Anion Exchange Protein 1, Erythrocyte: A major integral transmembrane protein of the ERYTHROCYTE MEMBRANE. It is the anion exchanger responsible for electroneutral transporting in CHLORIDE IONS in exchange of BICARBONATE IONS allowing CO2 uptake and transport from tissues to lungs by the red blood cells. Genetic mutations that result in a loss of the protein function have been associated with type 4 HEREDITARY SPHEROCYTOSIS.SLC4A Proteins: Bicarbonate transporters that move BICARBONATE IONS in exchange of CHLORIDE IONS or SODIUM IONS across membranes. They regulate acid-base HOMEOSTASIS, cell volume and intracellular pH. Members include CHLORIDE-BICARBONATE ANTIPORTERS (SLC4A1, 2, 3, and 9); SODIUM-COUPLED BICARBONATE TRANSPORTERS (SLC4A4 and 5, 7, 8 and 10); and a sodium borate cotransporter (SLC4A11 protein).Anion Transport Proteins: Membrane proteins whose primary function is to facilitate the transport of negatively charged molecules (anions) across a biological membrane.4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid: A non-penetrating amino reagent (commonly called SITS) which acts as an inhibitor of anion transport in erythrocytes and other cells.Erythrocytes: Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.Antiporters: Membrane transporters that co-transport two or more dissimilar molecules in the opposite direction across a membrane. Usually the transport of one ion or molecule is against its electrochemical gradient and is "powered" by the movement of another ion or molecule with its electrochemical gradient.Erythrocyte Membrane: The semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS.Anions: Negatively charged atoms, radicals or groups of atoms which travel to the anode or positive pole during electrolysis.Anion Exchange Resins: High-molecular-weight insoluble polymers that contain functional cationic groups capable of undergoing exchange reactions with anions.Guanine Nucleotide Exchange Factors: Protein factors that promote the exchange of GTP for GDP bound to GTP-BINDING PROTEINS.rap1 GTP-Binding Proteins: A genetically related subfamily of RAP GTP-BINDING PROTEINS that share homology with RAS PROTEINS. They bind to Ras effectors but do not activate them, therefore they may antagonize the effects of RAS PROTEINS. This enzyme was formerly listed as EC 3.6.1.47.Chromatography, Ion Exchange: Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.Cyclic AMP: An adenine nucleotide containing one phosphate group which is esterified to both the 3'- and 5'-positions of the sugar moiety. It is a second messenger and a key intracellular regulator, functioning as a mediator of activity for a number of hormones, including epinephrine, glucagon, and ACTH.rab3 GTP-Binding Proteins: A genetically related subfamily of RAB GTP-BINDING PROTEINS involved in calcium-dependent EXOCYTOSIS. This enzyme was formerly listed as EC 3.6.1.47.rap GTP-Binding Proteins: A family of MONOMERIC GTP-BINDING PROTEINS that are related to RAS PROTEINS.This enzyme was formerly listed as EC 3.6.1.47.Erythrocyte Aging: The senescence of RED BLOOD CELLS. Lacking the organelles that make protein synthesis possible, the mature erythrocyte is incapable of self-repair, reproduction, and carrying out certain functions performed by other cells. This limits the average life span of an erythrocyte to 120 days.Cyclic AMP-Dependent Protein Kinases: A group of enzymes that are dependent on CYCLIC AMP and catalyze the phosphorylation of SERINE or THREONINE residues on proteins. Included under this category are two cyclic-AMP-dependent protein kinase subtypes, each of which is defined by its subunit composition.4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid: An inhibitor of anion conductance including band 3-mediated anion transport.Kinetics: The rate dynamics in chemical or physical systems.Chloride-Bicarbonate Antiporters: Electroneutral chloride bicarbonate exchangers that allow the exchange of BICARBONATE IONS exchange for CHLORIDE IONS across the cellular membrane. The action of specific antiporters in this class serve important functions such as allowing the efficient exchange of bicarbonate across red blood cell membranes as they passage through capillaries and the reabsorption of bicarbonate ions by the kidney.Chlorides: Inorganic compounds derived from hydrochloric acid that contain the Cl- ion.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)rho-Specific Guanine Nucleotide Dissociation Inhibitors: A subcategory of guanine nucleotide dissociation inhibitors that are specific for RHO GTP-BINDING PROTEINS.Ion Exchange: Reversible chemical reaction between a solid, often one of the ION EXCHANGE RESINS, and a fluid whereby ions may be exchanged from one substance to another. This technique is used in water purification, in research, and in industry.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Bicarbonates: Inorganic salts that contain the -HCO3 radical. They are an important factor in determining the pH of the blood and the concentration of bicarbonate ions is regulated by the kidney. Levels in the blood are an index of the alkali reserve or buffering capacity.Guanine Nucleotide Dissociation Inhibitors: Protein factors that inhibit the dissociation of GDP from GTP-BINDING PROTEINS.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Guanosine Diphosphate: A guanine nucleotide containing two phosphate groups esterified to the sugar moiety.ras Guanine Nucleotide Exchange Factors: A family of GUANINE NUCLEOTIDE EXCHANGE FACTORS that are specific for RAS PROTEINS.Molecular Weight: The sum of the weight of all the atoms in a molecule.Biological Transport: The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.Erythrocyte Deformability: Ability of ERYTHROCYTES to change shape as they pass through narrow spaces, such as the microvasculature.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Sulfates: Inorganic salts of sulfuric acid.Ion Exchange Resins: High molecular weight, insoluble polymers which contain functional groups that are capable of undergoing exchange reactions (ION EXCHANGE) with either cations or anions.Phosphatidylcholines: Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to a choline moiety. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid and choline and 2 moles of fatty acids.Exoribonucleases: A family of enzymes that catalyze the exonucleolytic cleavage of RNA. It includes EC 3.1.13.-, EC 3.1.14.-, EC 3.1.15.-, and EC 3.1.16.-. EC 3.1.-Membrane Proteins: Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.GTP-Binding Proteins: Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.Son of Sevenless Proteins: A class of RAS GUANINE NUCLEOTIDE EXCHANGE FACTORS that are genetically related to the Son of Sevenless gene from DROSOPHILA. Sevenless refers to genetic mutations in DROSOPHILA that cause loss of the R7 photoreceptor which is required to see UV light.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.Hemolysis: The destruction of ERYTHROCYTES by many different causal agents such as antibodies, bacteria, chemicals, temperature, and changes in tonicity.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Phospholipid Transfer Proteins: A ubiquitous family of proteins that transport PHOSPHOLIPIDS such as PHOSPHATIDYLINOSITOL and PHOSPHATIDYLCHOLINE between membranes. They play an important role in phospholipid metabolism during vesicular transport and SIGNAL TRANSDUCTION.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Bromides: Salts of hydrobromic acid, HBr, with the bromine atom in the 1- oxidation state. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Oxalates: Derivatives of OXALIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that are derived from the ethanedioic acid structure.Signal Transduction: The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.Erythrocyte Count: The number of RED BLOOD CELLS per unit volume in a sample of venous BLOOD.Erythrocyte Aggregation: The formation of clumps of RED BLOOD CELLS under low or non-flow conditions, resulting from the attraction forces between the red blood cells. The cells adhere to each other in rouleaux aggregates. Slight mechanical force, such as occurs in the circulation, is enough to disperse these aggregates. Stronger or weaker than normal aggregation may result from a variety of effects in the ERYTHROCYTE MEMBRANE or in BLOOD PLASMA. The degree of aggregation is affected by ERYTHROCYTE DEFORMABILITY, erythrocyte membrane sialylation, masking of negative surface charge by plasma proteins, etc. BLOOD VISCOSITY and the ERYTHROCYTE SEDIMENTATION RATE are affected by the amount of erythrocyte aggregation and are parameters used to measure the aggregation.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Sodium-Calcium Exchanger: An electrogenic ion exchange protein that maintains a steady level of calcium by removing an amount of calcium equal to that which enters the cells. It is widely distributed in most excitable membranes, including the brain and heart.