Cystinyl Aminopeptidase: A zinc-containing sialoglycoprotein that is used to study aminopeptidase activity in the pathogenesis of hypertension. EC 3.4.11.3.Aminopeptidases: A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11.Leucyl Aminopeptidase: A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. This occurs in tissue cell cytosol, with high activity in the duodenum, liver, and kidney. The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide.Glutamyl Aminopeptidase: A ZINC-dependent membrane-bound aminopeptidase that catalyzes the N-terminal peptide cleavage of GLUTAMATE (and to a lesser extent ASPARTATE). The enzyme appears to play a role in the catabolic pathway of the RENIN-ANGIOTENSIN SYSTEM.Antigens, CD13: Zinc-binding metalloproteases that are members of the type II integral membrane metalloproteases. They are expressed by GRANULOCYTES; MONOCYTES; and their precursors as well as by various non-hematopoietic cells. They release an N-terminal amino acid from a peptide, amide or arylamide.Methionyl Aminopeptidases: Aminopeptidases that remove METHIONINE from the amino-terminus of a peptide chain, such as the initiator METHIONINE found on nascent peptide chains.Dipeptidyl-Peptidases and Tripeptidyl-Peptidases: A subclass of exopeptidases that includes enzymes which cleave either two or three AMINO ACIDS from the end of a peptide chain.Pyroglutamyl-Peptidase I: An enzyme that catalyzes the release of a N-terminal pyroglutamyl group from a polypeptide provided the next residue is not proline. It is inhibited by thiol-blocking reagents and occurs in mammalian tissues, microorganisms, and plants. (From Enzyme Nomenclature, 1992) EC 3.4.19.3.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Microvilli: Minute projections of cell membranes which greatly increase the surface area of the cell.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.Leucine: An essential branched-chain amino acid important for hemoglobin formation.Dipeptidyl Peptidase 4: A serine protease that catalyses the release of an N-terminal dipeptide. Several biologically-active peptides have been identified as dipeptidyl peptidase 4 substrates including INCRETINS; NEUROPEPTIDES; and CHEMOKINES. The protein is also found bound to ADENOSINE DEAMINASE on the T-CELL surface and is believed to play a role in T-cell activation.Protease Inhibitors: Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).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.Glucose Transporter Type 4: A glucose transport protein found in mature MUSCLE CELLS and ADIPOCYTES. It promotes transport of glucose from the BLOOD into target TISSUES. The inactive form of the protein is localized in CYTOPLASMIC VESICLES. In response to INSULIN, it is translocated to the PLASMA MEMBRANE where it facilitates glucose uptake.Encyclopedias as Topic: Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)Kallidin: A decapeptide bradykinin homolog cleaved from kininogen by kallikreins. It is a smooth-muscle stimulant and hypotensive agent that acts by vasodilatation.Quantitative Trait Loci: Genetic loci associated with a QUANTITATIVE TRAIT.Ribosomal Proteins: Proteins found in ribosomes. They are believed to have a catalytic function in reconstituting biologically active ribosomal subunits.Genetic Variation: Genotypic differences observed among individuals in a population.Polymorphism, Single Nucleotide: A single nucleotide variation in a genetic sequence that occurs at appreciable frequency in the population.Transcriptome: The pattern of GENE EXPRESSION at the level of genetic transcription in a specific organism or under specific circumstances in specific cells.Placenta: A highly vascularized mammalian fetal-maternal organ and major site of transport of oxygen, nutrients, and fetal waste products. It includes a fetal portion (CHORIONIC VILLI) derived from TROPHOBLASTS and a maternal portion (DECIDUA) derived from the uterine ENDOMETRIUM. The placenta produces an array of steroid, protein and peptide hormones (PLACENTAL HORMONES).Genotype: The genetic constitution of the individual, comprising the ALLELES present at each GENETIC LOCUS.Nootropic Agents: Drugs used to specifically facilitate learning or memory, particularly to prevent the cognitive deficits associated with dementias. These drugs act by a variety of mechanisms. While no potent nootropic drugs have yet been accepted for general use, several are being actively investigated.Angiotensin II: An octapeptide that is a potent but labile vasoconstrictor. It is produced from angiotensin I after the removal of two amino acids at the C-terminal by ANGIOTENSIN CONVERTING ENZYME. The amino acid in position 5 varies in different species. To block VASOCONSTRICTION and HYPERTENSION effect of angiotensin II, patients are often treated with ACE INHIBITORS or with ANGIOTENSIN II TYPE 1 RECEPTOR BLOCKERS.Internet: A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.Oxytocin: A nonapeptide hormone released from the neurohypophysis (PITUITARY GLAND, POSTERIOR). It differs from VASOPRESSIN by two amino acids at residues 3 and 8. Oxytocin acts on SMOOTH MUSCLE CELLS, such as causing UTERINE CONTRACTIONS and MILK EJECTION.Proteomics: The systematic study of the complete complement of proteins (PROTEOME) of organisms.Plasma: The residual portion of BLOOD that is left after removal of BLOOD CELLS by CENTRIFUGATION without prior BLOOD COAGULATION.Chromatography, Liquid: Chromatographic techniques in which the mobile phase is a liquid.Serum: The clear portion of BLOOD that is left after BLOOD COAGULATION to remove BLOOD CELLS and clotting proteins.