to a reduced number of red blood cells and insufficient oxygen supply to the tissues.

Hypochromic anemia can result from various underlying medical conditions, including iron deficiency, thalassemia, chronic inflammation, lead poisoning, and certain infections or chronic diseases. Treatment for hypochromic anemia depends on the underlying cause and may include iron supplements, dietary changes, medications, or blood transfusions.

Iron chelating agents are medications that bind to iron in the body, forming a stable complex that can then be excreted from the body. These agents are primarily used to treat iron overload, a condition that can occur due to frequent blood transfusions or certain genetic disorders such as hemochromatosis. By reducing the amount of iron in the body, these medications can help prevent or reduce damage to organs such as the heart and liver. Examples of iron chelating agents include deferoxamine, deferasirox, and deferiprone.

Ferrous compounds are inorganic substances that contain iron (Fe) in its +2 oxidation state. The term "ferrous" is derived from the Latin word "ferrum," which means iron. Ferrous compounds are often used in medicine, particularly in the treatment of iron-deficiency anemia due to their ability to provide bioavailable iron to the body.

Examples of ferrous compounds include ferrous sulfate, ferrous gluconate, and ferrous fumarate. These compounds are commonly found in dietary supplements and multivitamins. Ferrous sulfate is one of the most commonly used forms of iron supplementation, as it has a high iron content and is relatively inexpensive.

It's important to note that ferrous compounds can be toxic in large doses, so they should be taken under the guidance of a healthcare professional. Overdose can lead to symptoms such as nausea, vomiting, diarrhea, abdominal pain, and potentially fatal consequences if left untreated.

Ferric compounds are inorganic compounds that contain the iron(III) cation, Fe3+. Iron(III) is a transition metal and can form stable compounds with various anions. Ferric compounds are often colored due to the d-d transitions of the iron ion. Examples of ferric compounds include ferric chloride (FeCl3), ferric sulfate (Fe2(SO4)3), and ferric oxide (Fe2O3). Ferric compounds have a variety of uses, including as catalysts, in dye production, and in medical applications.

Iron Regulatory Protein 1 (IRP1) is a protein that plays a crucial role in the post-transcriptional regulation of iron homeostasis in cells. It is involved in the detection of cellular iron levels and responds by modulating the translation and stability of messenger RNAs (mRNAs) that encode proteins essential for iron metabolism.

IRP1 can bind to specific sequences called Iron Responsive Elements (IREs) present in the untranslated regions of mRNAs. When cellular iron levels are low, IRP1 binds to IREs and inhibits the translation of mRNAs encoding proteins responsible for iron uptake and storage, while stabilizing mRNAs that encode proteins involved in iron mobilization. Conversely, when iron levels are high, IRP1 dissociates from IREs, allowing for the normal translation of these mRNAs and maintaining iron homeostasis within the cell.

It is important to note that IRP1 has dual functions: it can act as an Iron Regulatory Protein (IRP) when iron levels are low, and as a cytosolic aconitase (an enzyme in the citric acid cycle) when iron levels are sufficient. This ability to switch between these two roles is facilitated by the presence of a [4Fe-4S] cluster, which is sensitive to cellular iron levels. When iron is abundant, the [4Fe-4S] cluster assembles, converting IRP1 into its cytosolic aconitase form; when iron is scarce, the cluster disassembles, enabling IRP1 to bind IREs and regulate iron metabolism-related gene expression.

Ceruloplasmin is a protein found in blood plasma that binds and transports copper ions. It plays a crucial role in copper metabolism, including the oxidation of ferrous iron to ferric iron, which is necessary for the incorporation of iron into transferrin, another protein responsible for transporting iron throughout the body. Ceruloplasmin also acts as an antioxidant by scavenging free radicals and has been implicated in neurodegenerative disorders like Alzheimer's disease and Wilson's disease, a genetic disorder characterized by abnormal copper accumulation in various organs.

Erythrocyte indices are a set of calculated values that provide information about the size and hemoglobin content of red blood cells (erythrocytes). These indices are commonly used in the complete blood count (CBC) test to help diagnose various types of anemia and other conditions affecting the red blood cells.

The three main erythrocyte indices are:

1. Mean Corpuscular Volume (MCV): This is the average volume of a single red blood cell, measured in femtoliters (fL). MCV helps to differentiate between microcytic, normocytic, and macrocytic anemia. Microcytic anemia is characterized by low MCV values (100 fL).
2. Mean Corpuscular Hemoglobin (MCH): This is the average amount of hemoglobin present in a single red blood cell, measured in picograms (pg). MCH helps to assess the oxygen-carrying capacity of red blood cells. Low MCH values may indicate hypochromic anemia, where the red blood cells have reduced hemoglobin content.
3. Mean Corpuscular Hemoglobin Concentration (MCHC): This is the average concentration of hemoglobin in a single red blood cell, measured as a percentage. MCHC reflects the hemoglobin concentration relative to the size of the red blood cells. Low MCHC values may indicate hypochromic anemia, while high MCHC values could suggest spherocytosis or other conditions affecting red blood cell shape and integrity.