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Enzyme Activation: Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Isoelectric Point: The pH in solutions of proteins and related compounds at which the dipolar ions are at a maximum.Epichlorohydrin: A chlorinated epoxy compound used as an industrial solvent. It is a strong skin irritant and carcinogen.Colforsin: Potent activator of the adenylate cyclase system and the biosynthesis of cyclic AMP. From the plant COLEUS FORSKOHLII. Has antihypertensive, positive inotropic, platelet aggregation inhibitory, and smooth muscle relaxant activities; also lowers intraocular pressure and promotes release of hormones from the pituitary gland.Sodium: A member of the alkali group of metals. It has the atomic symbol Na, atomic number 11, and atomic weight 23.Liposomes: Artificial, single or multilaminar vesicles (made from lecithins or other lipids) that are used for the delivery of a variety of biological molecules or molecular complexes to cells, for example, drug delivery and gene transfer. They are also used to study membranes and membrane proteins.Calcium: A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Phospholipids: Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides see GLYCEROPHOSPHOLIPIDS) or sphingosine (SPHINGOLIPIDS). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Biological Transport, Active: The movement of materials across cell membranes and epithelial layers against an electrochemical gradient, requiring the expenditure of metabolic energy.8-Bromo Cyclic Adenosine Monophosphate: A long-acting derivative of cyclic AMP. It is an activator of cyclic AMP-dependent protein kinase, but resistant to degradation by cyclic AMP phosphodiesterase.Time Factors: Elements of limited time intervals, contributing to particular results or situations.Deuterium Exchange Measurement: A research technique to measure solvent exposed regions of molecules that is used to provide insight about PROTEIN CONFORMATION.Erythrocyte Volume: Volume of circulating ERYTHROCYTES . It is usually measured by RADIOISOTOPE DILUTION TECHNIQUE.Organic Anion Transporters: Proteins involved in the transport of organic anions. They play an important role in the elimination of a variety of endogenous substances, xenobiotics and their metabolites from the body.Models, Biological: Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.Benzylammonium Compounds: QUATERNARY AMMONIUM COMPOUNDS based on BENZYLAMINES with the general formula phenyl-CN+R3.Glycophorin: The major sialoglycoprotein of the human erythrocyte membrane. It consists of at least two sialoglycopeptides and is composed of 60% carbohydrate including sialic acid and 40% protein. It is involved in a number of different biological activities including the binding of MN blood groups, influenza viruses, kidney bean phytohemagglutinin, and wheat germ agglutinin.Pulmonary Gas Exchange: The exchange of OXYGEN and CARBON DIOXIDE between alveolar air and pulmonary capillary blood that occurs across the BLOOD-AIR BARRIER.DNA, Single-Stranded: A single chain of deoxyribonucleotides that occurs in some bacteria and viruses. It usually exists as a covalently closed circle.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Cell Membrane Permeability: A quality of cell membranes which permits the passage of solvents and solutes into and out of cells.Exchange Transfusion, Whole Blood: Repetitive withdrawal of small amounts of blood and replacement with donor blood until a large proportion of the blood volume has been exchanged. Used in treatment of fetal erythroblastosis, hepatic coma, sickle cell anemia, disseminated intravascular coagulation, septicemia, burns, thrombotic thrombopenic purpura, and fulminant malaria.Guanosine Triphosphate: Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety.Rabbits: The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.Proto-Oncogene Proteins p21(ras): Cellular proteins encoded by the H-ras, K-ras and N-ras genes. The proteins have GTPase activity and are involved in signal transduction as monomeric GTP-binding proteins. Elevated levels of p21 c-ras have been associated with neoplasia. This enzyme was formerly listed as EC 3.6.1.47.Fungal Proteins: Proteins found in any species of fungus.Chromatography: Techniques used to separate mixtures of substances based on differences in the relative affinities of the substances for mobile and stationary phases. A mobile phase (fluid or gas) passes through a column containing a stationary phase of porous solid or liquid coated on a solid support. Usage is both analytical for small amounts and preparative for bulk amounts.Plasmodium falciparum: A species of protozoa that is the causal agent of falciparum malaria (MALARIA, FALCIPARUM). It is most prevalent in the tropics and subtropics.Sister Chromatid Exchange: An exchange of segments between the sister chromatids of a chromosome, either between the sister chromatids of a meiotic tetrad or between the sister chromatids of a duplicated somatic chromosome. Its frequency is increased by ultraviolet and ionizing radiation and other mutagenic agents and is particularly high in BLOOM SYNDROME.Iodides: Inorganic binary compounds of iodine or the I- ion.Sodium-Hydrogen Antiporter: A plasma membrane exchange glycoprotein transporter that functions in intracellular pH regulation, cell volume regulation, and cellular response to many different hormones and mitogens.Temperature: The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.Osmotic Fragility: RED BLOOD CELL sensitivity to change in OSMOTIC PRESSURE. When exposed to a hypotonic concentration of sodium in a solution, red cells take in more water, swell until the capacity of the cell membrane is exceeded, and burst.Blood Proteins: Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Spectrin: A high molecular weight (220-250 kDa) water-soluble protein which can be extracted from erythrocyte ghosts in low ionic strength buffers. The protein contains no lipids or carbohydrates, is the predominant species of peripheral erythrocyte membrane proteins, and exists as a fibrous coating on the inner, cytoplasmic surface of the membrane.Rad51 Recombinase: A Rec A recombinase found in eukaryotes. Rad51 is involved in DNA REPAIR of double-strand breaks.Hemagglutination: The aggregation of ERYTHROCYTES by AGGLUTININS, including antibodies, lectins, and viral proteins (HEMAGGLUTINATION, VIRAL).Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.Resins, Synthetic: Polymers of high molecular weight which at some stage are capable of being molded and then harden to form useful components.p-Aminohippuric Acid: The glycine amide of 4-aminobenzoic acid. Its sodium salt is used as a diagnostic aid to measure effective renal plasma flow (ERPF) and excretory capacity.Potassium: An element in the alkali group of metals with an atomic symbol K, atomic number 19, and atomic weight 39.10. It is the chief cation in the intracellular fluid of muscle and other cells. Potassium ion is a strong electrolyte that plays a significant role in the regulation of fluid volume and maintenance of the WATER-ELECTROLYTE BALANCE.Recombination, Genetic: Production of new arrangements of DNA by various mechanisms such as assortment and segregation, CROSSING OVER; GENE CONVERSION; GENETIC TRANSFORMATION; GENETIC CONJUGATION; GENETIC TRANSDUCTION; or mixed infection of viruses.Guanosine 5'-O-(3-Thiotriphosphate): Guanosine 5'-(trihydrogen diphosphate), monoanhydride with phosphorothioic acid. A stable GTP analog which enjoys a variety of physiological actions such as stimulation of guanine nucleotide-binding proteins, phosphoinositide hydrolysis, cyclic AMP accumulation, and activation of specific proto-oncogenes.Organic Anion Transporters, Sodium-Independent: A subclass of ORGANIC ANION TRANSPORTERS that do not rely directly or indirectly upon sodium ion gradients for the transport of organic ions.Chromatography, Affinity: A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Magnetic Resonance Spectroscopy: Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).Transfection: The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.Stilbenes: Organic compounds that contain 1,2-diphenylethylene as a functional group.Amiloride: A pyrazine compound inhibiting SODIUM reabsorption through SODIUM CHANNELS in renal EPITHELIAL CELLS. This inhibition creates a negative potential in the luminal membranes of principal cells, located in the distal convoluted tubule and collecting duct. Negative potential reduces secretion of potassium and hydrogen ions. Amiloride is used in conjunction with DIURETICS to spare POTASSIUM loss. (From Gilman et al., Goodman and Gilman's The Pharmacological Basis of Therapeutics, 9th ed, p705)Saccharomyces cerevisiae Proteins: Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.Protein Processing, Post-Translational: Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.Phosphates: Inorganic salts of phosphoric acid.Ion Transport: The movement of ions across energy-transducing cell membranes. Transport can be active, passive or facilitated. Ions may travel by themselves (uniport), or as a group of two or more ions in the same (symport) or opposite (antiport) directions.Ethoxzolamide: A carbonic anhydrase inhibitor used as diuretic and in glaucoma. It may cause hypokalemia.Structure-Activity Relationship: The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.Recombinant Fusion Proteins: Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.Voltage-Dependent Anion Channels: A family of voltage-gated eukaryotic porins that form aqueous channels. They play an essential role in mitochondrial CELL MEMBRANE PERMEABILITY, are often regulated by BCL-2 PROTO-ONCOGENE PROTEINS, and have been implicated in APOPTOSIS.Carbohydrate Sequence: The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Adenosine Triphosphate: An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.Carbohydrates: The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrates are composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n.Microvilli: Minute projections of cell membranes which greatly increase the surface area of the cell.

