Transferrin
Receptors, Transferrin
Iron
Transferrins
Ferritins
Iron Radioisotopes
Transferrin-Binding Proteins
Endocytosis
Lactoferrin
Hemochromatosis
Endosomes
Transferrin-Binding Protein B
Apoproteins
Transferrin-Binding Protein A
Gallium
Anemia, Iron-Deficiency
Bacterial Transferrin Receptor Complex
Iron-Regulatory Proteins
Iron Chelating Agents
Iron Overload
Receptors, Cell Surface
Reticulocytes
Hepcidins
Coated Pits, Cell-Membrane
Deferoxamine
Anemia, Hypochromic
Hemoglobins
Clathrin
Biological Transport
Iron Regulatory Protein 1
Siderophores
Cell Membrane
Cell Compartmentation
Gallium Radioisotopes
Serum Albumin
Membrane Proteins
Molecular Sequence Data
Protein Binding
rab4 GTP-Binding Proteins
Iron, Dietary
rab GTP-Binding Proteins
Nephelometry and Turbidimetry
Erythrocyte Indices
Clathrin-Coated Vesicles
Antimicrobial Cationic Peptides
Iron Isotopes
Amino Acid Sequence
Sertoli Cells
Blood Proteins
Erythropoiesis
Isoelectric Focusing
Histocompatibility Antigens Class I
Asialoglycoproteins
The effect of chelating agents on iron mobilization in Chang cell cultures. (1/3281)
The investigation of chelating agents with potential therapeutic value in patients with transfusional iron overload has been facilitated by the use of Chang cell cultures. These cells have been incubated with [59Fe]transferrin for 22 hr, following which most of the intracellular radioiron is found in the cytosol, distributed between a ferritin and a nonferritin form. Iron release from the cells depends on transferrin saturation in the medium, but when transferrin is 100% saturated, which normally does not allow iron release, desferrioxamine, 2,3-dihydroxybenzoic acid, rhodotorulic acid, cholythydroxamic acid, and tropolone all promote the mobilization of ferritin iron and its release from cells. They are effective to an approximately equal degree. The incubation of [59Fe]transferrin with tropolone in vitro at a molar ratio of 1:500 results in the transfer of most of the labeled iron to the chelator, reflecting the exceptionally high binding constant of this compound. How far these phenomena relate to therapeutic potentially remains to be seen. (+info)Studies of the binding of different iron donors to human serum transferrin and isolation of iron-binding fragments from the N- and C-terminal regions of the protein. (2/3281)
1. Trypsin digestion of human serum transferrin partially saturated with iron(III)-nitrilotriacetate at pH 5.5 or pH 8.5 produces a carbohydrate-containing iron-binding fragment of mol.wt. 43000. 2. When iron(III) citrate, FeCl3, iron (III) ascorabate and (NH4)2SO4,FeSO4 are used as iron donors to saturate the protein partially, at pH8.5, proteolytic digestion yields a fragment of mol.wt. 36000 that lacks carbohydrate. 3. The two fragments differ in their antigenic structures, amino acid compositions and peptide 'maps'. 4. The fragment with mol.wt. 36000 was assigned to the N-terminal region of the protein and the other to the C-terminal region. 5. The distribution of iron in human serum transferrin partially saturated with various iron donors was examined by electrophoresis in urea/polyacrylamide gels and the two possible monoferric forms were unequivocally identified. 6. The site designated A on human serum transferrin [Harris (1977) Biochemistry 16, 560--564] was assigned to the C-terminal region of the protein and the B site to the N-terminal region. 7. The distribution of iron on transferrin in human plasma was determined. (+info)The staphylococcal transferrin-binding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase. (3/3281)
Staphylococcus aureus and Staphylococcus epidermidis possess a 42-kDa cell wall transferrin-binding protein (Tpn) which is involved in the acquisition of transferrin-bound iron. To characterize this protein further, cell wall fractions were subjected to two-dimensional sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis blotted, and the N-terminus of Tpn was sequenced. Comparison of the first 20 amino acid residues of Tpn with the protein databases revealed a high degree of homology to the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Analysis of staphylococcal cell wall fractions for GAPDH activity confirmed the presence of a functional enzyme which, like Tpn, is regulated by the availability of iron in the growth medium. To determine whether Tpn is responsible for this GAPDH activity, it was affinity purified with NAD+ agarose. Both S. epidermidis and S. aureus Tpn catalyzed the conversion of glyceraldehyde-3-phosphate to 1,3-diphosphoglycerate. In contrast, Staphylococcus saprophyticus, which lacks a Tpn, has no cell wall-associated GAPDH activity. Native polyacrylamide gel electrophoresis of the affinity-purified Tpn revealed that it was present in the cell wall as a tetramer, consistent with the structures of all known cytoplasmic GAPDHs. Furthermore, the affinity-purified Tpn retained its ability to bind human transferrin both in its native tetrameric and SDS-denatured monomeric forms. Apart from interacting with human transferrin, Tpn, in common with the group A streptococcal cell wall GAPDH, binds human plasmin. Tpn-bound plasmin is enzymatically active and therefore may contribute to the ability of staphylococci to penetrate tissues during infections. These studies demonstrate that the staphylococcal transferrin receptor protein, Tpn, is a multifunctional cell wall GAPDH. (+info)Chemical and immunochemical measurement of total iron-binding capacity compared. (4/3281)
Radiometric, colorimetric, and two immunochemical methods for measuring total iron-binding capacity are compared. We evaluated the procedures on the basis of precision, applicability to a pediatric population, and accuracy as assessed by analytical recovery of purified transferrin. The immunoephelometric assay for transferrin provides significant advantages over the other methods examined. (+info)Effects of spinal cord injury on spermatogenesis and the expression of messenger ribonucleic acid for Sertoli cell proteins in rat Sertoli cell-enriched testes. (5/3281)
