Cation Transport Proteins
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.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
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.
The first chemical element in the periodic table. It has the atomic symbol H, atomic number 1, and atomic weight [1.00784; 1.00811]. It exists, under normal conditions, as a colorless, odorless, tasteless, diatomic gas. Hydrogen ions are PROTONS. Besides the common H1 isotope, hydrogen exists as the stable isotope DEUTERIUM and the unstable, radioactive isotope TRITIUM.
Amino Acid Sequence
Protein-lipid combinations abundant in brain tissue, but also present in a wide variety of animal and plant tissues. In contrast to lipoproteins, they are insoluble in water, but soluble in a chloroform-methanol mixture. The protein moiety has a high content of hydrophobic amino acids. The associated lipids consist of a mixture of GLYCEROPHOSPHATES; CEREBROSIDES; and SULFOGLYCOSPHINGOLIPIDS; while lipoproteins contain PHOSPHOLIPIDS; CHOLESTEROL; and TRIGLYCERIDES.
Electron Transport Complex I
A flavoprotein and iron sulfur-containing oxidoreductase complex that catalyzes the conversion of UBIQUINONE to ubiquinol. In MITOCHONDRIA the complex also couples its reaction to the transport of PROTONS across the internal mitochondrial membrane. The NADH DEHYDROGENASE component of the complex can be isolated and is listed as EC 126.96.36.199.
Genetic Complementation Test
Sequence Homology, Amino Acid
Protein Structure, Secondary
Membrane Transport Proteins
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
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.
Inactivation of the glucose 6-phosphate transporter causes glycogen storage disease type 1b. (1/1325)Glycogen storage disease type 1b (GSD-1b) is proposed to be caused by a deficiency in microsomal glucose 6-phosphate (G6P) transport, causing a loss of glucose-6-phosphatase activity and glucose homeostasis. However, for decades, this disorder has defied molecular characterization. In this study, we characterize the structural organization of the G6P transporter gene and identify mutations in the gene that segregate with the GSD-1b disorder. We report the functional characterization of the recombinant G6P transporter and demonstrate that mutations uncovered in GSD-1b patients disrupt G6P transport. Our results, for the first time, define a molecular basis for functional deficiency in GSD-1b and raise the possibility that the defective G6P transporter contributes to neutropenia and neutrophil/monocyte dysfunctions characteristic of GSD-1b patients. (+info)
Topology of the membrane domain of human erythrocyte anion exchange protein, AE1. (2/1325)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)
Functional importance and local environments of the cysteines in the tetracycline resistance protein encoded by plasmid pBR322. (3/1325)The properties of the cysteines in the pBR322-encoded tetracycline resistance protein have been examined. Cysteines are important but not essential for tetracycline transport activity. None of the cysteines reacted with biotin maleimide, suggesting that they are shielded from the aqueous phase or reside in a negatively charged local environment. (+info)
Na+/H+ antiporter activity in hamster embryos is activated during fertilization. (4/1325)This study characterized the activation of the regulatory activity of the Na+/H+ antiporter during fertilization of hamster embryos. Hamster oocytes appeared to lack any mechanism for the regulation of intracellular pH in the acid range. Similarly, no Na+/H+ antiporter activity could be detected in embryos that were collected from the reproductive tract between 1 and 5 h post-egg activation (PEA). Activity of the Na+/H+ antiporter was first detected in embryos collected at 5.5 h PEA and gradually increased to reach maximal activity in embryos collected at 7 h PEA. Parthenogenetically activated one-cell and two-cell embryos demonstrate Na+/H+ antiporter activity, indicating that antiporter activity is maternally derived and initiated by activation of the egg. The inability of cycloheximide, colchicine, or cytochalasin D to affect initiation of antiporter activity indicates that antiporter appearance is not dependent on the synthesis of new protein or recruitment of existing protein to the cell membrane. In contrast, incubation of one-cell embryos with sphingosine did inhibit the appearance of Na+/H+ antiporter activity, showing that inhibition of normal protein kinase C activity is detrimental to antiporter function. Furthermore, incubation of oocytes with a phorbol ester which stimulates protein kinase C activity induced Na+/H+ antiporter activity in oocytes in which the activity was previously absent. Incubation with an intracellular calcium chelator also reduced the appearance of antiporter activity. Taken together, these data indicate that the appearance of Na+/H+ antiporter activity following egg activation may be due, at least in part, to regulation by protein kinase C and intracellular calcium levels. (+info)
