Transferrin-Binding Protein B
Transferrin-Binding Proteins
Transferrin-Binding Protein A
Transferrin
Receptors, Transferrin
Iron
Pulmonary Surfactant-Associated Protein B
Neisseria gonorrhoeae
Neisseria meningitidis
A species of gram-negative, aerobic BACTERIA. It is a commensal and pathogen only of humans, and can be carried asymptomatically in the NASOPHARYNX. When found in cerebrospinal fluid it is the causative agent of cerebrospinal meningitis (MENINGITIS, MENINGOCOCCAL). It is also found in venereal discharges and blood. There are at least 13 serogroups based on antigenic differences in the capsular polysaccharides; the ones causing most meningitis infections being A, B, C, Y, and W-135. Each serogroup can be further classified by serotype, serosubtype, and immunotype.
Carrier Proteins
Endocytosis
Encyclopedias as Topic
Ferritins
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.
Purified meningococcal transferrin-binding protein B interacts with a secondary, strain-specific, binding site in the N-terminal lobe of human transferrin. (1/45)
Neisseria meningitidis, grown in iron-limited conditions, produces two transferrin-binding proteins (TbpA and TbpB) that independently and specifically bind human serum transferrin (hTF) but not bovine serum transferrin (bTF). We have used surface plasmon resonance to characterize the interaction between individual TbpA and TbpB and a series of full-length human-bovine chimaeric transferrins (hbTFs) under conditions of variable saturation with iron. A comparative analysis of hTF and hbTF chimaera-binding data confirmed that the major features involved in Tbp binding are located in the C-terminal lobe of hTF and that isolated TbpA can recognize distinct sites present in, or conformationally influenced by, residues 598-679. Binding by TbpB was maintained at a significant but decreased level after replacement of the entire hTF C-terminal lobe by the equivalent bovine sequence. The extent of this binding difference was dependent on the meningococcal strain and on the presence of hTF residues 255-350. This indicated that TbpB from strain SD has a secondary, strain-specific, binding site located within this region, whereas TbpB from strain B16B6 does not share this recognition site. Binding of TbpA was influenced primarily by sequence substitutions in the hTF C-terminal lobe, and co-purified TbpA and TbpB (TbpA+B) was functionally distinct from either of its components. The limited divergence between hTF and bTF has been related to observed differences in binding by Tbps and has been used to delineate those regions of hTF that are important for such interactions. (+info)Immunization with recombinant transferrin binding protein B enhances clearance of nontypeable Haemophilus influenzae from the rat lung. (2/45)
Nontypeable Haemophilus influenzae (NTHI) is an opportunistic pathogen, and heterogeneity in the surface-exposed immunodominant domains of NTHI proteins is thought to be associated with the failure of an infection to stimulate an immune response that is cross-protective against heterologous NTHI strains. The aim of this study was to assess the vaccine potential of a surface-exposed component of the NTHI human transferrin receptor, TbpB, and to determine if the antibody response elicited was cross-reactive with heterologous strains of NTHI. The efficacy of immunization with a recombinant form of TbpB (rTbpB) was determined by assessing the pulmonary clearance of viable bacteria 4 h after a live challenge with NTHI. There was a significant reduction in the number of viable bacteria in both the bronchoalveolar lavage fluid (34% for the 20-microgram dose and 58% for the 40-microgram dose) and lung homogenates (26% for the 20-microgram dose and 60% for the 40-microgram dose) of rats immunized with rTbpB compared to the control animals. While rTbpB-specific antibodies from immunized rats were nonspecific in the recognition of TbpB from six heterologous NTHI strains on Western blots, these antibodies differed in their ability to block transferrin binding to heterologous strains and to cross-react in bactericidal assays. If bactericidal antibodies are key indicators of the efficacy of the immune response in eliminating NTHI, this data suggests that while immunization with rTbpB stimulates protective responses against the homologous isolate, variability in the recognition of TbpB from heterologous isolates may limit the potential of rTbpB as an NTHI vaccine component. (+info)Allelic diversity of the two transferrin binding protein B gene isotypes among a collection of Neisseria meningitidis strains representative of serogroup B disease: implication for the composition of a recombinant TbpB-based vaccine. (3/45)
The distribution of the two isotypes of tbpB in a collection of 108 serogroup B meningococcal strains belonging to the four major clonal groups associated with epidemic and hyperendemic disease (the ET-37 complex, the ET-5 complex, lineage III, and cluster A4) was determined. Isotype I strains (with a 1.8-kb tbpB gene) was less represented than isotype II strains (19.4 versus 80.6%). Isotype I was restricted to the ET-37 complex strains, while isotype II was found in all four clonal complexes. The extent of the allelic diversity of tbpB in these two groups was studied by PCR restriction analysis and sequencing of 10 new tbpB genes. Four major tbpB gene variants were characterized: B16B6 (representative of isotype I) and M982, BZ83, and 8680 (representative of isotype II). The relevance of these variants was assessed at the antigenic level by the determination of cross-bactericidal activity of purified immunoglobulin G preparations raised to the corresponding recombinant TbpB (rTbpB) protein against a panel of 27 strains (5 of isotype I and 22 of isotype II). The results indicated that rTbpB corresponding to each variant was able to induce cross-bactericidal antibodies. However, the number of strains killed with an anti-rTbpB serum was slightly lower than that obtained with an anti-TbpA(+)B complex. None of the sera tested raised against an isotype I strain was able to kill an isotype II strain and vice versa. None of the specific antisera tested (anti-rTbpB or anti-TbpA(+)B complex) was able to kill all of the 22 isotype II strains tested. Moreover, using sera raised against the C-terminus domain of TbpB M982 (amino acids 352 to 691) or BZ83 (amino acids 329 to 669) fused to the maltose-binding protein, cross-bactericidal activity was detected against 12 and 7 isotype II strains, respectively, of the 22 tested. These results suggest surface accessibility of the C-terminal end of TbpB. Altogether, these results show that although more than one rTbpB will be required in the composition of a TbpB-based vaccine to achieve a fully cross-bactericidal activity, rTbpB and its C terminus were able by themselves to induce cross-bactericidal antibodies. (+info)Production of Neisseria meningitidis transferrin-binding protein B by recombinant Bordetella pertussis. (4/45)
Neisseria meningitidis serogroup B infections are among the major causes of fulminant septicemia and meningitis, especially severe in young children, and no broad vaccine is available yet. Because of poor immunogenicity of the serogroup B capsule, many efforts are now devoted to the identification of protective protein antigens. Among those are PorA and, more recently, transferrin-binding protein B (TbpB). In this study, TbpB of N. meningitidis was genetically fused to the N-terminal domain of the Bordetella pertussis filamentous hemagglutinin (FHA), and the fha-tbpB hybrid gene was expressed in B. pertussis either as a plasmid-borne gene or as a single copy inserted into the chromosome. The hybrid protein was efficiently secreted by the recombinant strains, despite its large size, and was recognized by both anti-FHA and anti-TbpB antibodies. A single intranasal administration of recombinant virulent or pertussis-toxin-deficient, attenuated B. pertussis to mice resulted in the production of antigen-specific systemic immunoglobulin G (IgG), as well as local IgG and IgA. The anti-TbpB serum antibodies were of the IgG1, IgG2a, and IgG2b isotypes and were found to express complement-mediated bactericidal activity against N. meningitidis. These observations indicate that recombinant B. pertussis may be a promising vector for the development of a mucosal vaccine against serogroup B meningococci. (+info)Insight into the structure and function of the transferrin receptor from Neisseria meningitidis using microcalorimetric techniques. (5/45)