The study was an examination of the effects of spinal cord injury (SCI) on spermatogenesis and Sertoli cell functions in adult rats with Sertoli cell-enriched (SCE) testes. The effects of SCI on the seminiferous epithelium were characterized by abnormalities in the remaining spermatogenic cells during the first month after SCI. Three days after SCI, serum testosterone levels were 80% lower, while serum FSH and LH levels were 25% and 50% higher, respectively, than those of sham control SCE rats. At this time, the levels of mRNA for androgen receptor (AR), FSH receptor (FSH-R), and androgen-binding protein (ABP) were normal whereas those for transferrin (Trf) had decreased by 40%. Thereafter, serum testosterone levels increased, but they remained lower than those of the sham control rats 28 days after SCI; and serum FSH and LH levels returned to normal. The levels of mRNA for AR, ABP, and Trf exhibited a biphasic increase 7 days after SCI and remained elevated 28 days after SCI. FSH-R mRNA levels were also elevated 90 days after SCI. Unexpectedly, active spermatogenesis, including qualitatively complete spermatogenesis, persisted in > 40% of the tubules 90 days after SCI. These results suggest that the stem cells and/or undifferentiated spermatogonia in SCE testes are less susceptible to the deleterious effects of SCI than the normal testes and that they were able to proliferate and differentiate after SCI. The presence of elevated levels of mRNA for Sertoli cell FSH-R and AR, as well as of that for the Sertoli cell proteins, in the SCE testes during the chronic stage of SCI suggests a modification of Sertoli cell physiology. Such changes in Sertoli cell functions may provide a beneficial environment for the proliferation of the stem cells and differentiation of postmeiotic cells, thus resulting in the persistence of spermatogenesis in these testes. (+info)Coronary heart disease and iron status: meta-analyses of prospective studies. (6/3281)
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 iron transport protein NRAMP2 is an integral membrane glycoprotein that colocalizes with transferrin in recycling endosomes. (7/3281)
The natural resistance associated macrophage protein (Nramp) gene family is composed of two members in mammals, Nramp1 and Nramp2. Nramp1 is expressed primarily in macrophages and mutations at this locus cause susceptibility to infectious diseases. Nramp2 has a much broader range of tissue expression and mutations at Nramp2 result in iron deficiency, indicating a role for Nramp2 in iron metabolism. To get further insight into the function and mechanism of action of Nramp proteins, we have generated isoform specific anti-Nramp1 and anti-Nramp2 antisera. Immunoblotting experiments indicate that Nramp2 is present in a number of cell types, including hemopoietic precursors, and is coexpressed with Nramp1 in primary macrophages and macrophage cell lines. Nramp2 is expressed as a 90-100-kD integral membrane protein extensively modified by glycosylation (>40% of molecular mass). Subcellular localization studies by immunofluorescence and confocal microscopy indicate distinct and nonoverlapping localization for Nramp1 and Nramp2. Nramp1 is expressed in the lysosomal compartment, whereas Nramp2 is not detectable in the lysosomes but is expressed primarily in recycling endosomes and also, to a lower extent, at the plasma membrane, colocalizing with transferrin. These findings suggest that Nramp2 plays a key role in the metabolism of transferrin-bound iron by transporting free Fe2+ across the endosomal membrane and into the cytoplasm. (+info)Acute haemodynamic and proteinuric effects of prednisolone in patients with a nephrotic syndrome. (8/3281)
BACKGROUND: Administration of prednisolone causes an abrupt rise in proteinuria in patients with a nephrotic syndrome. METHODS: To clarify the mechanisms responsible for this increase in proteinuria we have performed a placebo controlled study in 26 patients with a nephrotic syndrome. Systemic and renal haemodynamics and urinary protein excretion were measured after prednisolone and after placebo. RESULTS: After i.v. administration of 125-150 mg prednisolone total proteinuria increased from 6.66+/-4.42 to 9.37+/-6.07 mg/min (P<0.001). By analysing the excretion of proteins with different charge and weight (albumin, transferrin, IgG, IgG4 and beta2-microglobulin) it became apparent that the increase of proteinuria was the result of a change in size selectivity rather than a change in glomerular charge selectivity or tubular protein reabsorption. Glomerular filtration rate rose from 83+/-34 ml to 95+/-43 ml/min (P<0.001) after 5 h, whereas effective renal plasma flow and endogenous creatinine clearance remained unchanged. As a result filtration fraction was increased, compatible with an increased glomerular pressure, which probably contributes to the size selectivity changes. Since corticosteroids affect both the renin-angiotensin system and renal prostaglandins, we have evaluated the effects of prednisolone on proteinuria after pretreatment with 3 months of the angiotensin-converting enzyme inhibitor lisinopril or after 2 weeks of the prostaglandin synthesis inhibitor indomethacin. Neither drug had any effect on prednisolone-induced increases of proteinuria. CONCLUSIONS: Prednisolone increases proteinuria by changing the size selective barrier of the glomerular capillary. Neither the renin-angiotensin axis nor prostaglandins seem to be involved in these effects of prednisolone on proteinuria. (+info)Hereditary Hemochromatosis (HH):
Hereditary hemochromatosis is an inherited disorder that affects the body's ability to absorb iron. It is caused by a genetic mutation in the HFE gene, which codes for a protein involved in iron absorption. The mutated protein leads to excessive iron accumulation in the body, especially in the liver, pancreas, and other organs.