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Gas Chromatography-Mass Spectrometry: A microanalytical technique combining mass spectrometry and gas chromatography for the qualitative as well as quantitative determinations of compounds.Vasotocin: A nonapeptide that contains the ring of OXYTOCIN and the side chain of ARG-VASOPRESSIN with the latter determining the specific recognition of hormone receptors. Vasotocin is the non-mammalian vasopressin-like hormone or antidiuretic hormone regulating water and salt metabolism.Oryzias: The only genus in the family Oryziinae, order BELONIFORMES. Oryzias are egg-layers; other fish of the same order are livebearers. Oryzias are used extensively in testing carcinogens.Preoptic Area: Region of hypothalamus between the ANTERIOR COMMISSURE and OPTIC CHIASM.Body Temperature Regulation: The processes of heating and cooling that an organism uses to control its temperature.Pituitary Hormones, Posterior: Hormones released from the neurohypophysis (PITUITARY GLAND, POSTERIOR). They include a number of peptides which are formed in the NEURONS in the HYPOTHALAMUS, bound to NEUROPHYSINS, and stored in the nerve terminals in the posterior pituitary. Upon stimulation, these peptides are released into the hypophysial portal vessel blood.Receptors, Vasopressin: Specific molecular sites or proteins on or in cells to which VASOPRESSINS bind or interact in order to modify the function of the cells. Two types of vasopressin receptor exist, the V1 receptor in the vascular smooth muscle and the V2 receptor in the kidneys. The V1 receptor can be subdivided into V1a and V1b (formerly V3) receptors.Monosaccharide Transport Proteins: A large group of membrane transport proteins that shuttle MONOSACCHARIDES across CELL MEMBRANES.Glucose Transporter Type 1: A ubiquitously expressed glucose transporter that is important for constitutive, basal GLUCOSE transport. It is predominately expressed in ENDOTHELIAL CELLS and ERYTHROCYTES at the BLOOD-BRAIN BARRIER and is responsible for GLUCOSE entry into the BRAIN.Hydrophobic and Hydrophilic Interactions: The thermodynamic interaction between a substance and WATER.Acetonitriles: Compounds in which a methyl group is attached to the cyano moiety.Glycosylation: The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.Glycomics: The systematic study of the structure and function of the complete set of glycans (the glycome) produced in a single organism and identification of all the genes that encode glycoproteins.Tandem Mass Spectrometry: A mass spectrometry technique using two (MS/MS) or more mass analyzers. With two in tandem, the precursor ions are mass-selected by a first mass analyzer, and focused into a collision region where they are then fragmented into product ions which are then characterized by a second mass analyzer. A variety of techniques are used to separate the compounds, ionize them, and introduce them to the first mass analyzer. For example, for in GC-MS/MS, GAS CHROMATOGRAPHY-MASS SPECTROMETRY is involved in separating relatively small compounds by GAS CHROMATOGRAPHY prior to injecting them into an ionization chamber for the mass selection.Spectrometry, Mass, Electrospray Ionization: A mass spectrometry technique used for analysis of nonvolatile compounds such as proteins and macromolecules. The technique involves preparing electrically charged droplets from analyte molecules dissolved in solvent. The electrically charged droplets enter a vacuum chamber where the solvent is evaporated. Evaporation of solvent reduces the droplet size, thereby increasing the coulombic repulsion within the droplet. As the charged droplets get smaller, the excess charge within them causes them to disintegrate and release analyte molecules. The volatilized analyte molecules are then analyzed by mass spectrometry.Drug Packaging: Containers, packaging, and packaging materials for drugs and BIOLOGICAL PRODUCTS. These include those in ampule, capsule, tablet, solution or other forms. Packaging includes immediate-containers, secondary-containers, and cartons. In the United States, such packaging is controlled under the Federal Food, Drug, and Cosmetic Act which also stipulates requirements for tamper-resistance and child-resistance. Similar laws govern use elsewhere. (From Code of Federal Regulations, 21 CFR 1 Section 210, 1993) DRUG LABELING is also available.Pharmacopoeias as Topic: Authoritative treatises on drugs and preparations, their description, formulation, analytic composition, physical constants, main chemical properties used in identification, standards for strength, purity, and dosage, chemical tests for determining identity and purity, etc. They are usually published under governmental jurisdiction (e.g., USP, the United States Pharmacopoeia; BP, British Pharmacopoeia; P. Helv., the Swiss Pharmacopoeia). They differ from FORMULARIES in that they are far more complete: formularies tend to be mere listings of formulas and prescriptions.Drug Overdose: Accidental or deliberate use of a medication or street drug in excess of normal dosage.Acetaminophen: Analgesic antipyretic derivative of acetanilide. It has weak anti-inflammatory properties and is used as a common analgesic, but may cause liver, blood cell, and kidney damage.Large Neutral Amino Acid-Transporter 1: A CD98 antigen light chain that when heterodimerized with CD98 antigen heavy chain (ANTIGENS, CD98 HEAVY CHAIN) forms a protein that mediates sodium-independent L-type amino acid transport.Congresses as Topic: Conferences, conventions or formal meetings usually attended by delegates representing a special field of interest.