The transferrin receptor of Neisseria meningitidis is composed of the transmembrane protein TbpA and the outer membrane protein TbpB. Both receptor proteins have the capacity to independently bind their ligand human transferrin (htf). To elucidate the specific role of these proteins in receptor function, isothermal titration calorimetry was used to study the interaction between purified TbpA, TbpB or the entire receptor (TbpA + TbpB) with holo- and apo-htf. The entire receptor was shown to contain a single high affinity htf-binding site on TbpA and approximately two lower affinity binding sites on TbpB. The binding sites appear to be independent. Purified TbpA was shown to have strong ligand preference for apo-htf, whereas TbpA in the receptor complex with TbpB preferentially binds the holo form of htf. The orientation of the ligand specificity of TbpA toward holo-htf is proposed to be the physiological function of TbpB. Furthermore, the thermodynamic mode of htf binding by TbpB of isotypes I and II was shown to be different. A protocol for the generation of active, histidine-tagged TbpB as well as its individual N- and C-terminal domains is presented. Both domains are shown to strongly interact with each other, and isothermal titration calorimetry and circular dichroism experiments provide clear evidence for this interaction causing conformational changes. The N-terminal domain of TbpB was shown to be the site of htf binding, whereas the C-terminal domain is not involved in binding. Furthermore, the interactions between TbpA and the different domains of TbpB have been demonstrated. (+info)Peptide-peptide interactions between human transferrin and transferrin-binding protein B from Moraxella catarrhalis. (6/45)
Transferrin-binding protein B (TbpB) is one component of a bipartite receptor in several gram-negative bacterial species that binds host transferrin and mediates the uptake of iron for growth. Transferrin and TbpB are both bilobed proteins, and the interaction between these proteins seems to involve similar lobe-lobe interactions. Synthetic overlapping peptide libraries representing the N lobe of TbpB from Moraxella catarrhalis were prepared and probed with labeled human transferrin. Transferrin-binding peptides were localized to six different regions of the TbpB N lobe, and reciprocal experiments identified six different regions of the C lobe of transferrin that bound TbpB. Truncations of the N lobe of TbpB that sequentially removed each transferrin-binding determinant were used to probe an overlapping peptide library of the C lobe of human transferrin. The removal of each TbpB N-lobe transferrin-binding determinant resulted in a loss of reactivity with peptides from the synthetic peptide library representing the C lobe of transferrin. Thus, individual peptide-peptide interactions between ligand and receptor were identified. A structural model of human transferrin was used to map surface regions capable of binding to TbpB. (+info)The iron-responsive regulator fur is transcriptionally autoregulated and not essential in Neisseria meningitidis. (7/45)
Fur is a well-known iron-responsive repressor of gene transcription, which is used by many bacteria to respond to the low-iron environment that pathogens encounter during infection. The fur gene in Neisseria meningitidis has been described as an essential gene that may regulate a broad array of genes. We succeeded in obtaining an N. meningitidis mutant with the fur gene knocked out and used it to undertake studies of fur-mediated iron regulation. We show that expression of both Fur and the transferrin binding protein Tbp2 is iron regulated and demonstrate that this regulation is Fur mediated for the Tbp2 protein. Footprinting analysis revealed that Fur binds to two distinct sites upstream of its coding region with different affinities and that these binding sites overlap two promoters that differentially control transcription of the fur gene in response to iron. The presence of two independently regulated fur promoters may allow meningococcus to fine-tune expression of this regulator controlling iron homeostasis, possibly during infection. (+info)Immunogenicity of gonococcal transferrin binding proteins during natural infections. (8/45)
In this study, we examined the immune response during gonococcal infection to the individual transferrin binding proteins by using a quantitative enzyme-linked immunosorbent assay (ELISA). Recombinant transferrin binding protein A (rTbpA) and rTbpB were purified under nondenaturing conditions for use as ELISA antigens. Sera and secretions from culture-positive individuals were analyzed for antibodies to rTbpA and rTbpB and compared to samples from individuals with no history of gonococcal infection. Although antibodies to both rTbpA and rTbpB were detected in serum, in most cases the antibody levels were not significantly different from those measured in the control population. Also, previous history of gonococcal infection did not increase antibody levels in serum, suggesting the lack of an anamnestic response. Analysis of secretion samples revealed antibody levels that were generally below the limits of detection in our assay. Overall, this study demonstrated a paucity of systemic and local antibody responses to rTbps as a result of natural infection and represents a baseline over which a protective antibody response will have to be generated in order to develop an efficacious gonococcal vaccine. (+info)Transferrin-binding protein B is a bacterial surface receptor that binds to human transferrin, facilitating iron acquisition and contributing to the pathogenesis of certain bacterial infections.
Transferrin-binding protein B (TbpB) is not a medical term itself, but it is a bacterial protein involved in the process of iron acquisition by certain bacteria. Therefore, I will provide you with a biological definition:
Transferrin-binding Protein B (TbpB) is a bacterial surface protein primarily found in pathogenic Neisseria species, such as Neisseria gonorrhoeae and Neisseria meningitidis. TbpB plays a crucial role in the iron acquisition process by binding to human transferrin, a glycoprotein that transports iron in the bloodstream.
TbpB, along with Transferrin-binding Protein A (TbpA), facilitates the uptake of iron from transferrin, which is essential for bacterial growth and survival within the host. The interaction between TbpB and transferrin allows the bacteria to evade the host's immune system and establish an infection. Understanding the function of TbpB has implications in developing novel therapeutic strategies against Neisseria infections.
Transferrin-binding proteins are bacterial surface receptors that bind to human transferrin, a glycoprotein responsible for iron transport, facilitating the acquisition of iron from host sources during infection.
Transferrin-binding proteins (TBPS) are a group of bacterial surface receptors that bind to transferrin, a glycoprotein involved in iron transport in mammals. These proteins are produced by certain pathogenic bacteria as a means to acquire iron from the host environment, which is essential for their growth and survival.
Transferrin sequesters iron in the bloodstream, making it unavailable to many invading microorganisms. However, some bacteria have evolved TBPS that can bind to transferrin and strip it of its iron, allowing them to use this vital nutrient for their own metabolic needs. The interaction between TBPS and transferrin is an important aspect of bacterial virulence and has been studied as a potential target for developing new antimicrobial therapies.
Transferrin-binding protein A is a bacterial surface receptor that binds to transferrin, facilitating iron acquisition and contributing to virulence in certain pathogenic bacteria.