Symptoms of HH typically appear in adulthood and may include:
1. Fatigue and weakness
2. Joint pain and swelling
3. Abdominal discomfort and weight loss
4. Skin bronzing or darkening
5. Diabetes mellitus (type 2)
6. Heart problems, such as arrhythmias and heart failure
7. Liver cirrhosis and liver cancer
8. Infertility and sexual dysfunction
Acquired Hemochromatosis (AH):
Acquired hemochromatosis is a condition that develops in people who have chronic iron overload due to blood transfusions or other medical conditions that cause excessive iron accumulation. It can also occur in people with certain genetic mutations that affect iron metabolism.
Symptoms of AH may include:
1. Fatigue and weakness
2. Joint pain and swelling
3. Abdominal discomfort and weight loss
4. Skin bronzing or darkening
5. Diabetes mellitus (type 2)
6. Heart problems, such as arrhythmias and heart failure
7. Liver cirrhosis and liver cancer
8. Infertility and sexual dysfunction
Diagnosis of Hemochromatosis:
Hemochromatosis can be diagnosed through a combination of blood tests, imaging studies, and biopsies.
Blood Tests:
1. Serum iron and transferrin saturation: These tests measure the levels of iron in the blood and how well it is bound to transferrin, a protein that carries iron throughout the body. High levels of iron and low transferrin saturation can indicate hemochromatosis.
2. Ferritin: This test measures the level of ferritin, a protein that stores iron in the body. High levels of ferritin can indicate hemochromatosis.
3. Transferrin receptor gene analysis: This test can identify specific genetic mutations that cause hemochromatosis.
Imaging Studies:
1. Ultrasound: An ultrasound of the liver can show signs of cirrhosis or other liver damage caused by hemochromatosis.
2. CT or MRI scans: These tests can provide detailed images of the liver and other organs and tissues, helping doctors identify any damage caused by excessive iron accumulation.
Biopsies:
1. Liver biopsy: A liver biopsy involves removing a small sample of liver tissue for examination under a microscope. This test can help diagnose hemochromatosis and assess the extent of liver damage.
2. Biopsy of other organs: Biopsies of other organs, such as the pancreas or joints, may be performed to assess damage caused by hemochromatosis in these tissues.
It's important to note that not everyone with hemochromatosis will require all of these tests, and your healthcare provider will determine which tests are appropriate for you based on your symptoms and medical history.
Prevalence: Iron deficiency anemia is one of the most common nutritional disorders worldwide, affecting approximately 1.6 billion people, with women being more likely to be affected than men.
Causes: The main cause of iron deficiency anemia is a diet that does not provide enough iron. Other causes include:
* Poor absorption of iron from the diet
* Increased demand for iron due to growth or pregnancy
* Blood loss due to menstruation, internal bleeding, or surgery
* Chronic diseases such as kidney disease, cancer, and rheumatoid arthritis
Signs and symptoms: The signs and symptoms of iron deficiency anemia may include:
* Fatigue and weakness
* Pale skin
* Shortness of breath
* Dizziness or lightheadedness
* Headaches
* Cold hands and feet
Diagnosis: Iron deficiency anemia is diagnosed based on a physical exam, medical history, and laboratory tests, including:
* Complete blood count (CBC) to check for low red blood cell count and low hemoglobin level
* Serum iron and transferrin tests to check for low iron levels
* Ferritin test to check for low iron stores
Treatment: Treatment of iron deficiency anemia involves correcting the underlying cause, which may include:
* Dietary changes to increase iron intake
* Iron supplements to replenish iron stores
* Addressing any underlying causes such as bleeding or malabsorption
Complications: Iron deficiency anemia can lead to complications such as:
* Heart failure
* Increased risk of infections
* Poor cognitive function and development in children
Prevention: Preventing iron deficiency anemia involves consuming enough iron through a balanced diet, avoiding foods that inhibit iron absorption, and addressing any underlying causes. It is also important to maintain good overall health, including managing chronic conditions such as bleeding or malabsorption.
Symptoms of iron overload can include fatigue, weakness, joint pain, and abdominal discomfort. Treatment for iron overload usually involves reducing iron intake and undergoing regular phlebotomy (blood removal) to remove excess iron from the body. In severe cases, iron chelation therapy may be recommended to help remove excess iron from tissues and organs.
In addition to these medical definitions and treatments, there are also some key points to keep in mind when it comes to iron overload:
1. Iron is essential for human health, but too much of it can be harmful. The body needs a certain amount of iron to produce hemoglobin, the protein in red blood cells that carries oxygen throughout the body. However, excessive iron levels can damage organs and tissues.
2. Hereditary hemochromatosis is the most common cause of iron overload. This genetic disorder causes the body to absorb too much iron from food, leading to its accumulation in organs and tissues.