These erythrocyte indices are calculated based on the red blood cell count, hemoglobin concentration, and hematocrit results obtained from a CBC test. They provide valuable information for healthcare professionals to diagnose and manage various hematological conditions.

Ferrozine is not a medical term, but a chemical compound with the formula C$_{32}$H$_{18}$N$_{6}$Na$_{2}$O$_{8}$. It is also known as Fer(III)zine and 3-(2-Pyridyl)-5,6-bis(4-phenylsulfonic acid)‐1,2,4-triazine disodium salt.

Ferrozine is a reagent used in chemical assays to chelate and quantify iron(III) ions (Fe$^{3+}$). It forms a stable, intensely colored complex with Fe$^{3+}$, which can be measured spectrophotometrically. This property makes Ferrozine useful for determining the concentration of iron in various samples, such as water, food, or biological fluids.

However, it is not used directly as a medical treatment or diagnosis tool but rather as a laboratory reagent to support research and analytical purposes related to medicine.

Iron-binding proteins, also known as transferrins, are a type of protein responsible for the transport and storage of iron in the body. They play a crucial role in maintaining iron homeostasis by binding free iron ions and preventing them from participating in harmful chemical reactions that can produce reactive oxygen species (ROS) and cause cellular damage.

Transferrin is the primary iron-binding protein found in blood plasma, while lactoferrin is found in various exocrine secretions such as milk, tears, and saliva. Both transferrin and lactoferrin have a similar structure, consisting of two lobes that can bind one ferric ion (Fe3+) each. When iron is bound to these proteins, they are called holo-transferrin or holo-lactoferrin; when they are unbound, they are referred to as apo-transferrin or apo-lactoferrin.

Iron-binding proteins have a high affinity for iron and can regulate the amount of free iron available in the body. They help prevent iron overload, which can lead to oxidative stress and cellular damage, as well as iron deficiency, which can result in anemia and other health problems.

In summary, iron-binding proteins are essential for maintaining iron homeostasis by transporting and storing iron ions, preventing them from causing harm to the body's cells.

Phlebotomy is a medical term that refers to the process of making an incision in a vein, usually in the arm, in order to draw blood. It is also commonly known as venipuncture. This procedure is performed by healthcare professionals for various purposes such as diagnostic testing, blood donation, or therapeutic treatments like phlebotomy for patients with hemochromatosis (a condition where the body absorbs too much iron from food).

The person who performs this procedure is called a phlebotomist. They must be trained in the proper techniques to ensure that the process is safe and relatively pain-free for the patient, and that the blood sample is suitable for laboratory testing.

I'm sorry for any confusion, but "horses" is not a medical term. It is the common name given to the species *Equus ferus caballus*, which are large domesticated mammals used for transportation, work, and recreation. If you have any questions about horses or a related topic that you would like a medical perspective on, please let me know and I'd be happy to help!

Iron Regulatory Protein 2 (IRP2) is a regulatory protein involved in the post-transcriptional control of iron homeostasis. It binds to specific sequences called Iron Responsive Elements (IREs) found in the untranslated regions of mRNAs encoding proteins involved in iron metabolism, such as ferritin and transferrin receptor.

When cellular iron levels are low, IRP2 binds to the IREs and prevents the degradation of iron-related mRNAs, leading to increased synthesis of iron uptake proteins and decreased synthesis of iron storage proteins. Conversely, when iron levels are high, IRP2 is degraded, allowing for the normal turnover and translation of these mRNAs.

IRP2 plays a crucial role in maintaining appropriate intracellular iron concentrations and protecting cells from iron-induced oxidative stress. Dysregulation of IRP2 has been implicated in various diseases, including anemia, neurodegenerative disorders, and cancer.

Bloodletting is a medical procedure that was commonly used in the past to balance the four humors of the body, which were believed to be blood, phlegm, black bile, and yellow bile. The procedure involved withdrawing blood from a patient through various methods such as venesection (making an incision in a vein), leeches, or cupping.

The theory behind bloodletting was that if one humor became overabundant, it could cause disease or illness. By removing some of the excess humor, practitioners believed they could restore balance and promote healing. Bloodletting was used to treat a wide variety of conditions, including fever, inflammation, and pain.

While bloodletting is no longer practiced in modern medicine, it was once a common treatment for many different ailments. The practice dates back to ancient times and was used by various cultures throughout history, including the Greeks, Romans, Egyptians, and Chinese. However, its effectiveness as a medical treatment has been called into question, and it is now considered an outdated and potentially harmful procedure.