Transferrin-binding protein A (TbpA) is not a medical term itself, but it is a bacterial protein involved in the process of iron acquisition by certain bacteria. Therefore, I will provide a biological definition:
Transferrin-binding Protein A (TbpA) is a bacterial outer membrane protein primarily found in Neisseria species (e.g., Neisseria gonorrhoeae and Neisseria meningitidis). TbpA, along with Transferrin-binding Protein B (TbpB), plays a crucial role in the pathogenesis of these bacteria by facilitating the acquisition of iron from human transferrin, an essential host protein that stores and transports iron. By binding to human transferrin, TbpA and TbpB assist in the transport of iron across the bacterial outer membrane, promoting bacterial growth and survival within the human host.
Iron-binding proteins, also known as transferrins, are glycoproteins that bind and transport ferric iron (Fe3+) in the blood and other biological fluids, maintaining iron homeostasis and preventing the generation of harmful free radicals caused by iron excess.
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.
Transferrin is a glycoprotein that binds and transports iron ions in the blood to maintain iron homeostasis, protect against iron-induced oxidative stress, and deliver iron for erythropoiesis.
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.
Transferrin receptors are membrane-bound proteins that facilitate the cellular uptake and iron release from transferrin, a glycoprotein responsible for transporting iron in the bloodstream, through receptor-mediated endocytosis.
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, in the context of human health, is an essential dietary micromineral and a key component of hemoglobin, responsible for oxygen transport in the blood, which can also act as a crucial co-factor in various enzymatic reactions in the body.
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.
Pulmonary Surfactant-Associated Protein B is a component of lung surfactant that functions as a critical mediator in the innate immune response, contributing to host defense by reducing surface tension at the air-liquid interface and possessing antibacterial and antiviral properties.
Pulmonary Surfactant-Associated Protein B (SP-B) is a small, hydrophobic protein that is an essential component of pulmonary surfactant. Surfactant is a complex mixture of lipids and proteins that reduces surface tension at the air-liquid interface in the alveoli of the lungs, thereby preventing collapse of the alveoli during expiration and facilitating lung expansion during inspiration. SP-B plays a crucial role in the biophysical function of surfactant by promoting its spreading and stability. It is synthesized and processed within type II alveolar epithelial cells and secreted as a part of lamellar bodies, which are lipoprotein complexes that store and release surfactant. Deficiency or dysfunction of SP-B can lead to severe respiratory distress syndrome (RDS) in infants and other lung diseases in both children and adults.
Neisseria gonorrhoeae is a gram-negative, aerobic, oxidase-positive, coffee-bean-shaped diplococcus that causes the sexually transmitted infection gonorrhea and can lead to severe complications such as pelvic inflammatory disease, epididymitis, and infertility if left untreated.
Neisseria gonorrhoeae is a species of gram-negative, aerobic diplococcus that is the etiologic agent of gonorrhea, a sexually transmitted infection. It is commonly found in the mucous membranes of the reproductive tract, including the cervix, urethra, and rectum, as well as the throat and eyes. The bacterium can cause a range of symptoms, including discharge, burning during urination, and, in women, abnormal menstrual bleeding. If left untreated, it can lead to more serious complications, such as pelvic inflammatory disease and infertility. It is important to note that N. gonorrhoeae has developed resistance to many antibiotics over time, making treatment more challenging. A culture or nucleic acid amplification test (NAAT) is used for the diagnosis of this infection.
Neisseria meningitidis is a gram-negative, aerobic diplococcus that can cause life-threatening invasive diseases such as meningitis and septicemia, often residing asymptomatically in the human nasopharynx.
Neisseria meningitidis is a Gram-negative, aerobic, bean-shaped diplococcus bacterium. It is one of the leading causes of bacterial meningitis and sepsis (known as meningococcal disease) worldwide. The bacteria can be found in the back of the nose and throat of approximately 10-25% of the general population, particularly in children, teenagers, and young adults, without causing any symptoms or illness. However, when the bacterium invades the bloodstream and spreads to the brain or spinal cord, it can lead to life-threatening infections such as meningitis (inflammation of the membranes surrounding the brain and spinal cord) and septicemia (blood poisoning).
Neisseria meningitidis is classified into 12 serogroups based on the chemical structure of their capsular polysaccharides. The six major serogroups that cause most meningococcal disease worldwide are A, B, C, W, X, and Y. Vaccines are available to protect against some or all of these serogroups.
Meningococcal disease can progress rapidly, leading to severe symptoms such as high fever, headache, stiff neck, confusion, nausea, vomiting, and a rash consisting of purple or red spots. Immediate medical attention is required if someone experiences these symptoms, as meningococcal disease can cause permanent disabilities or death within hours if left untreated.
'Carrier proteins' are membrane-bound transport proteins that facilitate the passage of specific molecules across biological membranes by undergoing conformational changes, thus maintaining cellular homeostasis without altering the gradient.
Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).
Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.
Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.
Endocytosis is a cellular process where substances are brought into the cell by surrounding the material with membrane, forming a vesicle containing the ingested substance.
Endocytosis is the process by which cells absorb substances from their external environment by engulfing them in membrane-bound structures, resulting in the formation of intracellular vesicles. This mechanism allows cells to take up large molecules, such as proteins and lipids, as well as small particles, like bacteria and viruses. There are two main types of endocytosis: phagocytosis (cell eating) and pinocytosis (cell drinking). Phagocytosis involves the engulfment of solid particles, while pinocytosis deals with the uptake of fluids and dissolved substances. Other specialized forms of endocytosis include receptor-mediated endocytosis and caveolae-mediated endocytosis, which allow for the specific internalization of molecules through the interaction with cell surface receptors.
"Encyclopedias, as a medical topic, refer to comprehensive and organized collections of information on various medical disciplines, theories, practices, diseases, treatments, and related health sciences, serving as extensive reference sources for medical professionals, students, researchers, and general public." (29 words)
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.
Ferritins are intracellular protein complexes that store and release iron ions, maintaining iron homeostasis within cells, and function as a primary iron-storage protein in organisms. (26 words)
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.
Iron chelating agents are medications that bind to iron molecules in the body, forming a stable complex which can then be excreted, thereby reducing excessive or toxic levels of iron and its associated damage in conditions such as hemochromatosis, thalassemia, and iron overload from 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.
![transferrin binding protein B [Actinobacillus pleuropneumoniae] - Protein - NCBI](data:image/png;base64,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)
transferrin binding protein B [Actinobacillus pleuropneumoniae] - Protein - NCBI
transferrin binding protein B [Actinobacillus pleuropneumoniae] transferrin binding protein B [Actinobacillus pleuropneumoniae] ... The tool works with standard single letter nucleotide or protein codes including ambiguities and can match Prosite patterns in ... The tool works with standard single letter nucleotide or protein codes including ambiguities and can match Prosite patterns in ... transferrin binding protein B [Actinobacillus pleuropneumoniae]. GenBank: ADJ96603.1. Identical Proteins FASTA Graphics ...
Transferrin receptor - Wikipedia
In the absence of iron, one of these proteins (generally IRP2) binds to the hairpin like structure (IRE) that is in the 3 UTR ... Transferrin receptor (TfR) is a carrier protein for transferrin. It is needed for the import of iron into cells and is ... Once binding occurs, the mRNA is stabilized and degradation is inhibited. Transferrin receptor 1 Transferrin receptor 2 Soluble ... Earlier two transferrin receptors in humans, transferrin receptor 1 and transferrin receptor 2 had been characterized and until ...