3. Iron overload can increase the risk of certain diseases, such as liver cirrhosis, diabetes, and heart disease. It can also lead to a condition called hemosiderosis, which is characterized by the deposition of iron in tissues and organs.
4. Phlebotomy is a safe and effective treatment for iron overload. Regular blood removal can help reduce excess iron levels and prevent complications such as liver damage, heart failure, and anemia.
5. Iron chelation therapy may be recommended in severe cases of iron overload. This involves using drugs to remove excess iron from tissues and organs, but it is not always necessary and can have potential side effects.
In hypochromic anemia, the RBCs are smaller than normal and have a lower concentration of hemoglobin. This can lead to a decrease in the amount of oxygen being carried to the body's tissues, which can cause fatigue, weakness, and shortness of breath.
There are several possible causes of hypochromic anemia, including:
1. Iron deficiency: Iron is essential for the production of hemoglobin, so a lack of iron can lead to a decrease in hemoglobin levels and the development of hypochromic anemia.
2. Vitamin deficiency: Vitamins such as vitamin B12 and folate are important for the production of red blood cells, so a deficiency in these vitamins can lead to hypochromic anemia.
3. Chronic disease: Certain chronic diseases, such as kidney disease, rheumatoid arthritis, and cancer, can lead to hypochromic anemia.
4. Inherited disorders: Certain inherited disorders, such as thalassemia and sickle cell anemia, can cause hypochromic anemia.
5. Autoimmune disorders: Autoimmune disorders, such as autoimmune hemolytic anemia, can cause hypochromic anemia by destroying red blood cells.
Hypochromic anemia is typically diagnosed through a combination of physical examination, medical history, and laboratory tests such as complete blood counts (CBCs) and serum iron studies. Treatment depends on the underlying cause of the anemia and may include dietary changes, supplements, medication, or blood transfusions.
There are many different types of anemia, each with its own set of causes and symptoms. Some common types of anemia include:
1. Iron-deficiency anemia: This is the most common type of anemia and is caused by a lack of iron in the diet or a problem with the body's ability to absorb iron. Iron is essential for making hemoglobin.
2. Vitamin deficiency anemia: This type of anemia is caused by a lack of vitamins, such as vitamin B12 or folate, that are necessary for red blood cell production.
3. Anemia of chronic disease: This type of anemia is seen in people with chronic diseases, such as kidney disease, rheumatoid arthritis, and cancer.
4. Sickle cell anemia: This is a genetic disorder that affects the structure of hemoglobin and causes red blood cells to be shaped like crescents or sickles.
5. Thalassemia: This is a genetic disorder that affects the production of hemoglobin and can cause anemia, fatigue, and other health problems.
The symptoms of anemia can vary depending on the type and severity of the condition. Common symptoms include fatigue, weakness, pale skin, shortness of breath, and dizziness or lightheadedness. Anemia can be diagnosed with a blood test that measures the number and size of red blood cells, as well as the levels of hemoglobin and other nutrients.
Treatment for anemia depends on the underlying cause of the condition. In some cases, dietary changes or supplements may be sufficient to treat anemia. For example, people with iron-deficiency anemia may need to increase their intake of iron-rich foods or take iron supplements. In other cases, medical treatment may be necessary to address underlying conditions such as kidney disease or cancer.
Preventing anemia is important for maintaining good health and preventing complications. To prevent anemia, it is important to eat a balanced diet that includes plenty of iron-rich foods, vitamin C-rich foods, and other essential nutrients. It is also important to avoid certain substances that can interfere with the absorption of nutrients, such as alcohol and caffeine. Additionally, it is important to manage any underlying medical conditions and seek medical attention if symptoms of anemia persist or worsen over time.
In conclusion, anemia is a common blood disorder that can have significant health implications if left untreated. It is important to be aware of the different types of anemia, their causes, and symptoms in order to seek medical attention if necessary. With proper diagnosis and treatment, many cases of anemia can be successfully managed and prevented.
Transferrin
Transferrin saturation
Transferrin receptor
Transferrin receptor 2
Transferrin receptor 1
Soluble transferrin receptor
Beta-2 transferrin
Diferric-transferrin reductase
Carbohydrate deficient transferrin
Atransferrinemia
Hemochromatosis type 4
Cerebrospinal fluid leak
IGFBP3
Iron-responsive element-binding protein
Clement Finch
Human serum albumin
Melanotransferrin
Beta thalassemia
Indera Paul Singh
Composition of the human body
King brown snake
Hereditary haemochromatosis
Ruthenium anti-cancer drugs
GABARAP
Ulcerative colitis
Iron overload
Iron
Iron-binding proteins
Serum protein electrophoresis
Low-molecular-weight chromium-binding substance
Congenital Disorder of Glycosylation Transferrin
NHANES 2007-2008:
Transferrin Receptor Data Documentation, Codebook, and Frequencies
Human TfR (Transferrin R) Alexa Fluor® 405-conjugated Antibody FAB2474V-100UG: R&D Systems
"Preparation of a transferrin-targeted M13-based gene nanocarrier and e" by MOHAMMAD KHALAJKONDORI, MAHBOOBEH KAVOOSI et al.