Iron-dextran complex is a parenteral preparation used as an iron supplement to treat or prevent iron deficiency anemia in patients who cannot take oral iron or do not respond well to oral iron therapy. The complex is formed by combining iron salts with dextran, a type of polysaccharide derived from cornstarch, which acts as a carrier and helps increase the solubility and stability of the iron.

The iron-dextran complex is available in various forms, including injectable solutions and intravenous (IV) infusions. It works by releasing iron ions slowly into the body, where they can be taken up by red blood cell precursors in the bone marrow and used to synthesize hemoglobin, a protein that carries oxygen in the blood.

It is important to note that iron-dextran complex can cause anaphylactic reactions in some individuals, so it should be administered with caution and under medical supervision. Patients should be monitored for signs of allergic reactions during and after administration, and appropriate measures should be taken if necessary.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Beta-thalassemia is a genetic blood disorder that affects the production of hemoglobin, a protein in red blood cells that carries oxygen throughout the body. Specifically, beta-thalassemia is caused by mutations in the beta-globin gene, which leads to reduced or absent production of the beta-globin component of hemoglobin.

There are two main types of beta-thalassemia:

1. Beta-thalassemia major (also known as Cooley's anemia): This is a severe form of the disorder that typically becomes apparent in early childhood. It is characterized by a significant reduction or absence of beta-globin production, leading to anemia, enlarged spleen and liver, jaundice, and growth retardation.
2. Beta-thalassemia intermedia: This is a milder form of the disorder that may not become apparent until later in childhood or even adulthood. It is characterized by a variable reduction in beta-globin production, leading to mild to moderate anemia and other symptoms that can range from nonexistent to severe.

Treatment for beta-thalassemia depends on the severity of the disorder and may include blood transfusions, iron chelation therapy, and/or bone marrow transplantation. In some cases, genetic counseling and prenatal diagnosis may also be recommended for families with a history of the disorder.

Hepcidin is a peptide hormone primarily produced in the liver that plays a crucial role in regulating iron homeostasis within the body. It acts by inhibiting the absorption of dietary iron in the intestines and the release of iron from storage sites, such as macrophages, into the bloodstream. By reducing the amount of iron available for use, hepcidin helps prevent excessive iron accumulation in tissues, which can be harmful and contribute to the development of various diseases, including iron overload disorders and certain types of anemia. The production of hepcidin is regulated by several factors, including iron levels, inflammation, and erythropoiesis (the production of red blood cells).

Hemosiderosis is a medical condition characterized by the abnormal accumulation of hemosiderin, an iron-containing protein, in various organs and tissues of the body. Hemosiderin is derived from the breakdown of hemoglobin, which is the oxygen-carrying protein in red blood cells. When there is excessive breakdown of red blood cells or impaired clearance of hemosiderin, it can lead to its accumulation in organs such as the liver, spleen, and lungs.

Hemosiderosis can be classified into two types: primary and secondary. Primary hemosiderosis is a rare condition that is caused by genetic disorders affecting red blood cells, while secondary hemosiderosis is more common and is associated with various conditions that cause excessive breakdown of red blood cells or chronic inflammation. These conditions include hemolytic anemias, repeated blood transfusions, liver diseases, infections, and certain autoimmune disorders.

The accumulation of hemosiderin can lead to tissue damage and organ dysfunction, particularly in the lungs, where it can cause pulmonary fibrosis, and in the heart, where it can lead to heart failure. Hemosiderosis is typically diagnosed through a combination of medical history, physical examination, and laboratory tests, including blood tests and imaging studies such as chest X-rays or MRI scans. Treatment of hemosiderosis depends on the underlying cause and may include medications, blood transfusions, or supportive care to manage symptoms and prevent complications.

An encyclopedia is a comprehensive reference work containing articles on various topics, usually arranged in alphabetical order. In the context of medicine, a medical encyclopedia is a collection of articles that provide information about a wide range of medical topics, including diseases and conditions, treatments, tests, procedures, and anatomy and physiology. Medical encyclopedias may be published in print or electronic formats and are often used as a starting point for researching medical topics. They can provide reliable and accurate information on medical subjects, making them useful resources for healthcare professionals, students, and patients alike. Some well-known examples of medical encyclopedias include the Merck Manual and the Stedman's Medical Dictionary.