Which tests can diagnose iron deficiency anemia?
Soluble transferrin receptor. Iron gets into the cells by binding to a protein called transferrin. Having enough transferrin in ... High levels of transferrin may be a sign. of iron deficiency anemia, and doctors can use a soluble transferrin receptor (sTfR) ... Total iron binding capacity. Total iron binding capacity (TIBC) is a blood test to check for levels of iron in the blood. ... These are key proteins in red blood cells, which are responsible for carrying oxygen throughout the body in the blood. The body ...
Pulmonary Rehabilitation: Overview, Benefits of Pulmonary Rehabilitation, Patient Selection and Assessment
... and retinol-binding protein. However, these indicators generally are not reliable in identifying inadequate nutrition. They ... Biochemical tests have been advocated as a marker of nutritional status; they include albumin, prealbumin, transferrin, ... where its binding produces agonist activity while simultaneously preventing nicotine binding. Agonistic activity is ... Based on trials, it appears that protein supplementation of at least 1.7 g/kg of body weight per day is associated with ...
Neisseria meningitidis serogroup B Recombinant | Cusabio | Europe, UK & US Distribution
Recombinant Neisseria meningitidis serogroup B Transferrin-binding protein 1 (tbp1), partial , CSB-EP881449NGG Cusabio ... Recombinant Neisseria meningitidis serogroup B Transferrin-binding protein 1 (tbp1), partial , CSB-EP881449NGG , ... Transferrin-binding protein 1Gene Names: tbp1Research Areas: Cell BiologyOrganism: Neisseria... ... Recombinant Neisseria meningitidis serogroup B DNA-binding protein HU-beta (hupB) , CSB-EP350724NGG Cusabio Neisseria ...
Binding of Folic Acid to Serum Proteins | Acta Haematologica | Karger Publishers
The increase was particularly distinct in the binding to transferrin. At the same time, the binding to α-2-macroglobulin ... the total protein binding of FAA decreased remarkably. The decrease was also particularly distinct for transferrin ... Binding of Folic Acid to Serum Proteins: I. The Effect of Pregnancy Subject Area: Hematology , Oncology ... T. Markkanen, P. Himanen, R.-L. Pajula, S. Ruponen, O. Castrén; Binding of Folic Acid to Serum Proteins: I. The Effect of ...
Frontiers | Decidualization of human endometrial stromal cells requires steroid receptor coactivator-3
Decidualization and insulin-like growth factor (IGF) binding protein: implications for its role in stromal cell differentiation ... Louis, MO), 1% ITS-A (insulin, transferrin, selenite and sodium pyruvate), 500 ng/ml puromycin, 100 units/ml penicillin, and ... insulin growth factor binding protein-1; HAND2, heart and neural crest derivative expressed 2; FOXO1, forkhead box 1; HOXA10, ... insulin like growth factor binding protein-1 [IGFBP1 (57)]; heart and neural crest derivatives expressed 2 [HAND2 (58, 59)]; ...
Evolution of Sequence Type 4821 Clonal Complex Hyperinvasive and Quinolone-Resistant Meningococci - Volume 27, Number 4-April...
Fegan JE, Calmettes C, Islam EA, Ahn SK, Chaudhuri S, Yu RH, et al. Utility of hybrid transferrin binding protein antigens for ... We annotated and analyzed deduced encoding factor H-binding protein (fHbp), Neisseria heparin-binding antigen (NHBA), Neisseria ... The meningococcal vaccine candidate neisserial surface protein A (NspA) binds to factor H and enhances meningococcal resistance ... harboring mutations in penicillin-binding protein 2. These data show that the quinolone-resistant clone ChinaCC4821-R1-C/B has ...
CATH Superfamily 2.40.170.20
Total iron binding capacity: MedlinePlus Medical Encyclopedia
Iron moves through the blood attached to a protein called transferrin. This test helps your ... Iron moves through the blood attached to a protein called transferrin. This test helps your ... Total iron binding capacity (TIBC) is a blood test to see if you have too much or too little iron in your blood. ... Total iron binding capacity (TIBC) is a blood test to see if you have too much or too little iron in your blood. ...
Pharmaceutics | Free Full-Text | Candida glabrata Antifungal Resistance and Virulence Factors, a Perfect Pathogenic Combination
... glabrata can acquire free iron and iron from iron-binding proteins such as hemoglobin, ferritin, and transferrin. The ... are the main cell surface proteins involved in C. glabrata virulence [65,154,160]. Epa proteins are analogous to Als proteins ... Moreover, certain proteins have been identified in C. glabrata, such as Pwp7p and Aed1p, that are relevant for adherence in ... Genes and Proteins Involved. Mechanisms Involved. Result. Complex C. glabrata. Azoles. Multiple drugs. Mutations (polymorphisms ...
Iron and Total Iron-Binding Capacity - Health Encyclopedia - University of Rochester Medical Center
... mainly to a protein made by your liver called transferrin. The TIBC test is based on certain proteins, including transferrin, ... Iron, TIBC, and transferrin blood tests are almost always done together. Your blood may also be checked for: * Level of your ... This is the protein in your red blood cells that carries oxygen around your body. If you dont have enough iron, you may not ... The total iron-binding capacity (TIBC) test looks at how well the iron moves through your body. ...
Iron Foods for Kids and Babies & How Much They Need - SuperKids Nutrition
Transferrin saturation. protein in the blood that binds to iron to transport it. will be low. ... Total iron-binding capacity (TIBC). amount of iron that can bind to blood. will be high. ... Hemoglobin is a protein found in red blood cells that transports oxygen from the lungs to your whole body. Its also what makes ... protein that carries oxygen. will be low. Hematocrit. the calculated volume percentage of red blood cells (erythrocytes) in ...
Deubiquitylase OTUD3 prevents Parkinson's disease through stabilizing iron regulatory protein 2 | Cell Death & Disease
Here, we report OTUD3 (OTU domain-containing protein 3) functions as a deubiquitylase for IRP2, interacts with IRP2 in the ... cytoplasm, de-polyubiquitylates, and stabilizes IRP2 protein in an iron-independent manner. Depletion of OTUD3 results in a ... Iron regulatory protein 2 (IRP2) is a key factor in regulating brain iron homeostasis. Although two ubiquitin ligases that ... Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2. Struct, Funct, post- ...
Receptors, Transferrin | Profiles RNS
Carrier Proteins [D12.776.157]. *Transferrin-Binding Proteins [D12.776.157.905]. *Receptors, Transferrin [D12.776.157.905.500] ... Mass spectrometry study of a transferrin-based protein drug reveals the key role of protein aggregation for successful oral ... They specifically bind iron-bearing transferrin, are endocytosed with its ligand and then returned to the cell surface where ... "Receptors, Transferrin" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ...
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DailyMed - SUCRALFATE tablet
Why bloating and fatigue could be a sign you need a medieval cure | Daily Mail Online
To establish this involves a blood test called transferrin saturation to measure levels of transferrin, a protein that binds to ... Wheelchair-bound girl, 13, struggles to pour herself a... Eat dinner together to tackle obesity: Nanny in chief and... ... This is the protein that moves oxygen through the blood and the GP thought it meant Corrina was lacking in iron. She was on ... Protein bars that claim to be backed by science are recalled after customers find hairnets and shrink wrap in them ...