Bovine Transferrin ELISA Kit | E-10TX | Immunology Consultatnt Laboratory
JCI Insight -
Classical and intermediate monocytes scavenge non-transferrin-bound iron and damaged erythrocytes
Transferrin - DiaSys Diagnostic Systems GmbH
Transferrin | Alensa IN
Sus scrofa (Pig) Recombinant Transferrin/TF Protein (His Tag) (from HEK293 Cells) | VWR
CDT Test - Carbohydrate-deficient Transferrin Test | Accesa Labs ®
What is non-transferrin-bound iron (NBTI)? • The Blood Project
Elisa Of Transferrin - Comptes rendus de l'Académie bulgare des Sciences ???
Enhancement of transient transfection with serum-free and blood-free transferrin
Heritability of serum iron, ferritin and transferrin saturation in a genetically isolated population, the Erasmus Rucphen...
Rational Design of a Transferrin-Binding Peptide Sequence Tailored to Targeted Nanoparticle Internalization
Self-Amplifying Iridium(III) Photosensitizer for Ferroptosis-Mediated Immunotherapy Against Transferrin Receptor-Overexpressing...
Nutritional Status Assessment in Adults: Background, Indications, Contraindications
COMPARISON OF SERUM ALANINTRANSFERASE, TRANSFERRIN AND LACTOGLOBULIN LEVELS IN CHRONIC HBV INFECTION AMONG HBeAg POSITIVE AND...
Pressure Injuries (Pressure Ulcers) and Wound Care: Practice Essentials, Background, Anatomy
Regional differences in late-onset iron deposition, ferritin, transferrin, astrocyte proliferation, and microglial activation...
Eccles:CB Cell Culture - OpenWetWare
Hyperphosphatemia Treatment & Management: Approach Considerations, Phosphate Binders, Increased Renal Excretion
Denmark Tumor Markers Testing Market High Growth Opportunities for Cancer Diagnostic Tests and Analyzers
Glossary of Hematology Terms | Internal Medicine | U of U School of Medicine
mordant - Ontology Report - Rat Genome Database
TFR2 gene: MedlinePlus Genetics
NIOSHTIC-2 Search Results - Full View
Receptor32
- The method for measurement of soluble transferrin receptor (sTfR) is immuno-turbidimetry using Roche kits on the Hitachi 912 clinical analyzer. (cdc.gov)
- Transferrin receptor-1 gene polymorphisms are associated with type 2 diabetes. (bsc.es)
- The Transferrin Receptor (TfR or TfR-1, designated CD71) is a type 2 transmembrane glycoprotein expressed on erythroid progenitors, muscle cells and proliferating cells as a 188 kDa disulfide-linked homodimer of 95 kDa monomers (1‑4). (rndsystems.com)
- These included the iron exporter ferroportin (FPN1), ferritin, transferrin receptor, putative transporters of non-transferrin-bound iron (NTBI), and receptors for damaged erythrocytes. (jci.org)
- Human transferrin receptor 1 (TfR1), also designated CD71, is a homodimeric type II membrane glycoprotein of 90-95 kDa. (hycultbiotech.com)
- This receptor binds two molecules of the serum iron-transport protein transferrin (Tf) and is internalised into endosomes that are acidified, resulting in the release of iron from Tf. (hycultbiotech.com)
- While there are thousands of receptors that can be present on a cell, the transferrin receptor 1 (TfR1) is ubiquitously expressed, as every cell requires extracellular iron for health and growth. (cellculturedish.com)
- This Interagency Agreement is intended to conduct activities that will harmonize assays measuring soluble transferrin receptor (STfR), an important indicator to assess the global burden of iron deficiency in children and women of childbearing age. (nih.gov)
- The transferrin receptor (TfR) is a promising target in cancer therapy owing to its overexpression in most solid tumors and on the blood-brain barrier. (unige.it)
- Self-Amplifying Iridium(III) Photosensitizer for Ferroptosis-Mediated Immunotherapy Against Transferrin Receptor-Overexpressing Cancer. (bvsalud.org)
- This work presents a ferrocene-containing Ir(III) photosensitizer (IrFc1) that can bind with transferrin and be transported into triple-negative breast cancer (TNBC) cells via a transferrin receptor -mediated pathway. (bvsalud.org)
- Normal human lamina propria lymphocytes are in a heightened state of activation compared with peripheral blood with regard to cell-surface activation antigen expression (transferrin receptor, interleukin-2 receptor, 4F2) and the increased spontaneous secretion of immunoglobulins in vitro. (nih.gov)
- Using fluorescence-activated cell-sorter analyses with subtraction of autofluorescence on a single-cell basis, increased expression of lymphocyte activation antigens (interleukin-2 receptor, transferrin receptor, 4F2) was found on the cell surface of isolated intestinal B cells, T cells, CD4+ T cells, and CD8+ T cells in both Crohn's disease and ulcerative colitis. (nih.gov)
- IMSEAR at SEARO: Change of serum transferrin receptor due to malarial infection, an experiment in Plasmodium gallinaceum infected chicken model. (who.int)
- BACKGROUND & OBJECTIVES: The serum transferrin receptor (sTfR) concentration in an individual reflects the extent of erythropoietic activity and is considered as an useful marker of iron deficiency independent of concurrent inflammation or infection. (who.int)
- METHODS: Here we performed an animal experiment to study the chronological change of serum transferrin receptor due to infection of Plasmodium gallinaceum. (who.int)
- 1. Clinical utility of serum soluble transferrin receptor levels and comparison with bone marrow iron stores as an index for iron-deficient erythropoiesis in a heterogeneous group of patients. (nih.gov)
- 2. Serum transferrin receptor. (nih.gov)