Non-selective voltage-activated cation channel in the human red blood cell membrane. (5/1325)Using the patch-clamp technique, a non-selective voltage-activated Na+ and K+ channel in the human red blood cell membrane was found. The channel operates only at positive membrane potentials from about +30 mV (inside positive) onwards. For sodium and potassium ions, similar conductances of about 21 pS were determined. Together with the recently described K+(Na+)/H+ exchanger, this channel is responsible for the increase of residual K+ and Na+ fluxes across the human red blood cell membrane when the cells are suspended in low ionic strength medium. (+info)
Prospective analysis of traits related to 6-year change in sodium-lithium countertransport. Gubbio Population Study Research Group. (6/1325)Sodium-lithium countertransport (Na-Li CT) activity in red blood cells relates cross-sectionally and longitudinally to blood pressure and hypertension. Lifestyle and metabolic factors relate cross-sectionally to this sodium transporter. The aim of this study was to conduct a prospective analysis of 6-year Na-Li CT change and of traits related to Na-Li CT change. In 2183 participants in the Gubbio Population Study (972 men and 1211 women; baseline ages, 18 to 74 years), the following data collected at baseline and 6-year follow-up were analyzed: Na-Li CT; gender; age; body mass index (BMI); blood pressure; antihypertensive treatment; alcohol intake; smoking habits; urinary sodium-to-potassium ratio; and plasma cholesterol, glucose, uric acid, sodium, potassium, and triglycerides (measured only at follow-up). Six-year changes were defined as follow-up minus baseline values. Na-Li CT was higher at follow-up than at baseline in both genders (P<0.001). Baseline Na-Li CT; baseline and change values of BMI; and change values of alcohol intake, plasma potassium, and plasma glucose related to Na-Li CT change significantly and independently with control for other variables. Follow-up plasma triglyceride levels also related independently to Na-Li CT change. Coefficients were positive for BMI, alcohol intake, and plasma glucose and triglyceride levels and were negative for baseline Na-Li CT and plasma potassium levels. Baseline and change values of other variables did not relate significantly to Na-Li CT change. In conclusion, in prospective analyses, BMI, alcohol intake, plasma glucose, and lipids were directly related to Na-Li CT change; baseline Na-Li CT and plasma potassium levels were inversely related. The data support the concept that lifestyle and related metabolic factors influence Na-Li CT. (+info)
Peptide-bound major histocompatibility complex class I molecules associate with tapasin before dissociation from transporter associated with antigen processing. (7/1325)Major histocompatibility complex (MHC) class I molecules present antigenic peptides to CD8 T cells. The peptides are generated in the cytosol, then translocated across the membrane of the endoplasmic reticulum by the transporter associated with antigen processing (TAP). TAP is a trimeric complex consisting of TAP1, TAP2, and tapasin (TAP-A) as indicated for human cells by reciprocal coprecipitation with anti-TAP1/2 and anti-tapasin antibodies, respectively. TAP1 and TAP2 are required for the peptide transport. Tapasin is involved in the association of class I with TAP and in the assembly of class I with peptide. The mechanisms of tapasin function are still unknown. Moreover, there has been no evidence for a murine tapasin analogue, which has led to the suggestion that murine MHC class I binds directly to TAP1/2. In this study, we have cloned the mouse analogue of tapasin. The predicted amino acid sequence showed 78% identity to human tapasin with identical consensus sequences of signal peptide, N-linked glycosylation site, transmembrane domain and double lysine motif. However, there was less homology (47%) found at the predicted cytosolic domain, and in addition, mouse tapasin is 14 amino acids longer than the human analogue at the C terminus. This part of the molecule may determine the species specificity for interaction with MHC class I or