Can Humans Live Longer?: by miss libby Blog entry
The liver makes binding proteins called ferritin, transferrin and lactoferrin, to bind to iron as it enters the circulatory ... Insects control iron by iron-binding proteins (ferritin, transferrin).8 Excessive iron has been found to be the initiator of ... This results in iron loss.19 Aspirin also appears to increase the production of ferritin, an iron-binding protein produced in ... The reason is that grapes, like the figs that mynah birds eat, have those iron-binding pigments that tightly bind to iron. In ...
Nutritional Biomarkers Branch | CDC
Combined measurement of ferritin, soluble transferrin receptor, retinol binding protein, and C-reactive protein by an ... C-reactive protein, α-1-glycoprotein, and retinol-binding protein showed variable comparability with traditional reference ... Serum soluble transferrin receptor concentrations in US preschool children and non-pregnant women of childbearing age from the ... A simplified protein precipitation and filtration procedure for determining serum vitamin B(6) by high-performance liquid ...
Test To Determine Iron Levels | Iron Disorders Institute
Iron contained in blood serum (or plasma) is normally bound to the protein transferrin. Each molecule of transferrin can ... Iron in the plasma that is not bound to transferrin is often called non-transferrin bound iron (NTBI). This is a potentially ... Total Iron Binding Capacity (TIBC) and Transferrin Saturation % (TS%). Total iron binding capacity (TIBC) is often measured at ... iron is considered safely bound. Much above that, transferrin becomes saturated and it binding capacity drops to a point where ...
Transferin - Wikipedia
"Transferrin is an insulin-like growth factor-binding protein-3 binding protein". The Journal of Clinical Endocrinology and ... "Transferrin binds insulin-like growth factors and affects binding properties of insulin-like growth factor binding protein-3". ... GO:0001948, GO:0016582 protein binding. • ferric iron transmembrane transporter activity. • ferrous iron binding. • transferrin ... regulation of protein stability. • transferrin transport. • iron ion homeostasis. • platelet degranulation. • ion transport. • ...
Transferrin Receptor 2 (TFR2) (NM 003227) Human Untagged Clone - SC310106 | OriGene
... which is a member of the transferrin receptor-like family. This protein mediates cellular uptake of transferrin-bound iron, and ... Protein Families. Druggable Genome, Protease, Transmembrane. Gene Summary. This gene encodes a single-pass type II membrane ... Lenti ORF clone of Human transferrin receptor 2 (TFR2), transcript variant 1, Myc-DDK-tagged. * * 10 ug. 10 ug ... Lenti ORF clone of Human transferrin receptor 2 (TFR2), transcript variant 1, Myc-DDK-tagged. * * 10 ug. 10 ug ...
Red blood cell - wikidoc
Hemolyzed hemoglobin is bound to a protein in plasma called haptoglobin which is not excreted by the kidney. ... The iron is released into the plasma to be recirculated by a carrier protein called transferrin. Almost all erythrocytes are ... This is known as rouleaux formation, and it occurs more often if the levels of certain serum proteins are elevated, as for ... Respiratory protein-generated reactive oxygen species as an antimicrobial strategy. Nature Immunology, 26 August 2007. PMID ...
ALMS1 and Alström syndrome: a recessive form of metabolic, neurosensory and cardiac deficits | Journal of Molecular Medicine
Numerous candidate ALMS1-interacting proteins have been reported. Members of the α-actinin family of actin-binding proteins ... Endosomal trafficking of transferrin and Notch. Impairments in the trafficking and recycling of endocytosed transferrin (Tf) ... The ALMS1 protein. ALMS1 is a large (, 4000 residue) protein that lacks known catalytic domains [11, 12]. It has several ... Following up on leads from protein-protein interaction data, recently significantly enriched by a human interactome study [113 ...
Single-molecule fingerprinting of protein-drug interaction using a funneled biological nanopore | Nature Communications
... plot illustrate the ability of the YaxAB nanopore to discriminate individual small-molecule drugs bound to Bcl-xL from non- ... Efficient screening of protein-drug interactions (PDIs) has been impeded by the limitations of current biophysical approaches. ... Here, we develop a biological nanopore sensor for single-molecule detection of proteins and PDIs using the pore-forming toxin ... Here, the authors present a funneled YaxAB nanopore sensor which allows label-free, single-molecule detection of proteins and ...
Frontiers | A Hypothesis for the Possible Role of Zinc in the Immunological Pathways Related to COVID-19 Infection
... since it is mostly bound to proteins such as albumin, alpha-2-macroglobulin (A2M), and transferrin. Plasma zinc levels are ... The zinc-finger protein ZCCHC3 binds RNA and facilitates viral RNA sensing and activation of the RIG-I-like receptors. Immunity ... The zinc-finger protein ZCCHC3 binds RNA and facilitates the detection of intracellular RNA viruses by activating retinoic acid ... Mocchegiani E, Costarelli L, Giacconi R, Cipriano C, Muti E, Malavolta M. Zinc-binding proteins (metallothionein and alpha-2 ...