- 3. Serum transferrin receptor in children: usefulness for determinating the nature of anemia in infection. (nih.gov)
- 4. The usefulness of the serum transferrin receptor in detecting iron deficiency in the anemia of chronic disorders. (nih.gov)
- 5. Serum transferrin receptor, ferritin, and reticulocyte maturity indices during the first year of life in 'large' preterm infants. (nih.gov)
- 7. Usefulness of soluble transferrin receptor and ferritin in iron deficiency and chronic disease. (nih.gov)
- 8. Reticulocyte haemoglobin content vs. soluble transferrin receptor and ferritin index in iron deficiency anaemia accompanied with inflammation. (nih.gov)
- 9. Double diagnostic meaning of serum transferrin receptor in hemodialysis patients: two case reports. (nih.gov)
- 10. Serum transferrin receptor, serum ferritin and serum transferrin receptor-ferritin index in adults with iron deficiency anaemia. (nih.gov)
- 11. Transferrin receptor assay and zinc protoporphyrin as markers of iron-deficient erythropoiesis in end-stage renal disease patients. (nih.gov)
- 12. Single values of serum transferrin receptor and transferrin receptor ferritin index can be used to detect true and functional iron deficiency in rheumatoid arthritis patients with anemia. (nih.gov)
- 13. Serum soluble transferrin receptor in hypochromic microcytic anaemia. (nih.gov)
- 17. Serum transferrin receptor in children with respiratory infections. (nih.gov)
- 18. Improved preoperative iron status assessment by soluble transferrin receptor in elderly patients undergoing knee and hip replacement. (nih.gov)
- 19. Soluble transferrin receptor, ferritin and soluble transferrin receptor--Ferritin index in assessment of anaemia in rhaeumatoid arthritis. (nih.gov)
- 20. High serum transferrin receptor level in anemia of chronic disorders indicates coexistent iron deficiency. (nih.gov)
Saturation7
- In iron deficiency, transferrin levels are elevated, but the protein is less saturated with iron (serum iron and percent saturation of transferrin are decreased). (clinlabnavigator.com)
- Heritability of serum iron, ferritin and transferrin saturation in a genetically isolated population, the Erasmus Rucphen Family (ERF) Study. (ox.ac.uk)
- 0.0001) for transferrin saturation while adjusting for age, age(2) and sex. (ox.ac.uk)
- The HFE genotypes explained between 2 to 6% of the sex and age-adjusted variance in serum iron, ferritin and transferrin saturation. (ox.ac.uk)
- CONCLUSION: A substantial proportion of the variance of iron, ferritin and transferrin saturation can be explained by additive genetic effects, independent of sex and age. (ox.ac.uk)
- Publication: Elevated transferrin saturation, health-related quality of life and telomere length. (nih.gov)
- We sought to examine the relationship between elevated transferrin saturation (TS) and measures of health status (telomere length and patient-reported health-related quality of life) to assess whether elevated TS is associated with negative patient outcomes beyond increased risk for morbidity and mortality, using a cross-sectional analysis of the Hemochromatosis and Iron Overload Screening Study supplemented with assays for leukocyte telomere length in adults ≥25 years old (n = 669). (nih.gov)
Carbohydrate deficient t7
- We undertook a retrospective analysis of carbohydrate deficient transferrin analysis in PMM2-CDG patients managed at our clinical consortium sites to attempt to provide a natural history context for Taday et al. (biomedcentral.com)
- We undertook a retrospective analysis of clinically performed carbohydrate deficient transferrin analysis results of patients followed at Mayo clinic (Rochester, Minnesota, USA), Seattle Children's Hospital (Seattle, Washington, USA), and Children's Hospital of Philadelphia (Philadelphia, Pennsylvania, USA). (biomedcentral.com)
- We included all available carbohydrate deficient transferrin analysis results (average 3 measurements/patient, range 1-7 measurements). (biomedcentral.com)
- The CDT test measures the carbohydrate-deficient transferrin (CDT) blood level. (accesalabs.com)
- The CDT test is a blood test that measures the level of Carbohydrate-deficient Transferrin, Transferrin and %CDT levels. (accesalabs.com)
- The CDT test, also known as a CDT lab test, CDT level test, and a carbohydrate-deficient transferrin test, measures the CDT blood level. (accesalabs.com)
- Lacking carbohydrates, the amount of "carbohydrate-deficient" transferrin molecules as a percentage of all the transferrin molecules can be used as a marker for heavy drinking. (accesalabs.com)
Receptors4
- Transferrin has been identified as a therapeutic agent for the delivery of nanoparticles and small molecules due to the ability of transferrin to be covalently linked and also as a natural carrier of molecules for entering a cell through its receptors. (cellculturedish.com)
- 6. [Iron status with particular consideration of soluble transferrin receptors in children and youth with gastritis, with or without Helicobacter pylori infection]. (nih.gov)
- 14. Soluble transferrin receptors and comparison with bone marrow iron stores: comments on a study. (nih.gov)
- 16. The responses of serum transferrin receptors to iron supplements in subjects with iron-deficiency erythropoiesis and iron-deficiency anaemia. (nih.gov)
Uptake1
- As the major mediator of cellular iron uptake, it binds and internalizes diferric transferrin, allowing iron release at the low pH of the endosome (2, 5). (rndsystems.com)
Protein4