TAP1/2. Like human tapasin, mouse tapasin binds both to TAP1/2 and MHC class I. In TAP2-mutated RMA-S cells, both TAP1 and MHC class I were coprecipitated by anti-tapasin antiserum indicative of association of tapasin with TAP1 but not TAP2. With crosslinker-modified peptides and purified microsomes, anti-tapasin coprecipitated both peptide-bound MHC class I and TAP1/2. In contrast, anti-calreticulin only coprecipitated peptide-free MHC class I molecules. This difference in association with peptide-loaded class I suggests that tapasin functions later than calreticulin during MHC class I assembly, and controls peptide loading onto MHC class I molecules in the endoplasmic reticulum. (+info)
Granulocyte-macrophage colony-stimulating factor modulates tapasin expression in human neutrophils. (8/1325)Differential display-polymerase chain reaction (DD-PCR) was used to evaluate changes in mRNA expression of granulocyte-macrophage colony-stimulating factor (GM-CSF) treated human neutrophils to better understand how this cytokine affects the functions of neutrophils at the molecular level. Although a variety of cDNA fragments were identified as modulated by GM-CSF with the use of DD-PCR, one fragment in particular, NGS-17 (neutrophil GM-CSF-stimulated fragment #17), was characterized. The NGS-17 fragment hybridized to a 3.8-kh mRNA that encodes for a protein of a predicted molecular mass of 47.6 kDa. After cloning and sequencing, this gene was found to code for the recently sequenced tapasin or TAP-A protein. Immunoprecipitation and immunoblotting studies using anti-tapasin antibodies showed that tapasin is expressed in neutrophils and is associated with the MHC class I-TAP complex. Moreover, tapasin expression was found to be induced by dimethyl sulfoxide and by retinoic acid in HL-60 cells. This is the first report on the expression of tapasin in human neutrophils. It provides novel information, at the molecular level, on how GM-CSF enhances the functions of these cells. (+info)
Na+/H+ Antiporters Antiporters, such as Na+/H+ antiporter protein, allows ions H+ and Na+ to travel across a membrane in order ... Antiporters at the US National Library of Medicine Medical Subject Headings (MeSH) Pak, J. E.; Ekende, E. N.; Kifle, E. G.; et ... These antiporters can also close their channel to stop sodium from entering the cell, along with allowing excess sodium within ... Na+/H+ antiporters have been reviewed. In secondary active transport, one species of solute moves along its electrochemical ...
The Ca2+:cation antiporter (CaCA) family (TC# 2.A.19) is a member of the cation diffusion facilitator (CDF) superfamily. This ... The original text was at "2.A.19 The Ca2+:Cation Antiporter (CaCA) Family" Portal: Biology (Articles with imported dually ... H+ antiporter of E. coli and the sixth contains only one distant S. cerevisiae homologue of unknown function. Several ... "Isolation and functional characterization of Ca2+/H+ antiporters from cyanobacteria". The Journal of Biological Chemistry. 279 ...
... antiporter 1 Sodium-hydrogen antiporter 2 Sodium-hydrogen antiporter 3 Sodium-hydrogen antiporter 4 Sodium-hydrogen antiporter ... 5 Sodium-hydrogen antiporter 6 Sodium-hydrogen antiporter 7 Sodium-hydrogen antiporter 8 Sodium-hydrogen antiporter 9 There are ... H+ Antiporter (NhaB) Family TC# 2.A.35 - Na+:H+ Antiporter (NhaC) Family TC# 2.A.36 - Monovalent Cation:Proton Antiporter-1 ( ... Defects in Na+/H+ antiporters may result in heart or kidney failure. Angiotensin II upregulates this antiporter in the proximal ...
Sodium-hydrogen antiporter 1
... is an isoform of sodium-hydrogen antiporter that in humans is encoded by the SLC9A1 gene. The Na+/H+ antiporter (SLC9A1) is a ... Sodium-hydrogen antiporter 1 has been shown to interact with carbonic anhydrase II and CHP. It is also the target of the ... The sodium-hydrogen antiporter 1 (NHE-1) also known as sodium/hydrogen exchanger 1 or SLC9A1 (SoLute Carrier family 9A1) ... Dudley CR, Giuffra LA, Tippett P, Kidd KK, Reeders ST (November 1990). "The Na+/H+ antiporter: a "melt" polymorphism allows ...
The Ca2+:H+ antiporter-2 (CaCA2) family (TC# 2.A.106) is a member of the lysine exporter (LysE) superfamily. Note that this ... Gdt1p and TMEM165 are probably Golgi-localized Ca2+:H+ antiporters. Modification of the Golgi Ca2+ and pH balance could explain ... "2.A.106 Ca2+:H+ Antiporter-2 (CaCA2) Family". Transporter Classification Database. Retrieved 2016-03-01. Portal: Biology v t e ... family differs from the calcium:cation antiporter (CaCA) family which belongs to the cation diffusion facilitator (CDF) ...