FerritinReceptorSaturationTIBCHemoglobinAlbuminReceptorsMoleculeIRP1 and IRP2TbpARecombinantStructural ClassifiTfR2GlobulinIonsTransport proteinsAntibodyLactoferrinFerricAffinityCytokinesFolic AcidHuman SerumSerum ProteinsGlycoproteinRetinolLiverPlasmaFatty acid-biSpeciesDegradationCharacterizationMRNACytoplasmMolecular weightAnemiaPercentageIntestinalCell SurfaceOxygenCognatePPIsIron homeostasisMagnesiumTotalStabilityToxicitySequenceVitaminInteractionsComplexEnzymesLobes
Ferritin12
- Ferritin is an iron-containing protein in the blood. (medicalnewstoday.com)
- Esmaeili R, Zhang M, Sternberg MR, Mapango C, Pfeiffer CM . A new multiplex immunoassay for serum ferritin, soluble transferrin receptor, C-reactive protein, α-1-glycoprotein, and retinol-binding protein showed variable comparability with traditional reference assays external icon . (cdc.gov)
- Another 30% is stored in ferritin, a protein found throughout the body (although this percentage can be significantly higher or lower in cases of iron overload or deficiency), and a few percent in myoglobin, a protein specifically utilized by muscle cells. (irondisorders.org)
- Ferritin is a protein synthesized by the body that is mainly utilized to store iron for future use. (irondisorders.org)
- The serum iron, serum ferritin, total iron-binding capacity (TIBC), percentage transferrin saturation and C-reactive protein were estimated, as per the manufacturer's protocol. (scielo.br)
- The mean level of serum iron, ferritin, percentage transferrin saturation and TIBC were 309.44 ± 122.40mcg/dl, 860.36 ± 624.64ng/ml, 42.6 ± 17.30% and 241.32 ± 96.30 mcg/dl, respectively, in the cases and 95.36 ± 41.90mcg/dl, 122.28 ± 49.70ng/ml, 15.83 ± 3.10% and 492.6 ± 149.40mcg/dl in the controls, respectively. (scielo.br)
- transferrin A plasma protein (a β- globulin ) that can bind to iron and transport it to the liver for storage (see ferritin ) or to the cells of bone marrow , where it is used for the formation of haemoglobin. (encyclopedia.com)
- among other well-known iron-binding proteins such as hemoglobin, ferritin and transferrin, but also perhaps because its biological functions are so diverse. (kisch-online.de)
- MEEDAT also measures systemic inflammation (AGP, CRP), micronutrient deficiency (ferritin, soluble transferrin receptor, retinol binding protein 4, thyroglobulin), and Plasmodium falciparum antigenemia (histidine-rich protein 2). (washington.edu)
- 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)
- The IBC value and transferrin saturation are best interpreted in the context of additional iron studies (typically, serum iron, ferritin, transferrin) and in the clinical context of the patient's baseline health state. (medscape.com)
Receptor17
- Transferrin receptor (TfR) is a carrier protein for transferrin. (wikipedia.org)
- It imports iron by internalizing the transferrin-iron complex through receptor-mediated endocytosis. (wikipedia.org)
- The existence of a receptor for transferrin iron uptake has been recognized since the late 1950s. (wikipedia.org)
- Earlier two transferrin receptors in humans, transferrin receptor 1 and transferrin receptor 2 had been characterized and until recently cellular iron uptake was believed to occur chiefly via these two well documented transferrin receptors. (wikipedia.org)
- The multifunctional glycolytic enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH, EC 1.2.1.12) has been shown to utilize post translational modifications to exhibit higher order moonlighting behavior wherein it switches its function as a holo or apo transferrin receptor leading to either iron delivery or iron export respectively. (wikipedia.org)
- Low iron concentrations promote increased levels of transferrin receptor, to increase iron intake into the cell. (wikipedia.org)
- Thus, transferrin receptor maintains cellular iron homeostasis. (wikipedia.org)
- Transferrin receptor 1 Transferrin receptor 2 Soluble transferrin receptor GAPDH Qian ZM, Li H, Sun H, Ho K (December 2002). (wikipedia.org)
- Figure 3: The cycle of transferrin and transferrin receptor 1-mediated cellular iron uptake. (wikipedia.org)
- High levels of transferrin may be a sign of iron deficiency anemia, and doctors can use a soluble transferrin receptor (sTfR) test to check for these levels. (medicalnewstoday.com)
- Kada transferinski protein napunjen gvožđem naiđe na transferinski receptor na površini ćelije , npr. (wikipedia.org)
- Complejo de proteínas que forma un receptor para la TRANSFERRINA en BACTERIAS. (bvsalud.org)
- A complex of proteins that forms a receptor for TRANSFERRIN in BACTERIA. (bvsalud.org)
- When a transferrin loaded with iron encounters with a transferring receptor on cell surface, transferring binds to it and, as a consequence, is transported into the cell in a visicle by receptor-mediated endocytosis. (betalifesci.com)
- Soluble transferrin receptor (mg/L) [Time Frame: Screening, days 1 and 57. (who.int)
- It is a bispecific humanized monoclonal antibody against CD3, a T-cell surface antigen, and GPRC5D (human G-protein coupled receptor family C group 5 member D), a tumor-associated antigen with potential antineoplastic activity. (medscape.com)
- Motixafortide is an inhibitor of C-X-C motif chemokine receptor 4 (CXCR4) and blocks binding of its cognate ligand, stromal-derived factor-1α (SDF-1α)/C-X-C motif chemokine ligand 12 (CXCL12). (medscape.com)
Saturation10
- Transferrin saturation percentage (TS %) is calculated by dividing serum iron by TIBC, then multiplying by 100. (irondisorders.org)
- Total transferrin was measured by nephelometry after reaction of the protein with specific antisera (Behring Diagnostics, Marburg, Germany) and saturation of transferrin calculated after automated analysis of plasma iron using a commercially supplied kit (Boehringer-Mannheim). (bmj.com)
- however, in the last several years, this value is most commonly referred to simply as the transferrin saturation. (medscape.com)
- Higher transferrin saturation values are found in high iron states, such as megaloblastic anemia , sideroblastic anemia , and iron overload states. (medscape.com)
- Decreased transferrin saturation values are found in chronic iron deficiency, chronic infection, extensive malignancy, tissue inflammation states, uremia , and nephrotic syndrome . (medscape.com)
- The value of the transferrin saturation is calculated with the formula below. (medscape.com)
- A normal transferrin saturation value is found in patients with normal iron levels. (medscape.com)
- Transferrin saturation calculation requires the serum iron and IBC values. (medscape.com)
- Transferrin saturation is typically part of the iron deficiency panel. (medscape.com)
- However, more patients achieved transfusion independence with momelotinib than with ruxolitinib, and objective laboratory measures of anemia (eg, hemoglobin, serum iron, transferrin saturation) also favored momelotinib. (medscape.com)
TIBC9
- Total iron binding capacity (TIBC) is a blood test to check for levels of iron in the blood. (medicalnewstoday.com)
- Total iron binding capacity (TIBC) is a blood test to see if you have too much or too little iron in your blood. (medlineplus.gov)
- The total iron-binding capacity (TIBC) test looks at how well the iron moves through your body. (rochester.edu)
- The TIBC test is based on certain proteins, including transferrin, found in the blood. (rochester.edu)
- Your transferrin levels are almost always measured along with iron and TIBC. (rochester.edu)
- Iron, TIBC, and transferrin blood tests are almost always done together. (rochester.edu)
- Your healthcare provider will look at your iron level along with the TIBC, transferrin, and possibly other tests to see what the results mean. (rochester.edu)
- Total iron binding capacity (TIBC) is often measured at the same time as serum iron. (irondisorders.org)
- When TIBC is at or below the low end of a laboratory range, it is an indication that there is limited capacity for transferrin molecules to accept additional iron. (irondisorders.org)
Hemoglobin4