Endothelin stimulates glucose uptake and GLUT4 translocation via activation of endothelin ETA receptor in 3T3-L1 adipocytes. (1/94)

Endothelin-1 (ET-1) is a 21-amino acid peptide that binds to G-protein-coupled receptors to evoke biological responses. This report studies the effect of ET-1 on regulating glucose transport in 3T3-L1 adipocytes. ET-1, but not angiotensin II, stimulated glucose uptake in a dose-dependent manner with an EC50 value of 0.29 nM and a 2.47-fold stimulation at 100 nM. ET-1 stimulated glucose uptake in differentiated 3T3-L1 cells but had no effect in undifferentiated cells, although ET-1 stimulated phosphatidylinositol hydrolysis to a similar degree in both. The 3T3-L1 cells expressed approximately 560,000 sites/cell of ETA receptor, which was not altered during differentiation. Western blot analysis and immunofluorescence staining show that ET-1 stimulated the translocation of insulin-responsive aminopeptidase and GLUT4 to the plasma membrane. The effect of ET-1 on glucose uptake was blocked by A-216546, an antagonist selective for the ETA receptor. ET-1 treatment did not induce phosphorylation of insulin receptor beta-subunit, insulin receptor substrate-1, or Akt but stimulated the tyrosyl phosphorylation of a 75-kDa protein. Genistein (100 microM), an inhibitor of tyrosine kinases, inhibited ET-1-stimulated glucose uptake. Our results show that ET-1 stimulates GLUT4 translocation and glucose uptake in 3T3-L1 adipocytes via activation of ETA receptor.  (+info)

Molecular cloning of adipocyte-derived leucine aminopeptidase highly related to placental leucine aminopeptidase/oxytocinase. (2/94)

In the current study, we report the cloning and initial characterization of a novel human cytosolic aminopeptidase named adipocyte-derived leucine aminopeptidase (A-LAP). The sequence encodes a 941-amino acid protein with significant homology (43%) to placental leucine aminopeptidase (P-LAP)/oxytocinase. The predicted A-LAP contains the HEXXH(X)18E consensus sequence, which is characteristic of the M1 family of zinc-metallopeptidases. Although the deduced sequence contains a hydrophobic region near the N-terminus, the enzyme localized mainly in cytoplasm when expressed in COS-7 cells. Northern blot analysis revealed that A-LAP was expressed in all the tissues tested, some of which expressed at least three forms of mRNA, suggesting that the regulation of the gene expression is complex. When aminopeptidase activity of A-LAP was measured with various synthetic substrates, the enzyme revealed a preference for leucine, establishing that A-LAP is a novel leucine aminopeptidase with restricted substrate specificity. The identification of A-LAP, which reveals strong homology to P-LAP, might lead to the definition of a new subfamily of zinc-containing aminopeptidases belonging to the M1 family of metallopeptidases.  (+info)