- The hereditary hemochromatosis protein HFE competes with diferric transferrin for binding to TfR, and targets TfR for degradation rather than recycling (2, 5). (rndsystems.com)
- We tested that selected sequences have low aspecific protein adsorption and high binding energy toward transferrin, and one of them is efficiently internalized in cells with a transferrin-dependent pathway. (unige.it)
- Furthermore, it promotes transferrin-mediated endocytosis of gold nanoparticles by modifying their protein corona and promoting oriented adsorption of transferrin. (unige.it)
- Background: Because iron and cadmium share common transport mechanisms, iron-processing protein variants such as HFE C282Y, HFE H63D, and Transferrin P570S may influence cadmium metabolism. (cdc.gov)
Glycoprotein2
- Transferrin is a glycoprotein with a molecular weight of about 77, 000 daltons which is synthesized in the liver. (clinlabnavigator.com)
- This test makes use of a glycoprotein called transferrin that is made by the liver. (accesalabs.com)
Reagents1
- Human IgG antibody Laboratories manufactures the elisa of transferrin reagents distributed by Genprice. (science-bas.org)
Polymorphisms2
- Our aim was to evaluate associations between common HFE and Transferrin polymorphisms and toenail cadmium levels among older men. (cdc.gov)
- Methods: In a longitudinal cohort of men age 51-97, the Normative Aging Study (NAS), we evaluated toenail cadmium concentrations and missense single nucleotide polymorphisms (SNPs) in the HFE and Transferrin genes. (cdc.gov)
Phenotype1
- The relationship between a phenotype of transferrin (Tf) and ceruloplasmin (Cp) and the frequency of diarrhoea occurrence was analysed in 317 piglets. (copernicus.org)
Biomarkers1
- Additionally, some CDG types have previously been reported to demonstrate spontaneous improvement in glycosylated biomarkers, including transferrin. (biomedcentral.com)
Hemochromatosis1
- A high ratio of iron to transferrin in the blood may suggest a person has hemochromatosis. (nih.gov)
Iron3
- In the anemia of chronic disease, both transferrin and serum iron levels are typically low. (clinlabnavigator.com)
- What is non-transferrin-bound iron (NBTI)? (thebloodproject.com)
- As an alternative strategy, we rationally designed a peptide coating able to bind transferrin on suitable pockets not involved in binding to TfR or iron by using an iterative multiscale-modeling approach coupled with quantitative structure-activity and relationship (QSAR) analysis and evolutionary algorithms. (unige.it)
Molecules2
- After daily consumption of five or more alcoholic drinks, the liver starts producing transferrin that is lacking their normal carbohydrate (i.e. sugar) molecules. (accesalabs.com)
- Our data suggest that serum-free and blood-free transferrin can be used as a carrier for nucleic acids and potentially other molecules for trafficking molecules into cells. (cellculturedish.com)
Therapeutic1
- This observation questions the reliability of transferrin as a therapeutic outcome measure in clinical trials for PMM2-CDG. (biomedcentral.com)
Human5
- The Elisa Of Transferrin reagent is RUO (Research Use Only) to test human serum or cell culture lab samples. (science-bas.org)
- Description: Human Transferrin ELISA kit by Cygnus Technologies is available in Europe via Gentaur. (science-bas.org)
- Excess transferrin does not negatively impact transfection, and the incorporation of a blood- and serum-free, recombinant human transferrin supports high transfection efficiency and viral titer in a chemically defined, blood-free medium. (cellculturedish.com)
- Given the success of transferrin as a molecular carrier, the use of transferrin has still relied on serum-derived transferrin from either bovine serum or human serum. (cellculturedish.com)
- We have therefore developed a protocol for the use of a recombinant human transferrin that is not derived from serum or animal blood. (cellculturedish.com)
Gene2
- Preparation of a transferrin-targeted M13-based gene nanocarrier and e" by MOHAMMAD KHALAJKONDORI, MAHBOOBEH KAVOOSI et al. (tubitak.gov.tr)
- Here we prepared a transferrin-targeted M13-based gene nanocarrier (Tf-targeted M13-GFP) and examined its gene delivery and expression efficacy in the AGS cell line. (tubitak.gov.tr)
Measurement1
- Description: A sandwich ELISA for quantitative measurement of Monkey Transferrin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (science-bas.org)
Levels1
- While excess transferrin in transfection has already been identified to increase transfection efficiency, 2 we show that blood-free and serum-free transferrin added in excess during the transfection of adherent cells improves the transfection efficiency compared to low levels of transferrin and serum-derived transferrin. (cellculturedish.com)
Blood2
- However, to date, a serum-free and blood-free transferrin has not been tested for improvements to transfection efficiency. (cellculturedish.com)
- We have thus created a protocol for the improvement of transfection efficiency and viral titer without the need for blood-derived transferrin. (cellculturedish.com)
Results2
- These results indicate that excess transferrin does not negatively affect transfection and can enhance transfection efficiency of HEK-293T cells in serum-free, chemically defined conditions. (cellculturedish.com)
- Results: HFE and Transferrin genotypes were not associated with toenail cadmium concentrations in the main effect analyses, but there were significant interactions between HFE H63D and hemoglobin (pinteraction=0.021), as well as HFE H63D and vitamin C intake (pinteraction=0.048). (cdc.gov)