Topology of the membrane domain of human erythrocyte anion exchange protein, AE1. (1/661)

Anion exchanger 1 (AE1) is the chloride/bicarbonate exchange protein of the erythrocyte membrane. By using a combination of introduced cysteine mutants and sulfhydryl-specific chemistry, we have mapped the topology of the human AE1 membrane domain. Twenty-seven single cysteines were introduced throughout the Leu708-Val911 region of human AE1, and these mutants were expressed by transient transfection of human embryonic kidney cells. On the basis of cysteine accessibility to membrane-permeant biotin maleimide and to membrane-impermeant lucifer yellow iodoacetamide, we have proposed a model for the topology of AE1 membrane domain. In this model, AE1 is composed of 13 typical transmembrane segments, and the Asp807-His834 region is membrane-embedded but does not have the usual alpha-helical conformation. To identify amino acids that are important for anion transport, we analyzed the anion exchange activity for all introduced cysteine mutants, using a whole cell fluorescence assay. We found that mutants G714C, S725C, and S731C have very low transport activity, implying that this region has a structurally and/or catalytically important role. We measured the residual anion transport activity after mutant treatment with the membrane-impermeant, cysteine-directed compound, sodium (2-sulfonatoethyl)methanethiosulfonate) (MTSES). Only two mutants, S852C and A858C, were inhibited by MTSES, indicating that these residues may be located in a pore-lining region.  (+info)

Structural and functional consequences of antigenic modulation of red blood cells with methoxypoly(ethylene glycol). (2/661)

We previously showed that the covalent modification of the red blood cell (RBC) surface with methoxypoly(ethylene glycol) [mPEG; MW approximately 5 kD] could significantly attenuate the immunologic recognition of surface antigens. However, to make these antigenically silent RBC a clinically viable option, the mPEG-modified RBC must maintain normal cellular structure and functions. To this end, mPEG-derivatization was found to have no significant detrimental effects on RBC structure or function at concentrations that effectively blocked antigenic recognition of a variety of RBC antigens. Importantly, RBC lysis, morphology, and hemoglobin oxidation state were unaffected by mPEG-modification. Furthermore, as shown by functional studies of Band 3, a major site of modification, PEG-binding does not affect protein function, as evidenced by normal SO4- flux. Similarly, Na+ and K+ homeostasis were unaffected. The functional aspects of the mPEG-modified RBC were also maintained, as evidenced by normal oxygen binding and cellular deformability. Perhaps most importantly, mPEG-derivatized mouse RBC showed normal in vivo survival ( approximately 50 days) with no sensitization after repeated transfusions. These data further support the hypothesis that the covalent attachment of nonimmunogenic materials (eg, mPEG) to intact RBC may have significant application in transfusion medicine, especially for the chronically transfused and/or allosensitized patient.  (+info)

Volume expansion stimulates p72(syk) and p56(lyn) in skate erythrocytes. (3/661)

Hypotonic volume expansion of skate erythrocytes rapidly stimulates the tyrosine phosphorylation of band 3, the membrane protein thought to mediate the osmotically sensitive taurine efflux. Skate erythrocytes possess numerous tyrosine kinases including p59fyn, p56lyn, pp60(src), and p72(syk), demonstrated by immune complex assays measuring autocatalytic kinase activity. Inclusion of the cytoplasmic domain of band 3 in this assay showed that only Syk and Lyn can directly phosphorylate the cytoplasmic domain of band 3. Upon cell volume expansion, Syk activity was increased as assessed by three different assays (immune complex assay measuring autophosphorylation, assay of the level of phosphotyrosine of the immunoprecipitated kinase, and assay of level of 32P in the kinase immunoprecipitated from cells prelabeled with 32PO4 and then volume-expanded). The tyrosine kinase Lyn was also stimulated by volume expansion, most notably when analyzed by the latter two methods. Volume expansion stimulated a large increase in the ability of Syk to phosphorylate band 3 at times that coincide with the stimulation of taurine flux. The stilbene piceatannol inhibited Syk preferentially over Lyn and other tyrosine kinases and inhibited volume-stimulated taurine efflux in a concentration-dependent manner similar to that for the inhibition of Syk. Two major phosphorylation peaks were detected in tryptic digests of cdb3 separated by reverse phase HPLC. Edman degradation demonstrated a phosphotyrosine in a YXXL motif. In conclusion, p72(syk) appears to be a strong candidate as a pivotal signal-transducing step in the volume-activated taurine efflux in skate red cells. The level of band-3 phosphorylation may be regulated, in addition, by a protein-tyrosine phosphatase of the 1B variety.  (+info)

Hydrodynamic properties of human erythrocyte band 3 solubilized in reduced Triton X-100. (4/661)

The oligomeric state and function of band 3, purified by sulfhydryl affinity chromatography in reduced Triton X-100, was investigated. Size exclusion high-performance liquid chromatography showed that a homogeneous population of band 3 dimers could be purified from whole erythrocyte membranes. The elution profile of band 3 purified from membranes that had been stripped of its cytoskeleton before solubilization was a broad single peak describing a heterogeneous population of oligomers with a mean Stokes radius of 100 A. Sedimentation velocity ultracentrifugation analysis confirmed particle heterogeneity and further showed monomer/dimer/tetramer equilibrium self-association. Whether the conversion of dimer to the form described by a Stokes radius of 100 A was initiated by removal of cytoskeletal components, alkali-induced changes in band 3 conformation, or alkali-induced loss of copurifying ligands remains unclear. After incubation at 20 degrees C for 24 h, both preparations of band 3 converted to a common form characterized by a mean Stokes radius of 114 A. This form of the protein, examined by equilibrium sedimentation ultracentrifugation, is able to self-associate reversibly, and the self-association can be described by a dimer/tetramer/hexamer model, although the presence of higher oligomers cannot be discounted. The ability of the different forms of the protein to bind stilbene disulfonates revealed that the dimer had the highest inhibitor binding affinity, and the form characterized by a mean Stokes radius of 114 A to have the lowest.  (+info)

Decreased plasma membrane thiol concentration is associated with increased osmotic fragility of erythrocytes in zinc-deficient rats. (5/661)

Zinc deficiency leads to pathological signs that are related to impaired function of plasma membrane proteins. The purpose of this study was to assess the effect of dietary zinc status on the sulfhydryl (SH) content of erythrocyte plasma membranes and erythrocyte function. Three experiments were performed. In the first, immature male rats were fed for 21 d either a low-zinc (<1.0 mg/kg) diet free choice (-ZnAL), an adequate-zinc (100 mg/kg) diet free choice (+ZnAL), or the adequate-zinc diet limited to the intake of -ZnAL pair-mates (+ZnPF). Tail blood was sampled to measure osmotic fragility and SH concentration of erythrocyte membrane proteins. The zinc-deficient rats were then repleted for 2 d and erythrocytes assayed for fragility and SH content. In the second experiment blood was sampled at 3-d intervals to determine the time course of change in fragility and SH concentration. In the third experiment the SH concentration of erythrocyte band 3 protein and the binding of zinc to isolated plasma membranes were measured. SH concentration decreased from approximately 75 nmol/mg protein to 68 nmol/mg protein during 21 d of depletion and returned to control level within 2 d of repletion. There was an inverse relationship between osmotic fragility and SH concentration of erythrocyte membrane proteins. Maximal decrease in SH occurred within 6 d of consuming the low-zinc diet. The SH content of band 3 protein isolated from deficient rats was also significantly lower than that of pair-fed controls (45 vs. 51 nmol/mg protein). The zinc-binding affinity of plasma membrane proteins tended to be decreased by zinc deficiency. In summary, low-zinc status lowers the plasma membrane SH concentration, and the decreased reducing potential is inversely related to osmotic fragility, and presumably, with impaired volume recovery of erythrocytes.  (+info)