Identification of wortmannin-sensitive targets in 3T3-L1 adipocytes. DissociationoOf insulin-stimulated glucose uptake and glut4 translocation. (3/94)

The current studies investigated the contribution of phosphatidylinositol 3-kinase (PI3-kinase) isoforms to insulin-stimulated glucose uptake and glucose transporter 4 (GLUT4) translocation. Experiments involving the microinjection of antibodies specific for the p110 catalytic subunit of class I PI3-kinases demonstrated an absolute requirement for this form of the enzyme in GLUT4 translocation. This finding was confirmed by the demonstration that the PI3-kinase antagonist wortmannin inhibits GLUT4 and insulin-responsive aminopeptidase translocation with a dose response identical to that required to inhibit another class I PI3-kinase-dependent event, activation of pp70 S6-kinase. Interestingly, wortmannin inhibited insulin-stimulated glucose uptake at much lower doses, suggesting the existence of a second, higher affinity target of the drug. Subsequent removal of wortmannin from the media shifted this dose-response curve to one resembling that for GLUT4 translocation and pp70 S6-kinase. This is consistent with the lower affinity target being p110, which is irreversibly inhibited by wortmannin. Wortmannin did not reduce glucose uptake in cells stably expressing Myr-Akt, which constitutively induced GLUT4 translocation to the plasma membrane; this demonstrates that wortmannin does not inhibit the transporters directly. In addition to elucidating a second wortmannin-sensitive pathway in 3T3-L1 adipocytes, these studies suggest that the presence of GLUT4 on the plasma membrane is not sufficient for activation of glucose uptake.  (+info)

Insulin regulation of protein traffic in rat adipose cells. (4/94)

Rat adipocytes were biotinylated with cell-impermeable reagents, sulfo-N-hydroxysuccinimide-biotin and sulfo-N-hydroxysuccinimide-S-S-biotin in the absence and presence of insulin. Biotinylated and nonbiotinylated populations of the insulin-like growth factor-II/mannose 6-phosphate receptor, the transferrin receptor, and insulin-responsive aminopeptidase were separated by adsorption to streptavidin-agarose to determine the percentage of the biotinylated protein molecules versus their total amount in different subcellular compartments. Results indicate that adipose cells possess at least two distinct cell surface recycling pathways for insulin-like growth factor-II/mannose 6-phosphate receptor (MPR) and transferrin receptor (TfR): one which is mediated by glucose transporter isoform 4(Glut4)-vesicles and another that bypasses this compartment. Under basal conditions, the first pathway is not active, and cell surface recycling of TfR and, to a lesser extent, MPR proceeds via the second pathway. Insulin dramatically stimulates recycling through the first pathway and has little effect on the second. Within the Glut4-containing compartment, insulin has profoundly different effects on intracellular trafficking of insulin-responsive aminopeptidase on one hand and MPR and TfR on the other. After insulin administration, insulin-responsive aminopeptidase is redistributed from Glut4-containing vesicles to the plasma membrane and stays there for at least 30 min with minimal detectable internalization and recycling, whereas MPR and TfR rapidly shuttle between Glut4 vesicles and the plasma membrane in such a way that after 30 min of insulin treatment, virtually every receptor molecule in this compartment completes at least one trafficking cycle to the cell surface. Thus, different recycling proteins, which compose Glut4-containing vesicles, are internalized into this compartment at their own distinctive rates.  (+info)

GLUT-4myc ectopic expression in L6 myoblasts generates a GLUT-4-specific pool conferring insulin sensitivity. (5/94)

Insulin stimulates glucose uptake into muscle and fat cells via recruitment of the glucose transporter 4 (GLUT-4) from intracellular store(s) to the cell surface. Robust stimulation of glucose uptake by insulin coincides with the expression of GLUT-4 during differentiation of muscle and fat cells, but it is not known if GLUT-4 expression suffices to confer insulin sensitivity to glucose uptake. We have therefore examined the effect of expression of a myc epitope-tagged GLUT-4 (GLUT-4myc) into L6 myoblasts, which do not express endogenous GLUT-4 until differentiated into myotubes. Ectopic expression of GLUT-4myc markedly improved insulin sensitivity of glucose uptake in L6 myoblasts. The GLUT-4myc protein distributed equally to the cell surface and intracellular compartments in myoblasts, and the intracellular fraction of GLUT-4myc further increased in myotubes. In myoblasts, the intracellular GLUT-4myc compartment contained the majority of the insulin-regulatable amino peptidase (IRAP) but less than half of the GLUT-1, suggesting segregation of GLUT-4myc and IRAP to a specific cellular locus. Insulin stimulation of phosphatidylinositol 3-kinase and protein kinase B-alpha activities was similar for L6-GLUT-4myc myoblasts and myotubes. At both stages, GLUT-4myc responded to insulin by translocating to the cell surface. These results suggest that GLUT-4myc segregates into a specific compartment in L6 myoblasts and confers insulin sensitivity to these cells. L6-GLUT-4myc myoblasts, which are easily transfectable with various constructs, are a useful resource to study insulin action.  (+info)