"Ferritin - Homo sapiens (Human)". Look up ferritin or apoferritin in Wiktionary, the free dictionary. Ferritins at the U.S. ... Iron is released from ferritin for use by ferritin degradation, which is performed mainly by lysosomes. Vertebrate ferritin ... Plasma ferritin is also an indirect marker of the total amount of iron stored in the body; hence, serum ferritin is used as a ... Each ferritin complex can store about 4500 iron (Fe3+) ions. A human mitochondrial ferritin, MtF, was found to express as a pro ...
... is a ferroxidase enzyme that in humans is encoded by the FTMT gene. It is classified as a metal-binding ... 2007). "Ferritin: a novel mechanism for delivery of iron to the brain and other organs". Am. J. Physiol., Cell Physiol. 293 (2 ... 2002). "Mitochondrial ferritin: a new player in iron metabolism". Blood Cells Mol. Dis. 29 (3): 376-83. doi:10.1006/bcmd. ... After the protein is taken up by the mitochondria it can be processed into a mature protein and assemble functional ferritin ...
... is a protein that in humans is encoded by the FTL gene. Ferritin is the major protein responsible for ... Although the ferritin light chain unlike the ferritin heavy chain has no ferroxidase activity, the light chain may be ... Ferritin light chain has been shown to interact with FTH1. An oxygen molecule acts as the terminal electron acceptor during the ... The rates of iron uptake and release may be affected by changes to the components of the ferritin light chains and heavy chains ...
... is a protein that in humans is encoded by the FTH1P3 gene. "Human PubMed Reference:". ... "Entrez Gene: Ferritin heavy chain 1 pseudogene 3". Retrieved 2018-03-15. Di Sanzo M, Aversa I, Santamaria G, Gagliardi M, ... Panebianco M, Biamonte F, Zolea F, Faniello MC, Cuda G, Costanzo F (2016). "FTH1P3, a Novel H-Ferritin Pseudogene ...
Ferritin level above 200 ng/mL (449 pmol/L) in women or 300 ng/mL (674 pmol/L) in men who have no signs of inflammatory disease ... Serum ferritin concentration is likely to be high in persons with Q248H (mostly heterozygotes) than in wild-type SLC40A1. In ... Measurement of serum ferritin indicates for total body iron overload. Liver biopsy measures the iron concentration of liver. It ... "Ferritin". MedlinePlus. Retrieved 9 April 2014. "Iron (Fe)". Web MD. Retrieved 9 April 2014. McLaren, CE; Barton, JC; Adams, PC ...
Granick, S. (1942). "Ferritin I. Physical and chemical properties of horse spleen ferritin". J. Biol. Chem. 146 (2): 451]461. ... In the first paper, Granick showed that contrary to earlier studies purified ferritin contains no nucleic acid and varies in ... A second paper, by Granick and Michaelis, showed that iron could be removed from ferritin to produce apoferritin. Granick went ... Sam Granick (February 16, 1909 - April 29, 1977) was an American biochemist known for his studies of ferritin and iron ...
serum ferritin; This protein helps store iron in the body, a low levels of ferritin usually indicates a low levels of stored ...
Bernard, George W.; Carranza, Ferritin A.; Jovanovic, Sascha A. (1996). "Biologic Aspects of Dental Implants". In Carranza, ...
More ferritin is produced to suppress oxidative cell damage, although the amount of ferritin that cells can accumulate is ... Blood tests may show high levels of ferritin and low, normal, or high levels of transferrin saturation, depending on the form ... Iron accumulates preferentially in Kupffer cells, which are located in the liver, and serum ferritin increases; less iron is ... Iron is stored in cells and blood serum in a protein called ferritin. Reticuloendothelial macrophages, which can phagocytose ...
... the serum ferritin level correlates with the degree of iron overload. Ferritin levels are usually monitored serially in those ... If the serum ferritin is greater than 1000 ug/L at diagnosis there is a risk of liver damage and cirrhosis which may eventually ... Serum ferritin testing is a low-cost, readily available, and minimally invasive method for assessing body iron stores. However ... Once the serum ferritin and transferrin saturation are within the normal range, maintenance phlebotomies may be needed in some ...
... tissue and the presence of disordered arrays of ferritin in SNc tissue. The hypothesis also predicted that disordered ferritin ... The hypothesis is based in part on the observation by many independent researchers that electron tunneling occurs in ferritin, ... Rourk, Christopher John (September 2018). "Ferritin and neuromelanin "quantum dot" array structures in dopamine neurons of the ... "Electrical Conductivity of Ferritin Proteins by Conductive AFM". Nano Letters. 5 (4): 571-577. Bibcode:2005NanoL...5..571X. doi ...
In IVF and ICSI, a risk factor is the decreased expression of proteins in energy metabolism; Ferritin light chain and ATP5A1. ...
H2O in the protein ferritin). In terms of taxonomic distribution, the most common biominerals are the phosphate and carbonate ...