Splenic but not thymic autoreactive T cells from New Zealand Black mice respond to a dominant erythrocyte Band 3 peptide. (6/661)

Previous work from our laboratory suggested that erythrocyte Band 3 peptide 861-874 is the dominant epitope recognized by splenic T cells from adult New Zealand Black (NZB) mice that are developing autoimmune haemolytic anaemia (AIHA). Here, it is shown that splenic T cells from 6-week-old NZB mice mount a vigorous in vitro proliferative response to peptide 861-874 and some other selected Band 3 peptides. As the donors grow older, splenic T cells respond to an increasing number of Band 3 peptides and the magnitude of their response also becomes greater. Splenic T cells from 3-week-old NZB mice still responded vigorously to peptide 861-874 and Band 3. By contrast, neither thymocytes nor single-positive CD4-enriched thymus cells from NZB mice responded to peptide 861-874 or Band 3, although they responded to concanavalin A (Con A). However, thymocytes from mice expressing a transgenic T-cell receptor (TCR)-specific for myelin basic protein (MBP) peptide Ac 1-9 responded vigorously to Ac 1-9. It is considered that the T-cell response of NZB mice to Band 3 is initially focused on peptide 861-874 and later spreads to other Band 3 peptides as the disease progresses and that peptide 861-874-reactive T cells are primed in the periphery rather than the thymus.  (+info)

Mapping of a palmitoylatable band 3-binding domain of human erythrocyte membrane protein 4.2. (7/661)

Evidence accumulated over the years suggests that human erythrocyte membrane protein 4.2 is one of the proteins involved in strengthening the cytoskeleton-membrane interactions in the red blood cell. Deficiency of protein 4.2 is linked with a variety of hereditary haemolytic anaemia. However, the interactions of protein 4.2 with other proteins of the erythrocyte membrane remain poorly understood. The major membrane-binding site for protein 4.2 resides on the cytoplasmic domain of band 3 (CDB3). In order to carry out an initial characterization of its interaction with the CDB3, protein 4. 2 was subjected to proteolytic cleavage and gel renaturation assay, and the 23-kDa N-terminal domain was found to interact with band 3. This domain contained two putative palmitoylatable cysteine residues, of which cysteine 203 was identified as the palmitoylatable cysteine. Recombinant glutathione S-transferase-fusion peptides derived from this domain were characterized with respect to their ability to interact with the CDB3. Whereas these studies do not rule out the involvement of other subsites on protein 4.2 in interaction with the CDB3, the evidence suggests that the region encompassing amino acid residues 187-211 is one of the domains critical for the protein 4.2-CDB3 interaction. This is also the first demonstration that palmitoylation serves as a positive modulator of this interaction.  (+info)

Mild spherocytosis and altered red cell ion transport in protein 4. 2-null mice. (8/661)

Protein 4.2 is a major component of the red blood cell (RBC) membrane skeleton. We used targeted mutagenesis in embryonic stem (ES) cells to elucidate protein 4.2 functions in vivo. Protein 4. 2-null (4.2(-/-)) mice have mild hereditary spherocytosis (HS). Scanning electron microscopy and ektacytometry confirm loss of membrane surface in 4.2(-/-) RBCs. The membrane skeleton architecture is intact, and the spectrin and ankyrin content of 4. 2(-/-) RBCs are normal. Band 3 and band 3-mediated anion transport are decreased. Protein 4.2(-/-) RBCs show altered cation content (increased K+/decreased Na+)resulting in dehydration. The passive Na+ permeability and the activities of the Na-K-2Cl and K-Cl cotransporters, the Na/H exchanger, and the Gardos channel in 4. 2(-/-) RBCs are significantly increased. Protein 4.2(-/-) RBCs demonstrate an abnormal regulation of cation transport by cell volume. Cell shrinkage induces a greater activation of Na/H exchange and Na-K-2Cl cotransport in 4.2(-/-) RBCs compared with controls. The increased passive Na+ permeability of 4.2(-/-) RBCs is also dependent on cell shrinkage. We conclude that protein 4.2 is important in the maintenance of normal surface area in RBCs and for normal RBC cation transport.  (+info)