Munc18c function is required for insulin-stimulated plasma membrane fusion of GLUT4 and insulin-responsive amino peptidase storage vesicles. (6/94)

To examine the functional role of the interaction between Munc18c and syntaxin 4 in the regulation of GLUT4 translocation in 3T3L1 adipocytes, we assessed the effects of introducing three different peptide fragments (20 to 24 amino acids) of Munc18c from evolutionarily conserved regions of the Sec1 protein family predicted to be solvent exposed. One peptide, termed 18c/pep3, inhibited the binding of full-length Munc18c to syntaxin 4, whereas expression of the other two peptides had no effect. In parallel, microinjection of 18c/pep3 but not a control peptide inhibited the insulin-stimulated translocation of endogenous GLUT4 and insulin-responsive amino peptidase (IRAP) to the plasma membrane. In addition, expression of 18c/pep3 prevented the insulin-stimulated fusion of endogenous and enhanced green fluorescent protein epitope-tagged GLUT4- and IRAP-containing vesicles into the plasma membrane, as assessed by intact cell immunofluorescence. However, unlike the pattern of inhibition seen with full-length Munc18c expression, cells expressing 18c/pep3 displayed discrete clusters of GLUT4 abd IRAP storage vesicles at the cell surface which were not contiguous with the plasma membrane. Together, these data suggest that the interaction between Munc18c and syntaxin 4 is required for the integration of GLUT4 and IRAP storage vesicles into the plasma membrane but is not necessary for the insulin-stimulated trafficking to and association with the cell surface.  (+info)

Characterization of a recombinant soluble form of human placental leucine aminopeptidase/oxytocinase expressed in Chinese hamster ovary cells. (7/94)

Serum levels of human placental leucine aminopeptidase/oxytocinase (P-LAP) increase with gestation. cDNA cloning of P-LAP revealed that the enzyme is a type II membrane-bound protein containing the consensus HEXXH(X)18E motif found in the M1 family of zinc-metallopeptidase proteins. In this study, a recombinant soluble form of P-LAP found in maternal serum was expressed in Chinese hamster ovary cells, purified to homogeneity and then characterized. Although N-terminal sequencing revealed a four-amino-acid deletion, the purified enzyme was active and was shown to be a zinc-containing homodimeric protein with molecular mass of 280 kDa in solution. Using artificial substrates, it was shown that the enzyme has broad specificity and is inhibited by several compounds known as aminopeptidase inhibitors. Subsequently, sequential N-terminal amino-acid liberation of several peptide hormones by the enzyme was monitored and structures of the products were determined. Among the hormones having a cysteine residue at their N-terminal end and intramolecular disulfide bonds, it was found that vasopressin and oxytocin, but not calcitonin and endothelins, were cleaved by the enzyme. Because the molecular properties of oxytocinase so far reported often conflict, our results provide an initial biochemical and enzymatic characterization of moleculary defined P-LAP/oxytocinase.  (+info)

Insulin-responsive aminopeptidase trafficking in 3T3-L1 adipocytes. (8/94)

The insulin-responsive aminopeptidase (IRAP/VP165/gp160) was identified originally in GLUT4-containing vesicles and shown to translocate in response to insulin, much like the glucose transporter 4 (GLUT4). This study characterizes the trafficking and kinetics of IRAP in exocytosis, endocytosis, and recycling to the membrane in 3T3-L1 adipocytes. After exposure of 3T3-L1 adipocytes to insulin, IRAP translocated to the plasma membrane as assessed by either cell fractionation, surface biotinylation, or the plasma membrane sheet assay. The rate of exocytosis closely paralleled that of GLUT4. In the continuous presence of insulin, IRAP was endocytosed with a half-time of about 3-5 min. IRAP endocytosis is inhibited by cytosol acidification, a property of clathrin-mediated endocytosis, but not by the expression of a constitutively active Akt/PKB. Arrival in an LDM fraction derived via subcellular fractionation exhibited a slower time course than disappearance from the cell surface, suggesting additional endocytic intermediates. As assayed by membrane "sheets," GLUT4 and IRAP showed similar internalization rates that are wortmannin-insensitive and occur with a half-time of roughly 5 min. IRAP remaining on the cell surface 10 min following insulin removal was both biotin- and avidin-accessible, implying the absence of thin-necked invaginations. Finally, endocytosed IRAP quickly recycled back to the plasma membrane in a wortmannin-sensitive process. These results demonstrate rapid endocytosis and recycling of IRAP in the presence of insulin and trafficking that matches GLUT4 in rate.  (+info)