Instead, the patient would merely suffer a further drop in his already usually low ferritin level. Consequently, dialysis and ... 2010). "Prevalent Iron Metabolism Gene Variants Associated with Increased Brain Ferritin Iron in Healthy Older Men". J. ... and low ferritin value. Multiple tests are obligatory due to physiologically induced fluctuations. Mild persistent eosinophilia ... magnetic resonance and metabolic syndrome among outpatient referrals for elevated serum ferritin in the Basque Country". Annals ...
The metal micronutrients are taken up into organisms by specific transporters and bound to storage proteins such as ferritin or ... the protein ferritin plays an important role in controlling the distribution of iron. The abundant inorganic elements act as ... ferritin), and small molecules (e.g. siderophores) are employed to control metal ions concentration and bio-availability in ... H2O in the protein ferritin). Because extracellular iron is strongly involved in inducing calcification, its control is ...
... tissue and the presence of disordered arrays of ferritin in SNc tissue. The hypothesis also predicted that disordered ferritin ... Ho, Ru-Hung; Chen, Yu-Hung; Wang, Chong Mou (June 2012). "Surface differentiation of ferritin and apoferritin with atomic force ... Rourk, Christopher John (September 2018). "Ferritin and neuromelanin "quantum dot" array structures in dopamine neurons of the ... "Electrical Conductivity of Ferritin Proteins by Conductive AFM". Nano Letters. 5 (4): 571-577. doi:10.1021/nl048218x. ISSN 1530 ...
Further experiments have shown that ferritin structures similar to ones found in SNc tissue are able to conduct electrons over ... Experiments have shown that ferritin and neuromelanin in fixed human substantia nigra pars compacta (SNc) tissue are able to ... Both of these observations are consistent with earlier predictions that are part of a hypothesis that ferritin and neuromelanin ... Rourk, Christopher John (September 2018). "Ferritin and neuromelanin "quantum dot" array structures in dopamine neurons of the ...
Ferritin is an iron reservoir for an individual cell. It is found in all cells types and localized in the cytosol. Ferritin is ... Ferritin is used to diagnose low iron levels in humans. It can be used to indicate the level of bioavailable iron, which is ... Ferritin is a highly conserved protein through all domains of life. It is so conserved that subunits from horses and humans can ... "What Is a Ferritin Blood Test? What Do the Results Mean?". WebMD. Retrieved 2018-11-11. (CS1 maint: multiple names: authors ...
Bacterioferritin Transferrin Ferritin Ilari A, Stefanini S, Chiancone E, Tsernoglou D (January 2000). "The dodecameric ferritin ... A ferritin-like DNA-binding protein of Escherichia coli". The Journal of Biological Chemistry. 277 (31): 27689-96. doi:10.1074/ ... Grant RA, Filman DJ, Finkel SE, Kolter R, Hogle JM (April 1998). "The crystal structure of Dps, a ferritin homolog that binds ... Dps proteins belong to the ferritin superfamily and the DNA protection is afforded by means of a double mechanism: The first ...
Dysfunctional ferritin may accumulate as hemosiderin, which can be problematic in cases of iron overload. The ferritin storage ... Iron can be stored in ferritin as ferric iron due to the ferroxidase activity of the ferritin heavy chain. ... Both ferritin and ferroportin contain an IRE in their 5' UTRs, so that under iron deficiency their translation is repressed by ... At the bone marrow, transferrin is reduced from Fe3+ and Fe2+ and stored as ferritin to be incorporated into hemoglobin. The ...
Dysfunctional ferritin may accumulate as hemosiderin, which can be problematic in cases of iron overload. The ferritin storage ... Iron can be stored in ferritin as ferric iron due to the ferroxidase activity of the ferritin heavy chain. ... Both ferritin and ferroportin contain an IRE in their 5' UTRs, so that under iron deficiency their translation is repressed by ... The liver stores of ferritin are the primary physiologic source of reserve iron in the body. The reserves of iron in ...
The ideal is to increase the body's iron deposits, measured as levels of ferritin in serum, with the aim of reaching a ferritin ... Serum ferritin levels reflect the iron stores available in the body. The normal range is 20 to 200 ng/mL for men and 15 to 150 ... With ferritin levels higher than 100 ng/mL an increase in infections has been reported. Another way to treat LID is with an ... Serum ferritin falls to less than 20 ng/mL. Increased iron absorption, a compensatory change, results in an increased amount of ...
Quantum tunneling of the magnetization was reported in ferritin present in horse spleen proteins A direct measurement of the ... "Macroscopic Resonant Tunneling of Magnetization in Ferritin". Physical Review Letters. 79 (9): 1754-1757. Bibcode:1997PhRvL.. ...