Cells2
- Of these ligands, serum-derived transferrin is well-known to improve transfection efficiency of adherent cells. (cellculturedish.com)
- To determine if transferrin enhancement of transfection efficiency correlated with higher viral titers, we performed transient transfection with lentivirus plasmids for viral production with 293T cells. (cellculturedish.com)
Found1
- Transferrin is found in the tear film . (alensa.in)
Delivery1
- Previously, we prepared transferrin (Tf) decorated-nanostructured lipid carriers (NLCs) for rapamycin (150 ± 9 nm) to protect the drug from chemical and enzymatic degradation and for brain targeted delivery of rapamycin. (nih.gov)
Soluble transferrin receptor4
- The method for measurement of soluble transferrin receptor (sTfR) is immuno-turbidimetry using Roche kits on the Hitachi 912 clinical analyzer. (cdc.gov)
- A study by Sierpinski et al indicated that in patients with heart failure, serum soluble transferrin receptor is a better biomarker than serum ferritin or transferrin saturation for predicting iron deficiency in bone marrow. (medscape.com)
- Similarly, a study by Fitzsimons et al found a link between iron deficiency as manifested in a soluble transferrin receptor level of 1.76 mg/L or greater and all-cause mortality in persons with heart failure and preserved ejection fraction, the hazard ratio for that receptor level being 1.84. (medscape.com)
- This Interagency Agreement is intended to conduct activities that will harmonize assays measuring soluble transferrin receptor (STfR), an important indicator to assess the global burden of iron deficiency in children and women of childbearing age. (nih.gov)
Ferritin4
- [ 3 ] Unlike ferritin, the transferrin receptor level is not affected by infection or inflammation and is therefore useful in distinguishing iron deficiency anemia from anemia of chronic disease. (medscape.com)
- Along with other tests in an anemia panel ( iron , ferritin , reticulocyte count , lactate dehydrogenase [LDH], vitamin B-12 , folate ), the type of anemia can be diagnosed based on the transferrin receptor levels. (medscape.com)
- Iron tests (including ferritin, iron, transferrin, and IBC) are ideally drawn early in the morning, after a 12-hour fast, when serum iron values are highest. (medscape.com)
- Iron tests frequently performed together to diagnose iron deficiency or overload include serum iron, ferritin, IBC, and transferrin levels. (medscape.com)
Hemochromatosis1
- A high ratio of iron to transferrin in the blood may suggest a person has hemochromatosis. (nih.gov)
Receptor type2
- Iron delivery is mediated via transferrin internalization by the endocytosis of transferrin receptor type 1 (TFR1), one of the most abundant membrane proteins of erythroblasts. (nih.gov)
- Evaluation of the Association of Transferrin Receptor Type 2 Gene Mutation (Y250X) with Iron Overload in Major β- Thalassemia. (nih.gov)
TFR11
- Potential therapeutic uses targeting the transferrin-TFR1 axis or TFR2 in hematological disorders are also discussed. (nih.gov)
Protein8
- [ 4 ] This IBC value is therefore an indirect measure of protein transferrin, which binds iron in serum. (medscape.com)
- This gene encodes a single-pass type II membrane protein, which is a member of the transferrin receptor-like family. (nih.gov)
- This protein mediates cellular uptake of transferrin-bound iron, and may be involved in iron metabolism, hepatocyte function and erythrocyte differentiation. (nih.gov)
- The TFR2 gene provides instructions for making a protein called transferrin receptor 2. (medlineplus.gov)
- On the surface of hepatocytes, the receptor binds to a protein called transferrin, which transports iron through the blood to tissues throughout the body. (medlineplus.gov)
- Additionally, transferrin receptor 2 can bind to other proteins to help regulate iron storage levels in the body by controlling the levels of another protein called hepcidin. (medlineplus.gov)
- These mutations prevent the protein from binding to transferrin, blocking iron from entering hepatocytes. (medlineplus.gov)
- Background: Because iron and cadmium share common transport mechanisms, iron-processing protein variants such as HFE C282Y, HFE H63D, and Transferrin P570S may influence cadmium metabolism. (cdc.gov)
TFR22
- A second transferrin receptor-TFR2-associates with the erythropoietin receptor and has been implicated in the regulation of erythropoiesis. (nih.gov)
- Some TFR2 gene mutations prevent the production of transferrin receptor 2. (medlineplus.gov)
Binds1
- When transferrin binds to transferrin receptor 2, iron is allowed to enter the cell. (medlineplus.gov)
Genes1
- Methods: In a longitudinal cohort of men age 51-97, the Normative Aging Study (NAS), we evaluated toenail cadmium concentrations and missense single nucleotide polymorphisms (SNPs) in the HFE and Transferrin genes. (cdc.gov)
Regulation1
- Regulation of cell surface transferrin receptor-2 by iron-dependent cleavage and release of a soluble form. (nih.gov)
Main1
- Results: HFE and Transferrin genotypes were not associated with toenail cadmium concentrations in the main effect analyses, but there were significant interactions between HFE H63D and hemoglobin (pinteraction=0.021), as well as HFE H63D and vitamin C intake (pinteraction=0.048). (cdc.gov)
Tests1
- Transferrin Receptor: ARUP Lab Tests. (medscape.com)
Patients1
- Low expression of transferrin receptor 2 predict poor prognosis in gastric cancer patients. (nih.gov)