ATP:ADP antiporter family
The ATP:ADP Antiporter (AAA) Family (TC# 2.A.12) is a member of the major facilitator superfamily. Members of the AAA family ... As of this edit, this article uses content from "2.A.12 The ATP:ADP Antiporter (AAA) Family", which is licensed in a way that ... The transport reaction catalyzed by the antiporters is: ATP (out) + ADP (in) ⇌ ATP (in) + ADP (out) The AAA family proteins are ...
Sodium-hydrogen antiporter 3
The NHE3 antiporter imports one sodium ion into the cytosol of a tubule cell as it ejects one hydrogen ion from the cell into ... Sodium-hydrogen antiporter 3 also known as sodium-hydrogen exchanger 3 (NHE3) or solute carrier family 9 member 3 (SLC9A3) is a ... SLC9A3 is a sodium-hydrogen antiporter. It is found on the apical side of the epithelial cells of the proximal tubule of the ... The NHE3 antiporter indirectly contributes to blood buffering capacity because hydrogen ions that are ejected are the products ...
Sodium-hydrogen antiporter 2
Sodium-hydrogen exchanger 2 is a protein that in humans is encoded by the SLC9A2 gene. Solute carrier family GRCh38: Ensembl release 89: ENSG00000115616 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000026062 - Ensembl, May 2017 "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine. "Entrez Gene: SLC9A2 solute carrier family 9 (sodium/hydrogen exchanger), member 2". Chow CW (1999). "Regulation and intracellular localization of the epithelial isoforms of the Na+/H+ exchangers NHE2 and NHE3". Clinical and Investigative Medicine. 22 (5): 195-206. PMID 10579058. Kulanthaivel P, Furesz TC, Moe AJ, et al. (1992). "Human placental syncytiotrophoblast expresses two pharmacologically distinguishable types of Na(+)-H+ exchangers, NHE-1 in the maternal-facing (brush border) membrane and NHE-2 in the fetal-facing (basal) membrane". ...
Monovalent cation:proton antiporter-2
CPA superfamily Sodium-Proton antiporter Monovalent cation:Proton antiporter-1 Monovalent cation:Proton antiporter-3 ... depending on conditions Na+/H+ antiporter of Enterococcus hirae (i.e., NapA, TC# 2.A.37.2.1) K+/H+ antiporter of S. cerevisiae ... Waser M, Hess-Bienz D, Davies K, Solioz M (March 1992). "Cloning and disruption of a putative NaH-antiporter gene of ... Portal: Biology As of this edit, this article uses content from "2.A.37 The Monovalent Cation:Proton Antiporter-2 (CPA2) Family ...
Monovalent cation:proton antiporter-3
Sodium-Proton antiporter Monovalent Cation (K+ or Na+):Proton Antiporter-1 Monovalent Cation (K+ or Na+):Proton Antiporter-2 ... In this system, YufT is believed to be responsible for Na+:H+ antiporter activity, but it does not have activity in the absence ... The Monovalent Cation (K+ or Na+):Proton Antiporter-3 (CPA3) Family (TC# 2.A.63) is a member of the Na+ transporting Mrp ... Portal: Biology As of this edit, this article uses content from "2.A.63 The Monovalent Cation (K+ or Na+):Proton Antiporter-3 ( ...
Basic amino acid antiporter family
The Basic Amino Acid Antiporter (ArcD) family (TC# 2.A.118) is a constituent of the IT superfamily. This family consists of ... Portal: Biology As of this edit, this article uses content from "2.A.118 The Basic Amino Acid Antiporter (ArcD) Family", which ...
Monovalent cation:proton antiporter-1
Sodium-proton antiporter Monovalent cation:Proton antiporter-2 Monovalent cation:Proton antiporter-3 Transporter Classification ... proton antiporter-1 family in Arabidopsis thaliana, encodes a putative Li/H antiporter". The Plant Journal. 49 (4): 718-28. doi ... The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC# 2.A.36) is a large family of proteins derived from Gram-positive ... Portal: Biology As of this edit, this article uses content from "2.A.36 The Monovalent Cation:Proton Antiporter-1 (CPA1) Family ...
Sodium-hydrogen antiporter 3 regulator 1
... is a regulator of Sodium-hydrogen antiporter 3. It is encoded by the gene SLC9A3R1. It ... Sodium-hydrogen antiporter 3 regulator 1 has been shown to interact with: ADRB2, Beta-catenin, CFTR, GNAQ, OPRK1, PAG1, PDGFRA ...