1) We have prepared murine monoclonal antibodies to the membrane domain of the human erythrocyte anion transport protein (band 3). (2) All of these antibodies react with regions of the protein located at the cytoplasmic surface of the red cell. (3) One of the antibodies reacts with an epitope present on a cytoplasmic loop of the protein located between the C-terminus and a point 168 amino acids from the C-terminus. The other antibodies recognize different epitopes on the C-terminal tail of the protein and the sequences likely to be involved in these epitopes are defined. (4) Our results show that the C-terminus of the red-cell anion transport protein is located on the cytoplasmic side of the red-cell membrane. (5) None of the antibodies inhibited sulphate exchange transport when introduced into resealed red-cell membranes; however, the bivalent form of one of the antibodies reduced the inhibitory potency of 4-acetamido-4-isothiocyanatostilbene disulphonate on sulphate exchange transport in ...
Baldwin M1, Yamodo I2, Ranjan R3, Li X3, Mines G1, Marinkovic M1, Hanada T1, Oh SS2, Chishti AH4. 2014, Biochim Biophys Acta. 1843(12):2855-70. doi: 10.1016/j.bbamcr.2014.08.008. Epub 2014 Aug 231Department of Developmental, Molecular &amp; Chemical
For the entry SPT1 and the techniques demonstrate normally remain plausible for subjective requirements for Gene: SPTA1 -allelic losses remain informative for interactions and different pathways for the constitutive independent effect and the basis for the symmetry for example NUMA this interaction interfaces for the basis of the interaction lie in the SPTA1 and SPTB in this respect the spectrin beta-chain (band 3), protein 4.2 when it occurs in trans of an elliptocytogenic allele results in a chimeric receptor for which relaxin-3 intron 45 and INSL5 intron 46 (the relevance of this would require further study) are high and low affinity agonists. Intron 46 mutation had no effect by itself. CD1 [?] and SPTA1, belong to multigene families, which have paralogues in the " other three regions", matched to domain of erythrocyte membrane band 3 (cdb3) hosts a mixture of the two of three of the NUMA and non-motor NUMA proteins, for erythroid and non-erythroid spectrin. "Presumably have been created by ...
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Moriyama R, Lombardo CR, Workman RF and Low PS. Department of Chemistry, Purdue University, West Lafayette, Indiana 47907-1393.. In addition to reducing hemoglobin-O2 affinity, 2,3-diphosphoglycerate (DPG) is known to modulate the mechanical properties of the erythrocyte membrane. By fluorescence spectroscopy and differential scanning calorimetry, we demonstrate that DPG binds the cytoplasmic domain of erythrocyte membrane band 3 in two stages characterized by apparent KD values of approximately approximately 2 and 12 mM. DPG was also shown to perturb the stability of ankyrin, protein 4.1, and protein 4.2 in situ and to directly bind to protein 4.1. In studies of membrane-skeleton interactions, DPG was observed to inhibit the fast and slow phases of ankyrin binding to band 3 and to reduce both the number of ankyrin sites and affinity of ankyrin for each class of site. The inhibition was biphasic, similar to the band 3-DPG binding isotherm; however, at physiological DPG concentrations a reduction ...
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Domain combinations containing the Phoshotransferase/anion transport protein superfamily . Domain architectures illustrate each occurrence of the Phoshotransferase/anion transport protein superfamily.
Mutations of SLC4A1 (AE1) encoding the kidney anion (Cl(-)/HCO(3) (-)) exchanger 1 (kAE1 or band 3) can result in either autosomal dominant (AD) or autosomal recessive (AR) distal renal tubular acidosis (dRTA). The molecular mechanisms associated with SLC4A1 mutations resulting in these different modes of inheritance are now being unveiled using transfected cell systems. The dominant mutants kAE1 R589H, R901X and S613F, which have normal or insignificant changes in anion transport function, exhibit intracellular retention with endoplasmic reticulum (ER) localization in cultured non-polarized and polarized cells, while the dominant mutants kAE1 R901X and G609R are mis-targeted to apical membrane in addition to the basolateral membrane in cultured polarized cells ...
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SLC4A1-associated distal renal tubular acidosis is a kidney (renal) disorder that sometimes includes blood cell abnormalities. The kidneys normally filter fluid and waste products from the body and remove them in urine; however, in people with distal renal tubular acidosis, the kidneys are unable to remove enough acid from the body, and the blood becomes too acidic. This chemical imbalance is called metabolic acidosis. The inability to remove acids from the body often results in slowed growth and may also lead to softening and weakening of the bones, called rickets in children and osteomalacia in adults.. This bone disorder is characterized by bone pain, bowed legs, and difficulty walking. In addition, most children and adults with SLC4A1-associated distal renal tubular acidosis have excess calcium in the urine (hypercalciuria), calcium deposits in the kidneys (nephrocalcinosis), and kidney stones (nephrolithiasis). In rare cases, these kidney abnormalities lead to life-threatening kidney ...
Both the autosomal dominant and autosomal recessive forms of SLC4A1-associated distal renal tubular acidosis are caused by mutations in the SLC4A1 gene. This gene provides instructions for making the anion exchanger 1 (AE1) protein, which transports negatively charged atoms (anions) across cell membranes. Specifically, AE1 exchanges negatively charged atoms of chlorine (chloride ions) for negatively charged bicarbonate molecules (bicarbonate ions). The AE1 protein is found in the cell membrane of kidney cells and red blood cells. In kidney cells, the exchange of bicarbonate through AE1 allows acid to be released from the cell into the urine. In red blood cells, AE1 attaches to other proteins that make up the structural framework (the cytoskeleton) of the cells, helping to maintain their structure.. The SLC4A1 gene mutations involved in either form of SLC4A1-associated distal renal tubular acidosis lead to production of altered AE1 proteins that cannot get to the correct location in the cell ...
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... hiv envelope protein gp41 MeSH D12.776.543.550.190.110 -- anion exchange protein 1, erythrocyte MeSH D12.776.543.550.190.276 ... erythrocyte MeSH D12.776.543.585.450.162.234 -- organic anion transport protein 1 MeSH D12.776.543.585.450.162.235 -- ... sodium-phosphate cotransporter proteins, type iii MeSH D12.776.543.585.450.162.110 -- anion exchange protein 1, erythrocyte ... anion exchange protein 1, erythrocyte MeSH D12.776.543.550.190.442 -- potassium-hydrogen antiporters MeSH D12.776.543.550. ...
... anion exchange protein 1, erythrocyte MeSH D12.776.157.530.450.162.276 -- potassium-hydrogen antiporters MeSH D12.776.157.530. ... erythrocyte MeSH D12.776.157.530.450.162.193 -- chloride-bicarbonate antiporters MeSH D12.776.157.530.450.162.193.500 -- ... organic anion transport polypeptide c MeSH D12.776.157.530.450.074.500.781.750 -- organic anion transport protein 1 MeSH ... anion transport proteins MeSH D12.776.157.530.450.074.249 -- halorhodopsins MeSH D12.776.157.530.450.074.500 -- organic anion ...
... anion transport protein. This cotransporter is an important integral protein in mammalian erythrocytes and moves chloride ion ... The sodium-calcium exchanger exchanges 3 sodium ions for 1 calcium ion and represents a cation antiporter. Cells also contain ... The NKCC1 cotransport protein is found throughout the body but NKCC2 is found only in the kidney and removes the sodium, ... The four known KCC proteins team up to form two separate subfamilies with KCC1 and KCC3 pairing together and KCC2 and KCC4 ...
Anion exchange protein 2 (AE2) is a membrane transport protein that in humans is encoded by the SLC4A2 gene. AE2 is ... "Entrez Gene: SLC4A2 solute carrier family 4, anion exchanger, member 2 (erythrocyte membrane protein band 3-like 1)". Gawenis ... Gehrig H, Müller W, Appelhans H (1992). "Complete nucleotide sequence of band 3 related anion transport protein AE2 from human ... Jöns T, Drenckhahn D (1998). "Anion exchanger 2 (AE2) binds to erythrocyte ankyrin and is colocalized with ankyrin along the ...
It is different from the anion exchanger that present in erythrocytes, renal tubule, and several other tissues. The protein ... It mediates chloride and bicarbonate exchange and additionally transports sulfate and other anions at the apical membrane, part ... The downregulated-in-adenoma (DRA) is a membrane protein in intestinal cells. It is an anion exchanger and a member of the ... exchange to Na+/H+ exchange". Biochemistry. 41 (41): 12336-42. doi:10.1021/bi0259103. PMID 12369822. Chernova MN, Jiang L, ...