- Hemoglobin is a protein found in red blood cells that transports oxygen from the lungs to your whole body. (superkidsnutrition.com)
- Most of the body's iron (about 60%) is contained in hemoglobin, which is the essential oxygen carrying protein of the blood. (irondisorders.org)
- Magnesium below 2.05 mg/dL, hemoglobin, albumin, prealbumin and retinol binding protein below lower limit of normal and HbA1C above upper limit of normal were associated with PEI in univariate analysis. (wellnessresources.com)
- and tbpA and hgbB, transferrin-binding protein and hemoglobin-binding protein genes involved in iron acquisition. (biomedcentral.com)
Albumin3
- In addition, aluminum does not cross dialysis membranes because it is bound to albumin and transferrin plasma proteins. (nih.gov)
- There are very low levels of free zinc in plasma, since it is mostly bound to proteins such as albumin, alpha-2-macroglobulin (A2M), and transferrin. (frontiersin.org)
- mAb that bind aliphatic di- and polyisocyanates (conjugated to albumin), but not aromatic toluene or methylene diphenyl diisocyanate (TDI or MDI). (cdc.gov)
Receptors5
- Receptors, Transferrin" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (umassmed.edu)
- This graph shows the total number of publications written about "Receptors, Transferrin" by people in this website by year, and whether "Receptors, Transferrin" was a major or minor topic of these publications. (umassmed.edu)
- Below are the most recent publications written about "Receptors, Transferrin" by people in Profiles. (umassmed.edu)
- Peptides derived from sequence of cell surface proteins, such as intercellular adhesion molecule-1 (ICAM-1), LHRH, Bombesin, and LFA-1, have shown potent binding affinity to the target cell surface receptors. (biosyn.com)
- Arg-Gly-Asp (RGD) peptides,2 poly-Arg peptides), 3,4 proteins (e.g., antibodies,5 transport proteins, and transferrin6), and small molecules (e.g., folate7) have been used to selectively direct drugs to cancer cells with upregulated receptors by forming drug-carrier conjugates (Fig. 1). (biosyn.com)
Molecule7
- Each molecule of transferrin can transport two molecules of iron to areas of the body that need this element. (irondisorders.org)
- Here, we develop a biological nanopore sensor for single-molecule detection of proteins and PDIs using the pore-forming toxin YaxAB. (nature.com)
- Using this YaxAB nanopore, we demonstrate label-free, single-molecule detection of interactions between the anticancer Bcl-xL protein and small-molecule drugs as well as the Bak-BH3 peptide. (nature.com)
- Distinctive nanopore event distributions observed in the two-dimensional (ΔI/I o -versus-I N ) plot illustrate the ability of the YaxAB nanopore to discriminate individual small-molecule drugs bound to Bcl-xL from non-binders. (nature.com)
- One transferrin molecule can bind to two iron ions. (encyclopedia.com)
- This transferrin binds only one Fe3+ ion per protein molecule. (betalifesci.com)
- Each transferrin molecule has the ability to carry two iron ions in the ferric form. (betalifesci.com)
IRP1 and IRP22
- TfR production in the cell is regulated according to iron levels by iron-responsive element-binding proteins, IRP1 and IRP2. (wikipedia.org)
- Intracellular iron levels are elaborately balanced by iron efflux, uptake, and storage proteins that are regulated by iron regulatory proteins (IRPs, including IRP1 and IRP2) [ 16 ]. (nature.com)
TbpA2
- Matthew Barber and Nels Elde from the University of Utah School of Medicine compared transferrin-encoding genes from 21 primate species, and found remarkable variation at sites known to interact with a bacterial transferrin binding protein, TbpA. (the-scientist.com)
- A further investigation of transferrin sequence differences among humans revealed a variant that was unable to interact with the TbpA protein from H. influenzae . (the-scientist.com)
Recombinant2
- Recombinant human NOD2 protein corresponding to residues 28-301. (novusbio.com)
- The recombinant proteins are stable for up to 1 year from date of receipt at -70°C. (betalifesci.com)
Structural Classifi2
- SCOP: Structural Classification of Proteins and ASTRAL. (berkeley.edu)
- SCOPe: Structural Classification of Proteins - extended. (berkeley.edu)
TfR21
- TfR2 binds to transferrin with a 25-30 fold lower affinity than TfR1. (wikipedia.org)
Globulin2
- To address this, concentrations of testosterone, sex hormone binding globulin, androstanediol glucuronide (a metabolite of dihydrotestosterone) and estradiol were measured in stored serum specimens from men examined in the morning sample of the first phase of NHANES III (1988-1991). (cdc.gov)
- Most of the circulating testosterone is bound to carrier proteins (SHBG = sex hormone-binding globulin). (cdc.gov)
Ions3
- In this book, experts from a variety of disciplines describe the present knowledge of the structural features of lactoferrin, its carbohydrate side chains and its capacity to bind different metal ions and anions. (kisch-online.de)
- One of the major components required in order for the proper continuation of this process is transferrin, a protein that helps bind iron ions that have been absorbed from the duodenum, and transports these ions through the bloodstream into the cells. (differencebetween.net)
- The lower pH causes transferrin to release its iron ions. (betalifesci.com)
Transport proteins1
- Transferrins are iron binding transport proteins which bind Fe3+ ion in association with the binding of an anion, usually bicarbonate. (betalifesci.com)
Antibody7
- Endogenous testosterone released from the sample by ANS (8-anilino-1-naphthalene sulfonic acid) and norgestrel competes with the added testosterone derivative labeled with ruthenium complex for the binding sites on the biotinylated antibody. (cdc.gov)
- The binding sites of the labeled antibody become occupied partly by the sample analyte (depending on its concentration) and partly by the ruthenium-labeled hapten to form the respective immunocomplexes. (cdc.gov)
- Western Blot: NOD2 Antibody (2D9) [NB100-524] - HCMV infection induces NOD2 mRNA and protein in HFFs and U373 cells. (novusbio.com)
- Western Blot: NOD2 Antibody (2D9) [NB100-524] - Whole cell protein from THP-1 cells was separated on a 7.5% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% non-fat milk in TBST. (novusbio.com)
- A model showing the structure of the human transferrin protein WIKIMEDIA, EMW Damaging toxins and antibody-epitope interactions are frequently the battlegrounds of host-pathogen arms races, but a new study suggests a role for a different, so-called "nutritional" immune system. (the-scientist.com)
- Each mAb demonstrates slight differences in epitope specificity, for example, recognition of hydrogenated MDI (HMDI) or different carrier proteins (transferrin, actin) reacted with vapor phase HDI, and is encoded by unique recombination of different germline antibody genes, with distinct complementary determining regions. (cdc.gov)
- Elranatamab is an antibody that binds to both CD3 on T-cells and B-cell maturation antigen (BCMA), which are expressed on the surface of multiple myeloma cells. (medscape.com)
Lactoferrin1
- Lactoferrin is an intriguing protein with an interesting structure and several known or suggested biological activities. (kisch-online.de)
Ferric1
- This glycoprotein is thought to have been created as a result of an ancient gene duplication event that led to generation of homologous C and N-terminal domains each of which binds one ion of ferric iron. (betalifesci.com)
Affinity1
- Although iron boundto transferrin is less than 0.1% (4 mg) of the total body iron, it is themost important iron pool, with the highest rate of turnover (25 mg/24 h).Transferrin has a molecular weight of around 80 kDa and contains 2 specifichigh-affinity Fe(III) binding sites. (creativebiomart.net)
Cytokines1
- The changes in body iron distribution are caused by cytokines and acute phase proteins. (haematologica.org)
Folic Acid1
- Binding of serum folic acid activity (FAA) to the protein fractions during and after pregnancy was studied by DEAE Sephadex A-50 gel chromatography. (karger.com)