Serum ferritin (the storage form of iron) is routinely measured in those with beta thalassemia to determine the degree of iron ... These tests include complete blood count; hemoglobin electrophoresis; serum transferrin, ferritin, total iron-binding capacity ... in adults with transfusion dependent beta thalassemia as compared to placebo and was also associated with decreased ferritin ... overload; with increased ferritin levels directing the use of iron chelation therapy. The three iron chelators; subcutaneous ...
This is true for ferritin levels and iron levels in the organs as well, it is important for patients to go regularly for ... "Ferritin: Reference Range, Interpretation, Collection and Panels". 2018-07-05. {{cite journal}}: Cite journal requires ,journal ... than to simply get regular blood tests to check ferritin levels, which only show a trend, and do not reflect actual organ iron ... hematologists generally do not begin chelation therapy until ferritin levels reach at least 1000 ng/ml. It is more important to ...
The ferritin is composed of 24 subunits of protein complex and a small iron oxide core. The core of the ferritin is in the form ... There has been attempts to overcome these intrinsic physical limits of the ferritin. One approach is the use of magnetic ... Jutz G, van Rijn P, Santos Miranda B, Böker A (February 2015). "Ferritin: a versatile building block for bionanotechnology". ... One approach involves synthesizing the fusion protein of ion channels with iron containing proteins such as ferritins to ...
Feldherr, C M (1962). "The Intracellular Distribution of Ferritin Following Microinjection". J Cell Biol. 12 (1): 159-167. doi: ... Examples include amoeba microinjected with ferritin and mouse eggs microinjected with bovine albumin. Because proteins have ...
Balla G, Jacob HS, Balla J, Rosenberg M, Nath K, Apple F, Eaton JW, Vercellotti GM (Sep 1992). "Ferritin: a cytoprotective ... Furthermore, part of antioxidants properties of NO is attributable to up-regulation of heme-oxygenase-I and ferritin expression ...
It is also bound to ferritin for storage. Maltol reaches its highest plasma concentrations after 1 to 1.5 hours. It is quickly ...
... ferritin is normal or high, reflecting the fact that iron is sequestered within cells, and ferritin is being produced as an ... In iron deficiency anemia (IDA) ferritin is low. Total iron-binding capacity (TIBC) is high in iron deficiency, reflecting ...
"Ferritin - Homo sapiens (Human)". Look up ferritin or apoferritin in Wiktionary, the free dictionary. Ferritins at the U.S. ... Iron is released from ferritin for use by ferritin degradation, which is performed mainly by lysosomes. Vertebrate ferritin ... Plasma ferritin is also an indirect marker of the total amount of iron stored in the body; hence, serum ferritin is used as a ... Each ferritin complex can store about 4500 iron (Fe3+) ions. A human mitochondrial ferritin, MtF, was found to express as a pro ...
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... EMBO Rep. 2020 Nov 5;21(11):e50202. doi: 10.15252/embr ... Deferiprone, an iron chelator, treatment resulted in the increased expression of mitochondrial ferritin (FTMT) and the ...
LBXFER - Ferritin (ng/mL). Variable Name: LBXFER SAS Label: Ferritin (ng/mL). English Text: Ferritin (ng/mL). Target: Both ... LBDFERSI - Ferritin (ug/L). Variable Name: LBDFERSI. SAS Label: Ferritin (ug/L). English Text: Ferritin (ug/L). Target: Both ... The 1st incubation uses 10 uL of sample, a ferritin-specific antibody and a labeled ferritin-specific antibody to form a ... A crossover study was performed to compare the 2009-2010 Ferritin data to the 2007-2008 Ferritin data. The Roche Hitachi 912 ...
Doctors may order a ferritin test when they suspect kids have too little or too much iron in their bodies. ... What Is a Ferritin Test?. Ferritin is the protein inside of red blood cells that stores iron. A ferritin (FAIR-eh-tin) test ... This can affect the ferritin test.. Why Are Ferritin Tests Done?. Having a low number of red blood cells is called anemia. It ... Doctors may order a ferritin test to check for too little or too much iron in the body. A ferritin test can help doctors see if ...
ferritin heavy chain. Names. H-ferritin. ferritin H subunit. ferritin heavy chain 1. NP_034369.1. *EC 1.16.3.1 ... Iron and Ferritin Modulate MHC Class I Expression and NK Cell Recognition. Title: Iron and Ferritin Modulate MHC Class I ... H-Ferritin is essential for macrophages capacity to store or detoxify exogenously added iron. Title: H-Ferritin is essential ... Fth1 ferritin heavy polypeptide 1 [Mus musculus] Fth1 ferritin heavy polypeptide 1 [Mus musculus]. Gene ID:14319 ...
Magnetogenetic cell activation using endogenous ferritin. Lisa Pomeranz, Rosemary Li, View ORCID ProfileXiaofei Yu, Leah Kelly ... Toward these ends, we first generated a novel anti-ferritin nanobody that when fused to transient receptor potential cation ... While prior studies have shown that magnetic activation of ferritin-tagged ion channels allows cell-specific modulation of ... Together, the novel anti-ferritin nanobody, nanobody-TRPV1 construct and new hardware advance the utility of magnetogenetics in ...