Na+/H+ antiporter A (NhaA) family (TC# 2.A.33) contains a number of bacterial sodium-proton antiporter (SPAP) proteins. These ... Sodium-Proton antiporter Antiporter Transporter Classification Database Williams KA, Geldmacher-Kaufer U, Padan E, Schuldiner S ... antiporter participates in the periplasmic cation passage and pH regulation of the antiporter". Journal of Molecular Biology. ... Na+-H+ antiporters are integral membrane proteins that exchange Na+ for H+ across the cytoplasmic membrane and many ...
Antiporter Symporter Cammack, Richard; Atwood, Teresa; Campbell, Peter; Parish, Howard; Smith, Anthony; Vella, Frank; Stirling ... Wolfersberger, MG (November 1994). "Uniporters, Symporters and Antiporters". J Exp Biol. 196: 5-6. PMID 7823043. Hoppe, U. ( ...
An example of an antiporter mediated transport protein is the sodium-calcium antiporter, a transport protein involved in ... This transport protein is an antiporter system because it transports three sodium ions across the plasma membrane in exchange ... WOLFERSBERGER, MICHAEL (1994). "Uniporters, symporters and antiporters" (PDF). Department of Biology, Temple University, ...
In an antiporter two species of ions or other solutes are pumped in opposite directions across a membrane. One of these species ... In an antiporter, one substrate is transported in one direction across the membrane while another is cotransported in the ... This antiporter mechanism is important within the membranes of cardiac muscle cells in order to keep the calcium concentration ... An example is the sodium-calcium exchanger or antiporter, which allows three sodium ions into the cell to transport one calcium ...
Membrane transport protein
2.A: Porters (uniporters, symporters, antiporters), SLCs. Excitatory amino acid transporters (EAATs) EAAT1 EAAT2 EAAT3 EAAT4 ...
A Proton gradient moves the ions into the vacuole by proton-sodium antiporter or the proton-calcium antiporter. In plants, ... Antiporters and symporters both transport two or more different types of molecules at the same time in a coupled movement. An ... In contrast to antiporters, symporters move ions or molecules in the same direction. In this case both ions being transported ... The AE1 antiporter is essential in the removal of carbon dioxide waste that is converted to bicarbonate inside the erythrocyte ...
ClCF proteins have been shown to function as fluoride-specific fluoride/proton antiporters. The three-dimensional structure of ... "Fluoride resistance and transport by riboswitch-controlled CLC antiporters". Proc Natl Acad Sci U S A. 109 (38): 15289-15294. ...
Glucose-6-phosphate exchanger SLC37A2
... glucose-6-phosphate antiporters". PLOS ONE. 6 (9): e23157. Bibcode:2011PLoSO...623157P. doi:10.1371/journal.pone.0023157. PMC ...
Glucose-6-phosphate exchanger SLC37A1
... inorganic phosphate antiporter, transporting glucose 6-phosphate from the cytoplasm into the lumen of the ER, while ... glucose-6-phosphate antiporters". PLOS ONE. 6 (9): e23157. Bibcode:2011PLoSO...623157P. doi:10.1371/journal.pone.0023157. PMC ...
Multidrug and toxin extrusion protein 2
"Entrez Gene: MATE2 H+/organic cation antiporter". Morita Y, Kodama K, Shiota S, Mine T, Kataoka A, Mizushima T, Tsuchiya T ( ... NorM seems to function as drug/sodium antiporter which is the first example of Na+-coupled multidrug efflux transporter ... organic cation antiporters". Biochemical Pharmacology. 74 (2): 359-71. doi:10.1016/j.bcp.2007.04.010. hdl:2433/124277. PMID ... "Identification and functional characterization of a new human kidney-specific H+/organic cation antiporter, kidney-specific ...
malate-alpha-ketoglutarate antiporter in the inner membrane. glutamate-aspartate antiporter in the inner membrane. The primary ... The second antiporter (the glutamate-aspartate antiporter) imports glutamate from the cytosol into the matrix and exports ... Once malate is formed, the first antiporter (malate-alpha-ketoglutarate) imports the malate from the cytosol into the ...
Specifically, he focuses on the multidrug antiporter EmrE. Investigation of its subunit structure led the Schuldiner Group to ... an electrogenic antiporter from Escherichia coli. J. Biol. Chem. 268, 5382-5387 Schuldiner, S., Shirvan, A., Stern-Bach, Y., ...