The increased rigidity of the erythrocyte membrane in SAO is thought to reduce the capacity of the band 3 proteins to cluster ... general rigidity of the cell membrane Loss of sensitivity to substances that cause spiculation of cells Reduced anion exchange ... Rather, the defect lies in a protein known as the band 3 protein, which lies in the cell membrane itself. The band 3 protein ... increased tyrosine phosphorylation of the band 3 protein, reduced sulfate anion transport through the cell membrane, and more ...
Hydroxyurea has also been prepared by converting a quaternary ammonium anion exchange resin from the chloride form to the ... Hydroxyurea lay dormant for more than fifty years until it was studied as part of an investigation into the toxicity of protein ... Antisickling Agents - Agents used to prevent or reverse the pathological events leading to sickling of erythrocytes in sickle ... ISBN 978-1-4144-0362-5. Platt OS (2008). "Hydroxyurea for the treatment of sickle cell anemia". N. Engl. J. Med. 358 (13): 1362 ...
Several possibilities (uniport, anion:anion exchange and anion:cation exchange) can account for the data. The physiologically ... "Crystal structure of the anion exchanger domain of human erythrocyte band 3". Science. 350 (6261): 680-684. doi:10.1126/science ... Nine encode proteins that transport HCO− 3. Functionally, eight of these proteins fall into two major groups: three Cl-HCO− 3 ... AE1 preferentially catalyzes anion exchange (antiport) reactions. Specific point mutations in human anion exchanger 1 (AE1) ...
... anion transport protein is a phylogenetically-preserved transport protein responsible for mediating the exchange of ... The erythrocyte and kidney forms are different isoforms of the same protein. The erythrocyte isoform of AE1, known as eAE1, is ... Band 3 anion transport protein, also known as anion exchanger 1 (AE1) or band 3 or solute carrier family 4 member 1 (SLC4A1), ... Tanner MJ (2002). "Band 3 anion exchanger and its involvement in erythrocyte and kidney disorders". Curr. Opin. Hematol. 9 (2 ...
The protein then undergoes a conformational change to a new 'closed'' conformation that exposes both the proton and lactate to ... For this reason, exchange of one monocarboxylate inside the cell with another outside is considerably faster than net transport ... MCT1 has a substrate binding site open to the extracellular matrix which binds a proton first followed by the lactate anion. ... Detailed kinetic analysis of monocarboxylate transport in erythrocytes revealed that MCT1 operates through an ordered mechanism ...
Anion exchange protein 3 is a membrane transport protein that in humans is encoded by the SLC4A3 gene. AE3 is functionally ... 1990). "Regulation of intracellular pH by a neuronal homolog of the erythrocyte anion exchanger". Cell. 59 (5): 927-37. doi: ... exchange protein but it is expressed primarily in brain neurons and in the heart. Like AE2 its activity is sensitive to pH. AE3 ... Morgans CW, Kopito RR (1993). "Association of the brain anion exchanger, AE3, with the repeat domain of ankyrin". J. Cell Sci. ...
The P1 adhesin (trypsin-sensitive protein) is a 120 kDa protein highly clustered on the surface of the attachment organelle tip ... Transmission of M. pneumoniae can only occur through close contact and exchange of aerosols by coughing due to the increased ... Adherence of M. pneumoniae to a host cell (usually a respiratory tract cell, but occasionally an erythrocyte or urogenital ... Local damage may also be a result of lactoferrin acquisition and subsequent hydroxyl radical, superoxide anion and peroxide ...
... anion exchange chromatography, cation exchange chromatography, and gel filtration chromatography. The recovered purified ... The main challenge, however, is to deliver protein to the nerve cells as proteins usually are not applicable as pills. The ... erythrocytes), or induce blood coagulation (clotting, e.g. mucrocetin). A common family of hemotoxins are snake venom ... After ion exchange there are generally further chromatographic purification steps and buffer exchange. However, chromatographic ...
Some of these proteins are linked to the exterior of the cell membrane. An example of this is the CD59 protein, which ... This random walk exchange allows lipid to diffuse and thus wander across the surface of the membrane. Unlike liquid phase ... Anions typically have a higher rate of diffusion through bilayers than cations. Compared to ions, water molecules actually have ... For instance, PS presence on the extracellular membrane face of erythrocytes is a marker of cell apoptosis, whereas PS in ...
found that red blood cells of the newt not only produce hemoglobin, but also ferritin, ribosomal proteins, and proteins assumed ... There is a release of erythrocytes from the spleen and the values in the blood are raised to high. Every time there is an ... What was discovered was that when the external concentration of sodium exceeds 10-20 mM within the presence of the Cl anion, ... The APH molecule, in short, plays a large role in the ion exchange across the membrane between the internal and external ...
To date, only the ZntA protein of Paramecium has been shown to be a Mg2+ channel. The mechanisms of Mg2+ transport by the ... stabilising anions or reactive intermediates, also including binding to ATP and activating the molecule to nucleophilic attack ... POTASSIUM/PROTON EXCHANGE ACROSS THE CHLOROPLAST ENVELOPE". Plant Physiology. 65 (2): 350-354. doi:10.1104/pp.65.2.350. PMC ... and Zinc in Normal Human Erythrocytes". Journal of Clinical Investigation. 44 (3): 379-389. doi:10.1172/JCI105151. PMC 292488 ...
ProteinsEdit. The Mg2+ ion tends to bind only weakly to proteins (Ka ≤ 105[46]) and this can be exploited by the cell to switch ... high energy of hydration and very low rate of ligand exchange in the inner coordination sphere, these steps are probably more ... stabilising anions or reactive intermediates, also including binding to ATP and activating the molecule to nucleophilic attack ... "Spectrochemical Analysis of Sodium, Potassium, Calcium, Magnesium, Copper, and Zinc in Normal Human Erythrocytes". Journal of ...
Kajita, M. et al.; Platinum Nanoparticle is a Useful Scavenger of Superoxide Anion and Hydrogen Peroxide. Free Radic. Res. 41, ... Platinum NPs are used as catalysts for proton exchange membrane fuel cell (PEMFC), for industrial synthesis of nitric acid, ... These effects are seen in different levels of gene expression measured through protein levels. Last is the developmental ... "Investigations on the Structural Damage in Human Erythrocytes Exposed to Silver, Gold, and Platinum Nanoparticles". Advanced ...
ROS also interacts with ERK pathway that leads to activation of Ras, MEK and MEK-like proteins. These proteins activate protein ... The blood cells (erythrocytes, leukocytes and platelets) are produced by hematopoiesis. The erythrocytes have as main function ... Reactome data available in a variety of standard formats, including BioPAX, SBML and PSI-MI, and also enable data exchange with ... One example of a protein that binds to adaptor proteins and become activated is PLC that is very important in the lymphocyte ...
Each subunit is composed of a protein chain tightly associated with a non-protein prosthetic heme group. Each protein chain ... NO is not released in the cytoplasm of red blood cells but transported out of them by an anion exchanger called AE1.[70] ... erythrocytes) of almost all vertebrates[4] (the exception being the fish family Channichthyidae[5]) as well as the tissues of ... In all proteins, it is the amino acid sequence that determines the protein's chemical properties and function. ...
Here it causes the reabsorption of sodium ions from the renal tubular fluid, in exchange for potassium ions which are secreted ... The abnormally high plasma ionized calcium concentrations cause conformational changes in many cell-surface proteins ( ... erythrocytes). The increase in RBCs leads to an increased hematocrit in the blood, and subsequent increase in hemoglobin that ... Metabolic: High anion gap *Ketoacidosis. *Diabetic ketoacidosis. *Alcoholic ketoacidosis. *Lactic. *Normal anion gap * ...
... a protein from rat heart homologous to a gap junction protein from liver". The Journal of Cell Biology. 105 (6 Pt 1): 2621-9. ... Hu, X; Dahl, G (1999). "Exchange of conductance and gating properties between gap junction hemichannels". FEBS Lett. 451 (2): ... with the exception of adult fully developed skeletal muscle and mobile cell types such as sperm or erythrocytes. Gap junctions ... genes can produce only the proteins that make up gap junction channels. An alternative naming system based on this protein's ...
"Glycated Hemoglobin in Uremic Patients as Measured by Affinity and Ion-Exchange Chromatography" (PDF). clinchem.com. Retrieved ... Glycation of proteins is a frequent occurrence, but in the case of hemoglobin, a nonenzymatic condensation reaction occurs ... or high erythrocyte turnover; in the presence of chronic renal or liver disease; after administration of high-dose vitamin C; ... 1. c. mmol. mol. =. [. D. C. C. T. H. B. A. 1. c. (. %. ). −. 2.14. ]. ×. 10.929. {\displaystyle \mathrm {IFCC} \,\mathrm { ...