A ferritin blood test can tell whether you are getting too much or too little iron. Learn more. ... Ferritin is a protein that stores iron in your cells. ... Other names: serum ferritin, serum ferritin level, ferritin ... What is a Ferritin Blood Test?. A ferritin blood test measures the level of ferritin in your blood. Ferritin is a protein that ... Ferritin, Serum; 296 p.. *Mayo Clinic [Internet]. Mayo Foundation for Medical Education and Research; c1998-2022. Ferritin Test ...
Ferritin is a protein found inside cells that stores iron for the bodys future use. A ferritin test indirectly measures the ... Ferritin levels can become elevated if the patient has an inflammatory disorder. ... Retrieved from http://drmyhill.co.uk/drmyhill/index.php?title=Ferritin_levels_in_serum&oldid=22881 ...
More info for Fold a.25: Ferritin-like. Timeline for Fold a.25: Ferritin-like: *Fold a.25: Ferritin-like first appeared (with ... Fold a.25: Ferritin-like appears in SCOPe 2.03. *Fold a.25: Ferritin-like appears in SCOPe 2.05. *Fold a.25: Ferritin-like ... hetero)dimer of alpha-hairpin subunits similar to that of the half-ferritin family; no bound metals inside the bundle. ... a.25.1: Ferritin-like [47240] (10 families) contains bimetal-ion centre in the middle of the bundle. ...
Ferritin). Cat# MBS656884. Supplier: MyBiosource. Available at Gentaur Genprice in 5 to 7 Working Days. Place your Order Online ... MBS656884 , Laburnum alpinum (LAA) (Ferritin) MyBiosource Lectins MBS656884 , Laburnum alpinum (LAA) (Ferritin). (No reviews ... MBS656884 , Laburnum alpinum (LAA) (Ferritin). Rating Required Select Rating. 1 star (worst). 2 stars. 3 stars (average). 4 ...
What is ferritin made from?. The unique structure of ferritin forms a spherical shell in which the iron is "stored" as Fe(III) ... What is ferritin function?. Ferritin is a protein that stores iron inside your cells. You need iron to make healthy red blood ... What is ferritin normal level?. The normal range for blood ferritin is: For men, 24 to 336 micrograms per liter. For women, 11 ... What causes high ferritin levels?. The most common causes of elevated ferritin levels are obesity, inflammation, and daily ...
A Ferritin (Iron) Blood Test In Austell Can Monitor Your Iron Levels And Confirm A Deficiency. ... Ferritin is a protein in the body that binds to iron. The level of ferritin correlates with the total amount of iron stored in ... Liver dysfunction can cause elevated ferritin levels because the liver is unable to clear it from the body. Ferritin may also ... The Ferritin Test measures the level of ferritin molecules in the blood. ...
SDS-CGE is effective in quickly resolving the H- and L-subunits of ferritins from horse spleen, human liver, recombinant human ... In addition, the H- and L-subunits of ferritin are fairly close in molecular weight (∼21,000 and ∼20,000, respectively) and are ... Traditionally, SDS-PAGE has been used to characterize the H- and L-subunit ratios in ferritin; however, this technique is ... Most commercial horse spleen ferritins lacked intact H-subunits under denaturing conditions. ...
Serum total cholesterol and ferritin and blood haemoglobin concentrations in primary schoolchildren. ... Serum total cholesterol and ferritin and blood haemoglobin concentrations in primary schoolchildren. ...
Ferritin from Reuber H-35 hepatomas was compared with ferritin from livers of ACI rats, the strain of rats in which the ... Ferritin from Reuber H-35 hepatomas was compared with ferritin from livers of ACI rats, the strain of rats in which the ... The isoelectric points of these two proteins are 5.20 ± 0.02 (H-35 ferritin) and 4.95 ± 0.03 (ACI liver ferritin). The amino ... Distinctive Properties of Ferritin from the Reuber H-35 Rat Hepatoma1 Joseph C. K. Lee; Joseph C. K. Lee ...
In epidemiological studies, serum ferritin was the second-strongest determinant of blood glucose (after BMI) in regression ... In epidemiological studies, serum ferritin was the second-strongest determinant of blood glucose (after BMI) in regression ... Serum Ferritin as a Component of the Insulin Resistance Syndrome José-Manuel Fernández-Real, MD; José-Manuel Fernández-Real, MD ... and S1 suggest that serum ferritin could be a marker of the insulin resistance syndrome. Serum ferritin may also be an ...
Ferritin is a 24-subunit protein composed of two types of subunits: ferritin heavy chain and ferritin light chain. The source ... Clinical characteristics according to the ferritin-to-hemoglobin ratio. Variables. Ferritin/. hemoglobin ,13 (n = 63). Ferritin ... The ferritin-to-hemoglobin ratio is calculated by dividing the ferritin level, which increases with tumor progression, by the ... The ferritin level, hemoglobin level, and ferritin-to-hemoglobin ratio at the initiation of treatment were investigated. After ...
In this report, we describe formulation development and comparability studies with a self-assembled SARS-CoV-2 spike ferritin ... Formulation development and comparability studies with an aluminum-salt adjuvanted SARS-CoV-2 Spike ferritin nanoparticle ...