Human Serum2
- Chaudhary-Webb M, Schleicher RL, Erhardt JG, Pendergrast EC, Pfeiffer CM. An HPLC ultraviolet method using low sample volume and protein precipitation for the measurement of retinol in human serum suitable for laboratories in low- and middle-income countries external icon . (cdc.gov)
- The current work focused on stability-structure studies of human serum transferrin using Nano-Differential Scanning Fluorimetry (NanoDSF), Isothermal Chemical Denaturation (ICD), light scattering techniques, and Small Angle X-ray Scattering (SAXS). (lu.se)
Serum Proteins1
- This is known as rouleaux formation , and it occurs more often if the levels of certain serum proteins are elevated, as for instance during inflammation . (wikidoc.org)
Glycoprotein2
- transferrin ( siderophilin ) (trans- fer -in) n. a glycoprotein, found in the blood plasma, that acts as a carrier for iron in the bloodstream. (encyclopedia.com)
- Transferrin is a glycoprotein with an approximate molecular weight of 76.5 kDa. (betalifesci.com)
Retinol1
- Retinol-binding protein 4 (µmol/L) [Time Frame: Screening, days 1 and 57. (who.int)
Liver2
- Iron in your body is carried, or bound, mainly to a protein made by your liver called transferrin. (rochester.edu)
- The function of Transferrin is to transport iron from the intestine, reticuloendothelial system, and liver parenchymal cells to all proliferating cells in the body. (betalifesci.com)
Plasma4
- Iron contained in blood serum (or plasma) is normally bound to the protein transferrin. (irondisorders.org)
- When laboratories test for SI, they are testing iron contained in plasma that is generally bound to transferrin. (irondisorders.org)
- Iron in the plasma that is not bound to transferrin is often called non-transferrin bound iron (NTBI). (irondisorders.org)
- Native Rat Tf arethe principal plasma proteins that bind wine catechins. (creativebiomart.net)
Fatty acid-bi2
- The Micronutrient and EED Assessment Tool (MEEDAT) is a multiplexed immunoassay that measures biomarkers previously associated with child growth faltering and/or oral vaccine immunogenicity: intestinal fatty acid-binding protein (I-FABP), soluble CD14 (sCD14), insulin-like growth factor 1 (IGF-1), and fibroblast growth factor 21 (FGF21). (washington.edu)
- Intestinal fatty acid-binding protein (pg/mL) [Time Frame: Screening, Days 2, 23, 57, 58 and 79. (who.int)
Species1
- Some of the iron will then bind to other molecules not have transferrin's ability to protect its host from iron catalyzed lipid peroxidation and the formation of reactive oxygen species. (irondisorders.org)
Degradation3
- Once binding occurs, the mRNA is stabilized and degradation is inhibited. (wikipedia.org)
- Hepdicin exerts its biological function upon binding to the only known cellular iron exporter, ferroportin (SLC40A1), thereby leading to ferroportin internalization and degradation. (haematologica.org)
- An assay system using bleomycin dependent degradation of DNA to measure free or loosely bound iron has been established. (bmj.com)
Characterization1
- Mass spectrometry-guided optimization and characterization of a biologically active transferrin-lysozyme model drug conjugate. (umassmed.edu)
MRNA2
- In the absence of iron, one of these proteins (generally IRP2) binds to the hairpin like structure (IRE) that is in the 3' UTR of the TfR mRNA. (wikipedia.org)
- Under various iron conditions, IRPs could bind to IREs in the targeted mRNA, stabilize the mRNA or prevent its translation. (nature.com)
Cytoplasm2
- Here, we report OTUD3 (OTU domain-containing protein 3) functions as a deubiquitylase for IRP2, interacts with IRP2 in the cytoplasm, de-polyubiquitylates, and stabilizes IRP2 protein in an iron-independent manner. (nature.com)
- In cytoplasm, zinc mostly binds zinc-chelating proteins called metallothioneins (MTs). (frontiersin.org)
Molecular weight1
- The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. (novusbio.com)
Anemia1
- Doctors may give this test along with transferrin tests to check for signs of anemia. (medicalnewstoday.com)
Percentage1
- When laboratories measure serum iron they often also measure transferrin and calculate the percentage of transferrin molecules that are used to bind iron. (irondisorders.org)
Intestinal1
- For instance, most labile zinc in the body is absorbed by intestinal epithelial cells via SLC39a4 protein, and excessive zinc is excreted through the kidneys, and the intestine via SLC39a5 ( 12 ). (frontiersin.org)
Cell Surface1
- 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. (umassmed.edu)
Oxygen4
- These are key proteins in red blood cells, which are responsible for carrying oxygen throughout the body in the blood. (medicalnewstoday.com)
- This is the protein in your red blood cells that carries oxygen around your body. (rochester.edu)
- Finally, iron is necessary to form myoglobin-a type of protein that carries and stores oxygen in the muscle tissue. (superkidsnutrition.com)
- Each of these proteins uses iron to supply oxygen and energy for everyday needs. (irondisorders.org)
Cognate1
- The therapeutic efficacy of drugs is mediated by physical interaction with their cognate targets (mainly proteins). (nature.com)
PPIs2
- Although protein-protein interactions (PPIs) are promising targets, drugging them is one of the key challenges in drug discovery 19 . (nature.com)
- The online tools DAVID, Reactome, and AmiGO were employed for annotation, visualization, and integration of DEGs related to HT and PTC, and the STRING database and Cytoscape software were applied to predict and visualize protein-protein networks (PPIs) for DEG-encoded proteins. (medsci.org)
Iron homeostasis1
- Iron regulatory protein 2 (IRP2) is a key factor in regulating brain iron homeostasis. (nature.com)
Magnesium1
- Then, a standard amount of magnesium carbonate is added, which binds to the unbound iron, forming iron-carbonate complexes. (medscape.com)
Total1
- Within a week after delivery, the total protein binding of FAA decreased remarkably. (karger.com)
Stability3
- he binding and release of iron is dependent of several factors, such as pH, ionic strength, and chelators that have an influence on protein stability. (lu.se)
- NanoDSF allows for monitoring protein stability with increasing temperature and provides information about the melting temperature (T½). (lu.se)
- The overall stability and behavior of transferrin was investigated at varying pH and ionic strength using nanoDSF and ICD. (lu.se)
Toxicity1
- Iron toxicity results when circulating iron exceeds the capacity of transferrin available to bind it. (irondisorders.org)
Sequence3
- View conserved domains detected in this protein sequence using CD-search. (nih.gov)
- In different ethnic groups, this sequence was present in 6 percent to 25 percent of people, showing a snapshot of transferrin evolution, with the pathogen-evading version changing in frequency depending on the environment. (the-scientist.com)
- You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. (betalifesci.com)
Vitamin1
- 25-OHD (25-hydroxyvitamin D), the major circulating metabolite of vitamin D, was measured in serum by competitive protein-binding (CPB) assay and radioimmunoassay kit (Nichols, San Juan Capistrano, California). (who.int)
Interactions1
- In drug discovery, efficient screening of protein-drug interactions (PDIs) is hampered by the limitations of current biophysical approaches. (nature.com)
Complex2
- In line with a more complex picture, multiple isoforms of the protein likely exist and non-centrosomal sites of localisation have been reported. (springer.com)
- Many pathogenic bacteria utilize the transferrin-binding complex to acquire their supply of iron from serum. (bvsalud.org)
Enzymes1
- Enzymes and proteins that contain iron are essential in a number of different biological oxidations as well as transport. (differencebetween.net)
Lobes1
- [18] The N- and C- terminal sequences are represented by globular lobes and between the two lobes is an iron-binding site. (wikipedia.org)