See: Sodium-proton antiporter Non-contrast helical CT. See computed tomography This disambiguation page lists articles ...
Antiporters also use the concentration gradient of one molecule to move another up its concentration gradient but the coupled ... There are different types of transporters including, pumps, uniporters, antiporters, and symporters. Active transporters or ion ...
Sodium-hydrogen antiporter Antiporter Transporter Classification Database Prakash, Shraddha; Cooper, Garret; Singhi, Soumya; ... Portal: Biology As of this edit, this article uses content from "2.A.34 The NhaB Na+:H+ Antiporter (NhaB) Family", which is ... The E. coli NhaB is 58% identical to the orthologous Vibrio alginolyticus Na+/H+ antiporter. Although the latter protein is ... antiporter NhaB of Vibrio alginolyticus plays a role in its activity". Journal of Bacteriology. 183 (19): 5762-5767. doi: ...
It also appears to inhibit the cystine-glutamate antiporter. It is a codrug which is a combination of sulfapyridine and 5- ... Bridges, Richard J; Natale, Nicholas R; Patel, Sarjubhai A (1 January 2012). "System xc- cystine/glutamate antiporter: an ...
One is believed to be a Na+:H+ antiporter; the other is a malate·H+:lactate·Na+ antiporter. Several paralogues are found in ... Sodium-Proton antiporter Antiporter Transporter Classification Database Ivey, D. M.; Guffanti, A. A.; Bossewitch, J. S.; Padan ... Ito, M.; Guffanti, A. A.; Zemsky, J.; Ivey, D. M.; Krulwich, T. A. (1997-06-01). "Role of the nhaC-encoded Na+/H+ antiporter of ... Portal: Biology As of this edit, this article uses content from "2.A.35 The NhaC Na+:H+ Antiporter (NhaC) Family", which is ...
Potassium-Hydrogen Antiporters | Harvard Catalyst Profiles | Harvard Catalyst
"Potassium-Hydrogen Antiporters" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ( ... This graph shows the total number of publications written about "Potassium-Hydrogen Antiporters" by people in Harvard Catalyst ... Below are the most recent publications written about "Potassium-Hydrogen Antiporters" by people in Profiles. ... Below are MeSH descriptors whose meaning is more general than "Potassium-Hydrogen Antiporters". ...
The Cl-/H+ antiporter ClC-7 is the primary chloride permeation pathway in lysosomes - PubMed
The Cl-/H+ antiporter ClC-7 is the primary chloride permeation pathway in lysosomes Austin R Graves et al. Nature. 2008. . ... The Cl-/H+ antiporter ClC-7 is the primary chloride permeation pathway in lysosomes Austin R Graves 1 , Patricia K Curran, ... Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5. Picollo A, Pusch M. Picollo A, et al. Nature. ... The chloride antiporter CLCN7 is a modifier of lysosome dysfunction in FIG4 and VAC14 mutants. Cao X, Lenk GM, Mikusevic V, ...
EVIDENCE FOR INCREASED INVIVO NA+/H+ ANTIPORTER ACTIVITY IN SKELETAL-MUSCLE OF SPONTANEOUSLY HYPERTENSIVE RATS - Centre for...
Tuberostemonine may enhance the function of the SLC7A11/glutamate antiporter to restrain the ferroptosis to alleviate pulmonary...
Tuberostemonine may enhance the function of the SLC7A11/glutamate antiporter to restrain the ferroptosis to alleviate pulmonary ... Tuberostemonine may enhance the function of the SLC7A11/glutamate antiporter to restrain t ... glutamate antiporter to restrain the ferroptosis. MATERIALS AND METHODS:. We validated the effects of tuberostemonine and ...
Changed and Deleted MeSH Headings-2018. NLM Technical Bulletin. 2017 Nov-Dec
Extracellular determinants of anion discrimination of the Cl-/H+ antiporter protein CLC-5. - Department of Physiology, Anatomy...
Here we show for the Cl-/H+ antiporter CLC-5 that the conserved and extracellularly exposed Lys210 residue is critical to ... H+ antiporters that carry out fundamental physiological tasks by transporting Cl- across plasma membrane and intracellular ... Here we show for the Cl-/H+ antiporter CLC-5 that the conserved and extracellularly exposed Lys210 residue is critical to ... Mammalian CLC proteins comprise both Cl- channels and Cl-/H+ antiporters that carry out fundamental physiological tasks by ...