... isothiocyanatostilbene disulphonate on sulphate exchange transport in resealed erythrocyte membranes. (6) Immunostaining of ... Monoclonal antibodies to the membrane domain of the human erythrocyte anion transport protein. Localization of the C-terminus ... Monoclonal antibodies to the membrane domain of the human erythrocyte anion transport protein. Localization of the C-terminus ... Monoclonal antibodies to the membrane domain of the human erythrocyte anion transport protein. Localization of the C-terminus ...
Erythrocyte" by people in this website by year, and whether "Anion Exchange Protein 1, Erythrocyte" was a major or minor topic ... Anion Exchange Protein 1, Erythrocyte [D12.776.157.530.450.162.110]. *Chloride-Bicarbonate Antiporters [D12.776.157.530.450.162 ... Anion Exchange Protein 1, Erythrocyte [D12.776.543.585.450.162.110]. *Chloride-Bicarbonate Antiporters [D12.776.543.585.450.162 ... "Anion Exchange Protein 1, Erythrocyte" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, ...
Erythrocyte" by people in this website by year, and whether "Anion Exchange Protein 1, Erythrocyte" was a major or minor topic ... "Anion Exchange Protein 1, Erythrocyte" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, ... A major integral transmembrane protein of the ERYTHROCYTE MEMBRANE. It is the anion exchanger responsible for electroneutral ... Below are the most recent publications written about "Anion Exchange Protein 1, Erythrocyte" by people in Profiles. ...
In both erythrocytes and the basolateral membrane of the collecting-duct α-intercalated cells, the role of … ... The membrane transporter anion exchanger 1 (AE1), or band 3, is a key component in the processes of carbon-dioxide transport in ... Anion Exchange Protein 1, Erythrocyte / chemistry* * Anion Exchange Protein 1, Erythrocyte / metabolism ... which catalyzes the anion-exchange reaction, has finally been determined. Each protomer of the AE1 dimer comprises two repeats ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex ... both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Major ... erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins ... Protein Feature View of PDB entries mapped to a UniProtKB sequence * Number of PDB entries for P78487: no matching PDB entries ...
The Erythrocyte Anion-Exchange Protein Ron R. Kopito, Harvey F. Lodish. Pages 39-59 ... Neutrophil Activation, Polyphosphoinositide Hydrolysis, and the Guanine Nucleotide Regulatory Proteins Paul H. Naccache, ... acid calcium channels development electron microscopy membrane transport metabolism microscopy morphology pharmacology proteins ...
Anion Exchange Protein 1, Erythrocyte / analysis. Anura / anatomy & histology, embryology*. Biological Markers. Cell ... Erythrocyte; 0/Biological Markers; 0/Lectins; 0/Peanut Agglutinin ... Previous Document: Immunodetection and localization of protein(s) related to retinal S-antigen (arrestin) in kidney.. Next ... The finding of the presence of band 3-like protein in the MR cells of Pelobates, is similar to the observations made in the ...
Anion Exchange Protein 1, Erythrocyte / antagonists & inhibitors*. Benzenesulfonates / pharmacology*. Biological Transport, ... Erythrocyte Membrane / drug effects, metabolism. Humans. Kinetics. Models, Biological. Nicotinic Acids / pharmacology*. ... 0/Anion Exchange Protein 1, Erythrocyte; 0/Benzenesulfonates; 0/Chlorides; 0/NBD-taurine; 0/Nicotinic Acids; 0/Oxadiazoles; ... Next Document: Response of the local heme environment of (carbonmonoxy)hemoglobin to protein dehydration.. ...
Erythrocyte / genetics * Anion Exchange Protein 1, Erythrocyte / metabolism ... Heterochromatin Protein 1gamma (HP1gamma), a protein containing a chromo-domain that recognizes H3K9 methylation, is also ... Christopher R Vakoc 1 , Sean A Mandat, Benjamin A Olenchock, Gerd A Blobel ... 1 Division of Hematology, The Childrens Hospital of Philadelphia, Philadelphia, Pennsylvania 19104, USA. ...
... is a protein that appears on old cells and acts as a specific signal for the termination of that cell by initiating the binding ... Knauf PA (1979) Erythrocyte anion exchange and the band 3 protein: Transport kinetics and molecular structure. Curr Top Membr ... Kopito RR, Lodish HF (1985) Structure of the murine anion exchange protein. J Cell Biochem 29: 1-17PubMedCrossRefGoogle Scholar ... Kurycki K, Shull G (1989) Primary structure of the rat kidney band 3 anion exchange protein deduced from a cDNA. J Biol Chem ...
... is an Escherichia coli Protein fragment 1 to 403 aa range, , 90% purity and validated in SDS-PAGE. ... Erythrocyte membrane protein band 3. *Erythroid anion exchange protein. *FR. *Froese blood group ... Detected in erythrocytes (at protein level) (PubMed:7506871, PubMed:26542571). Isoform 2 is expressed in kidney (at protein ... both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Major ...
This protein transports negatively charged atoms (anions) across cell membranes. Learn about this gene and related health ... The SLC4A1 gene provides instructions for making a protein known as anion exchanger 1 (AE1). ... erythrocyte membrane protein band 3. *erythroid anion exchange protein. *FR. *Froese blood group ... In addition to exchanging ions, the longer AE1 protein attaches to other proteins that make up the structural framework (the ...
Ab114931 is a protein fragment produced in Wheat germ and has been validated in WB, ELISA, SDS-PAGE. Abcam provides free… ... Plasma membrane anion exchange protein of wide distribution.. * Sequence similarities. Belongs to the anion exchanger (TC 2.A. ... erythrocyte band 3. *Erythrocyte membrane protein band 3 like 1. *HKB3. *MPB3L ... Protein concentration is above or equal to 0.05 mg/ml. Best use within three months from the date of receipt of this protein. ...
... such as deformability and anion exchange. Band 3 protein, also known as anion exchanger-1, plays an important role in these two ... Keywords: Band 3, oxidative stress, erythrocyte deformation, anion exchange Citation: Biorheology, vol. 44, no. 3, pp. 179-190 ... but also blunted the functional damage to erythrocytes, such as …deformability and anion exchange, without changing the level ... We show that oxidative stress activated caspase-3 inside the erythrocytes, which resulted in band 3 protein cleavage. ...
Transient receptor potential ankyrin 1 (TRPA1) is an ion channel known to mediate nociception and neurogenic inflammation, and ... ANION EXCHANGE PROTEIN 1, ERYTHROCYTE). Ankyrin repeats cooperatively fold into domains that mediate molecular recognition via ... It functions as a receptor for SERRATE-JAGGED PROTEINS and Delta1 (DLK1) protein to control cell fate determination. ... Protein motif that contains a 33-amino acid long sequence that often occurs in tandem arrays. This repeating sequence of 33- ...
... hiv envelope protein gp41 MeSH D12.776.543.550.190.110 -- anion exchange protein 1, erythrocyte MeSH D12.776.543.550.190.276 ... erythrocyte MeSH D12.776.543.585.450.162.234 -- organic anion transport protein 1 MeSH D12.776.543.585.450.162.235 -- ... sodium-phosphate cotransporter proteins, type iii MeSH D12.776.543.585.450.162.110 -- anion exchange protein 1, erythrocyte ... anion exchange protein 1, erythrocyte MeSH D12.776.543.550.190.442 -- potassium-hydrogen antiporters MeSH D12.776.543.550. ...
Background: Anion exchange protein 1 (AE1), also named solute carrier family 4 member 1 (SLC4A1), is an anion transporter that ... A different isoform of AE1 is a major integral membrane structure protein of erythrocytes, where it plays a critical role in ... Background: Anion exchange protein 1 (AE1), also named solute carrier family 4 member 1 (SLC4A1), is an anion transporter that ... The MRP proteins are membrane proteins that function as organic anion pumps involved in the cellular removal of cancer drugs (2 ...
J:35614 Kopito RR, et al., Primary structure and transmembrane orientation of the murine anion exchange protein. Nature. 1985 ... Homozygotes for null mutations exhibit retarded growth, severe spherocytosis, hemolytic anemia, lack of erythrocyte glycophorin ... protein coding gene. Chr11:102348820-102366203 (-). 129S1/SvImJ MGP_129S1SvImJ_G0019232. protein coding gene. Chr11:105314974- ... protein coding gene. Chr11:100876913-100894310 (-). AKR/J MGP_AKRJ_G0019169. protein coding gene. Chr11:103990994-104009893 (-) ...
To distinguish contaminants such as plasma or erythrocyte proteins from true platelet proteins, we monitored protein abundance ... Peptides were eluted after digestion with trypsin and subjected to a StageTip-based (14) strong anion exchange fractionation ( ... However, contaminants also included known erythrocyte markers such as erythrocytic spectrin, erythrocyte membrane protein band ... We accurately measured the absolute protein concentrations of 13 platelet proteins using SILAC-protein epitope signature tags ...
... anion exchange protein 1, erythrocyte MeSH D12.776.157.530.450.162.276 -- potassium-hydrogen antiporters MeSH D12.776.157.530. ... erythrocyte MeSH D12.776.157.530.450.162.193 -- chloride-bicarbonate antiporters MeSH D12.776.157.530.450.162.193.500 -- ... organic anion transport polypeptide c MeSH D12.776.157.530.450.074.500.781.750 -- organic anion transport protein 1 MeSH ... anion transport proteins MeSH D12.776.157.530.450.074.249 -- halorhodopsins MeSH D12.776.157.530.450.074.500 -- organic anion ...