Ferritin concentration was significantly related to absorbable iron (r=.72) and total iron (r=.70) intake. The results suggest ... Food diaries revealed lower daily absorbable iron intake by the low femtin group compared to the normal ferritin group. ... plasma ferritin concentrations were studied while performing a VO2max and an endurance test (80% VO2max) on a cycle ergometer. ... Ferritin concentration was significantly related to absorbable iron (r=.72) and total iron (r=.70) intake. The results suggest ...
In this study, we performed a systematic review and meta-analysis to compare IL-6, ferritin and LDH in VTE and non-VTE COVID-19 ... Meta-analysis was then conducted to compare levels of IL-6, ferritin and LDH between the two groups. We finally included and ... It has been proved that interleukin-6 (IL-6), ferritin and lactate dehydrogenase (LDH) may play an important role in the ... Therefore, close monitoring of changes in IL-6 and ferritin concentrations is of great value in assisting clinicans to rapidly ...
Antioxidant action of L-alanine: Heme oxygenase-1 and ferritin as possible mediators. Biochemical and Biophysical Research ... Antioxidant action of L-alanine : Heme oxygenase-1 and ferritin as possible mediators. In: Biochemical and Biophysical Research ... Antioxidant action of L-alanine: Heme oxygenase-1 and ferritin as possible mediators. / Grosser, Nina; Oberle, Stefanie; Berndt ... The present study demonstrates that L-alanine stimulates expression of the antioxidant defense proteins HO-1 and ferritin in ...
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Plant ferritins are targeted to mitochondria as well as to chloroplasts. AtFer4 is the Arabidopsis thaliana ferritin isoform ... Plant ferritins are targeted to mitochondria as well as to chloroplasts. AtFer4 is the Arabidopsis thaliana ferritin isoform ... Ferritins are iron-storage proteins involved in the environmental and developmental control of the free iron pool within cells ... Ferritins are iron-storage proteins involved in the environmental and developmental control of the free iron pool within cells ...
Keywords : Non-Hodgkin Lymphoma, C-reactive protein, Beta 2 microglobulin, Ferritin, Lactate dehydrogenase, Serum specific ... Conclusions: We are in the opinion that serum ferritin and CRP parameters may be used as tumor markers and may be indicators in ... Results: Post-treatment serum ferritin and CRP levels were found to be significantly decreased in patients with NHL compared to ... Objective: The aim of this study was to measure serum C reactive protein, β2 microglobulin, ferritin, lactate dehydrogenase, ...
Buy an iron, TIBC and ferritin panel online from Quest®! ... What can cause a high ferritin level? Ferritin isnt solely a ... Ferritin is a protein in the blood that contains iron and helps you understand how much iron your body is storing. If your iron ... Iron, TIBC & Ferritin Panel. Measure the amount of iron in your blood, how well your blood transports iron, and the amount of ... If your ferritin levels are higher than normal, you may have an underlying condition that causes your body to store too much ...
The correlation of serum ferritin to body iron stores still exists, however, it is set at a higher level of serum ferritin. ... Each ferritin molecule is thought to consist of a spherical protein shell of molecular weight about 460 000 daltons made up of ... Ferritin is a high-molecular weight iron-containing protein that functions in the body as an iron storage compound. ... About two-thirds of the iron stores in the human body exist in the form of ferritin. The remaining iron stores are contained in ...
The Performance of the Point of Care Test (POCT) i-CHROMA Ferritin Method and other Methods Enrolled in the RIQAS. 더 보기 ... Assessment of Iron Deficiency in Pregnant Women by Using Soluble Transferrin Receptor - Ferritin Index. 더 보기 ... The Performance of the Point of Care Test (POCT) i-CHROMA Ferritin Method and other Methods Enrolled in the RIQAS ... Assessment of Iron Deficiency in Pregnant Women by Using Soluble Transferrin Receptor - Ferritin Index ...
... with the most common form being ferritin (accounting... ... What is ferritin? Approximately 25% of the iron in a normal ... Ferritin analyses provide a sensitive, specific, and reliable measurement for determining iron deficiency at an early stage, ... adult is present in a storage form (2), with the most common form being ferritin (accounting for about 2/3 of storage iron). ...
3.5.4. Ferritin. Ferritin is the main iron storage protein. It is necessary for iron homeostasis and participates in a wide ... Ferritin. M 20-250 µg/L,. F 10-120 µg/L. Controversial. Oxidative stress. Cardiometabolic disorders. [57,129,130]. ... High serum ferritin levels are associated with SVD, coronary heart disease, cancer, and adverse outcomes after stem cell ... It is synthesized in hepatocytes [129]. The serum ferritin level is mainly used as a biomarker of total iron reserves in the ...

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