Genetic testing of glycogen storage disease type Ib in Japan: five novel G6PT1 mutations and a rapid detection method for a...
NIH Guide: INNOVATIVE USE OF NON-MAMMALIAN MODEL ORGANISMS TO STUDY MEMBRANE TRANSPORT
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SLC9A6 gene: MedlinePlus Genetics
Sandwalk: An Intelligent Design Creationist disputes the evolution of citrate utilization in the LTEE ... Lenski responds
The antiporter is a kind of revolving door. It allows one molecule to be swapped for another. In this case, the citrate is ... But a mutation in the citrate-eaters allowed them to make an "antiporter" protein, CitT, that allows citrate to cross the ... deleted for the anaerobic citrate/succinate antiporter) and E. coli ΔdctA::kan (deleted for the aerobic succinate transporter ...
Department of Basic and Clinical Sciences | Albany College of Pharmacy and Health Sciences
Transmembrane protein - wikidoc
John Lippolis : USDA ARS
Antiporters [D12.776.543.550.190] * Chloride-Bicarbonate Antiporters [D12.776.543.550.190.276] * Potassium-Hydrogen Antiporters ... Antiporters [D12.776.543.585.450.162] * Chloride-Bicarbonate Antiporters [D12.776.543.585.450.162.193] * Mitochondrial ADP, ATP ... Antiporters [D12.776.157.530.450.162] * Chloride-Bicarbonate Antiporters [D12.776.157.530.450.162.193] * Potassium-Hydrogen ... 1994; ANTIPORTERS was indexed under CARRIER PROTEINS 1980-1993. History Note. 1994; use ANTIPORTERS (NM) 1980-1993. Date ...
- Tuberostemonine may enhance the function of the SLC7A11/glutamate antiporter to restrain the ferroptosis to alleviate pulmonary fibrosis. (bvsalud.org)
- AIM OF THE STUDY The aim of this study is to observe whether tuberostemonine alleviates pulmonary fibrosis by enhancing the function of the SLC7A11/ glutamate antiporter to restrain the ferroptosis . (bvsalud.org)
- xCT/SLC7A11 antiporter function inhibits HIV-1 infection. (acphs.edu)
- Molecular basis of substrate-induced permeation by an amino acid antiporter. (bsc.es)
- Here we show for the Cl-/H+ antiporter CLC-5 that the conserved and extracellularly exposed Lys210 residue is critical to determine the anion specificity for transport activity. (ox.ac.uk)
- The Cl-/H+ antiporter ClC-7 is the primary chloride permeation pathway in lysosomes. (nih.gov)
- Mammalian CLC proteins comprise both Cl- channels and Cl-/H+ antiporters that carry out fundamental physiological tasks by transporting Cl- across plasma membrane and intracellular compartments. (ox.ac.uk)
- Potassium-Hydrogen Antiporters" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
- 12. The glucose-6-phosphate transporter is a phosphate-linked antiporter deficient in glycogen storage disease type Ib and Ic. (nih.gov)
- 10. The SLC37 family of phosphate-linked sugar phosphate antiporters. (nih.gov)
- When amiloride was administered to block the sodium/hydrogen antiporter, 2-ME induced twice the incidence of cardiovascular malformations in fetuses than 2-ME alone. (cdc.gov)
- Motivated by the discovery that certain bacterial CLC proteins are secondary active Cl-/H+ antiporters, we hypothesized that mammalian CLC proteins might not be classical Cl- ion channels but might exhibit Cl(-)-coupled proton transport activity. (nih.gov)
- However, little is known about the Na+/H+ antiporter NhaC family of proteins in the extremely halophilic archaea. (bvsalud.org)
- Phylogenetic analysis shows that both NhaC1 and NhaC2 belong to the Na+/H+ antiporter NhaC family of proteins and are significantly distant from the identified NhaC proteins from Bacillus. (bvsalud.org)
- Mechanism of cation specificity of Na+/H+ antiporters. (nih.gov)
- Five analogs of the antiporter inhibitor amiloride reduced norepinephrine stimulation of cGMP accumulation with the same relative potency as they act on the antiporter. (nih.gov)
- Further analysis indicated that norepinephrine is probably acting via an alpha 1-adrenergic----[Ca2+]i----Ca2+/phospholipid- dependent protein kinase (protein kinase C) mechanism to activate the Na+/H+ antiporter, thereby causing cytoplasmic alkalization. (nih.gov)