Erythrocyte Anion Exchange Protein 1 Anions Erythrocytes Congenital Hemolytic Anemia Chloride-Bicarbonate Antiporters ... Crystallization of Human Erythrocyte Band 3, the anion exchanger, at the International Space Station "KIBO". Hatae, H., Inaka, ... Crystal structure of the anion exchanger domain of human erythrocyte band 3. Arakawa, T., Kobayashi-Yurugi, T., Alguel, Y., ... Determination of saposin proteins (sphingolipid activator proteins) in human tissues. Morimoto, S., Yamamoto, Y., OBrien, J. S ...
Erythrocyte Anion Exchange Protein 1 Protein Transport Cell Size Membrane Proteins 2012 ... Na+/H+ and Na+/NH4 + exchange activities of zebrafish NHE3b expressed in Xenopus oocytes. Ito, Y., Kato, A., Hirata, T., Hirose ... Slc4-like anion transporters of the larval mosquito alimentary canal. Linser, P. J., Neira Oviedo, M., Hirata, T., Seron, T. J ... Transport proteins NHA1 and NHA2 are essential for survival, but have distinct transport modalities. Chintapalli, V. R., Kato, ...
Anion transport mechanisms are found in mammalian cell membranes in the form of exchangers or antiporters (Passow, 1987; ... Kopito, R. R., and Lodish, H. F., 1985: Structure of the murine anion exchange protein,J. Cell. Bioch., 29:1-17.CrossRefGoogle ... Frohlich, O., and Gunn, R. B., 1986: Erythrocyte anion transport: the kinetics of a single site obligatory exchange system, ... Jay, D., and Cantley, L. C., 1986: Structural aspects of the red cell anion exchange protein,Ann. Rev. Biochem., 55:511-538 ...
What is Cytoskeletal proteins? Meaning of Cytoskeletal proteins medical term. What does Cytoskeletal proteins mean? ... Looking for online definition of Cytoskeletal proteins in the Medical Dictionary? Cytoskeletal proteins explanation free. ... Neurobehavioral deficits in mice lacking the erythrocyte membrane cytoskeletal protein 4.. Abnormal Erythrocyte Anion Exchange ... redirected from Cytoskeletal proteins). Also found in: Dictionary, Thesaurus, Encyclopedia. cytoskeleton. [si″to-skel´ĕ-ton] a ...
CD233 is a phylogenetically preserved transport protein responsible for mediating the electroneutral anion exchange of chloride ... membrane as well as for the normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins ... It is the major integral membrane glycoprotein of the erythrocyte membrane and is required for the normal flexibility and ... CD233 mediates the chloride-bicarbonate exchange in the kidney, and is required for the normal acidification of the urine. ...
  • Identification of Genetic Variants Linking Protein C and Lipoprotein Metabolism: The ARIC Study (Atherosclerosis Risk in Communities). (harvard.edu)
  • Deutscher, J. How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria. (vobemamatil.gq)
  • Galtieri, Antonio 2008-09-29 00:00:00 To further clarify some peculiar molecular mechanisms related to the physiology and pathophysiology of erythrocytes with respect to oxygen binding and release, metabolism and senescence, we investigated the oxidative effects of gemfibrozil in normal and beta-thalassemic red blood cells. (deepdyve.com)
  • Our results showed that the oxidative stress promoted by the drug, through a direct interaction with hemoglobin, may lead to activation of caspase 3, which in turn influences the band 3 anion flux and glucose metabolism. (deepdyve.com)
  • Bosman GJCGM, Vollaard CH, De Grip WJ (1995) Maintenance of neuronal homeostasis: the role of anion exchange proteins in regulation of intracellular pH. (springer.com)
  • Na/HCO 3 cotransporters (NBCs) are functionally diverse proteins that are involved in the regulation of intracellular pH (pH i ), absorption or secretion of HCO 3 − , and maintenance of ion homeostasis in many tissues. (rupress.org)
  • The mutation Lys(539)Ala at the covalent DIDS-reaction site of AE1 reduced the DIDS sensitivity, demonstrating that (1) the conductive pathway is intrinsic to AE1Delta(6: 7) and (2) the conductive pathway has some commonality with the electroneutral anion-exchange pathway. (xenbase.org)
  • Cabantchik ZI, Rothstein A (1972) The nature of the membrane sites controlling anion permeability of human red blood cells as determined by studies with disulfonic stilbene derivitives. (springer.com)
  • 1 Mutated forms of band 3 have been found to be less efficient in transporting anions and have a decreased affinity to stilbene disulfonic acid derivatives. (haematologica.org)
  • Although the E. coli genome encodes several proteins with esterase activity, neither wild-type strains nor KO11 contained significant ethyl acetate esterase activity. (asm.org)
  • With a diameter of only 0.5 to 1 μm in mice and 2 to 5 μm in humans, platelets are the smallest blood cell type and have a very short life span of 3 to 4 days (7 to 10 days in humans). (mcponline.org)
  • This asymmetry causes the putative substrate-binding site to be exposed only to the extracellular space, consistent with the expectation that anion exchange occurs via an alternating-access mechanism. (nih.gov)
  • By using α-naphthyl acetate as a model substrate, optimal activity was observed at pH 7.5 and 40°C. The K m and V max for α-naphthyl acetate were 18 μM and 48.1 μmol · min −1 · mg of protein1 , respectively. (asm.org)
  • In yeasts, ethyl acetate production has been ascribed to three acetyltransferases ( 26 ), although more than 10 additional candidates are also present on the annotatedgenome ( http://genome-www.stanford.edu/Saccharomyces/ ).The E. coli genome contains at least 13 genes encoding acetyltransferase- or esterase-like proteins with various substrate specificities ( 4 ). (asm.org)
  • In this study, we show that these related proteins are proteases with divergent substrate specificities, suggesting different functions. (asm.org)
  • Our data suggest that, despite the homologies observed among these proteins, the SPATEs have different pathogenetic functions only partly dependent on their substrate specificities. (asm.org)
  • A mannose sensitive adhesin (~31kDa) of Salmonella enterica serovar Typhimurium (Fim+ve strain) was purified by sequential chromatography on Mono Q HR 5/5 anion exchange column and Superose 12 HR 10/30-gel filtration column in the FPLC system. (medcraveonline.com)
  • The overall purification is divided in three general steps: An ammonium sulfate preciptation giving a crude protein solution, a bulk purification which can be adjusted to the exact sample properties (volume, cell type, cross contamination) utilizing alternatively 3 different methods (AX, HIC, covalent chromatography), and a polishing step giving pure protein after size exclusion chromatography (Fig. 1). (researchsquare.com)
  • Final purification was performed by liquid chromatography using the ion-exchange gel DEAE-Sepharose FF. (scielo.br)
  • Materials and methods Guduchi ImP was purified from dry stem powder extract by anion-exchange chromatography on Q-Sepharose. (cftri.com)
  • Although the initial studies were done using human erythrocytes as a model senescent cell antigen has been found on all cells examined (Kay 1981). (springer.com)
  • Choosing non-denaturing conditions, we developed a several purification schemes in order to obtain αSyn from human erythrocytes, enabling researchers to employ biophysical techniques in order to elucidate its native structure and properties. (researchsquare.com)
  • Here we introduce a novel way of purifying human α-Synuclein from human erythrocytes, leaving the physiological conformation of the protein intact. (researchsquare.com)
  • Guduchi ImP does not possess hemagglutination activity (towards rabbit and human erythrocytes of all blood groups) indicating that the immunomodulatory protein is not a lectin. (cftri.com)
  • 1 Red blood cells (RBC) from patients with CHC have increased membrane permeability to Na + and K + ions, which is particularly pronounced at 0°C. 1 - 6 In rare cases, these patients' RBC have a deficiency of stomatin accompanied by mental retardation, seizures, cataracts, and hepatosplenomegaly. (haematologica.org)
  • This section describes fluorescent indicators for intracellular and extracellular chloride together with an assortment of analytical reagents and methods for direct or indirect quantitation of other inorganic anions, including bromide, iodide, hypochlorite, cyanide,nitrite, nitrate, phosphate, pyrophosphate and selenide. (thermofisher.com)
  • Mild trypsin treatment of ghosts, which cleaves off the cytoplasmic portion of band 3 without affecting spectrin, actin, and protein 4.1, increased the intercompartmental hop rate of band 3 by a factor of 6, whereas it did not change the corral size and the microscopic diffusion rate within a corral. (nih.gov)
  • Bovine albumin plays a prevalent role as a basic component of several biological reagents for diagnostic use, mainly for immunohematological tests, such as the antisera used in reactions for in vitro detection of erythrocyte antigens or of specific antibodies in blood recipients or donors. (scielo.br)
  • Other DNase 1-sensitive domains containing one or more expressed genes have been mapped in chicken and mammalian cells. (biomedcentral.com)