Leucyl/cystinyl aminopeptidase, also known as cystinyl aminopeptidase (CAP), insulin-regulated aminopeptidase (IRAP), human placental leucine aminopeptidase (PLAP), oxytocinase, and vasopressinase, is an enzyme of the aminopeptidase group that in humans is encoded by the LNPEP gene. This gene encodes a zinc-dependent aminopeptidase (metalloexopeptidase) that cleaves vasopressin, oxytocin, lys-bradykinin, met-enkephalin, dynorphin A and other peptide hormones. The protein can be secreted in maternal serum, reside in intracellular vesicles with the insulin-responsive glucose transporter GLUT4, or form a type II integral membrane glycoprotein. The protein catalyzes the final step in the conversion of angiotensinogen to angiotensin IV (AT4) and is also a receptor for AT4. Alternative splicing results in multiple transcript variants encoding different isoforms. Mutations in this gene have been associated to psoriasis risk.(doi:10.1038/jid.2013.317) Cystinyl aminopeptidase has been shown to interact ...
The hexapeptide angiotensin IV (Ang IV) is a metabolite of angiotensin II (Ang II) and plays a central role in the brain. It was reported more than two decades ago that intracerebroventricular injection of Ang IV improved memory and learning in the rat. Several hypotheses have been put forward to explain the positive effects of Ang IV and related analogues on cognition. It has been proposed that the insulin-regulated aminopeptidase (IRAP) is the main target of Ang IV. This paper discusses progress in the discovery of inhibitors of IRAP as potential enhancers of cognitive functions. Very potent inhibitors of the protease have been synthesised, but pharmacokinetic issues (including problems associated with crossing the blood-brain barrier) remain to be solved. The paper also briefly presents an overview of the status in the discovery of inhibitors of ACE and renin, and of AT1R antagonists and AT2R agonists, in order to enable other discovery processes within the RAS system to be compared. The paper
Angiotensin IV (Ang IV) and related peptide analogues, as well as non-peptide inhibitors of insulin-regulated aminopeptidase (IRAP), have previously been shown to enhance memory and cognition in animal models. Furthermore, the endogenous IRAP substrates oxytocin and vasopressin are known to facilitate learning and memory. In this study, the two recently synthesized 13-membered macrocylic competitive IRAP inhibitors HA08 and HA09, which were designed to mimic the N-terminal of oxytocin and vasopressin, were assessed and compared based on their ability to bind to the IRAP active site, and alter dendritic spine density in rat hippocampal primary cultures. The binding modes of the IRAP inhibitors HA08, HA09 and of Ang IV in either the extended or γ-turn conformation at the C-terminal to human IRAP were predicted by docking and molecular dynamics (MD) simulations. The binding free energies calculated with the linear interaction energy (LIE) method, which are in excellent agreement with experimental ...
Crystallization trials were performed by sitting drop vapor diffusion in 96-well plates (Greiner Bio-One, Stonehouse, U.K.), using a Cartesian Technologies Microsys MIC4000 liquid-handling robot, incubated at 21°C and periodically inspected using a TAP Biosystems storage vault (TAP, Royston, U.K.).. Purified IRAP at a concentration of 10 mg/ml in 150 mM NaCl and 10 mM HEPES buffer (pH 7.4) was screened for crystallization against various commercially available screens. The protein stock and reservoir solution was mixed at a 1:1 ratio to form a drop of volume 200 nL. Usable crystals were obtained at several conditions of the Morpheus Screen (Molecular Dimensions) (32). In all cases, data were collected at the I03 beamline at the Diamond Light Source UK, equipped with a Pilatus3 6M pixel detector, at a wavelength of 0.976 Å. Data were merged and scaled using the xia2 package (33).. The best dataset collected from an unsoaked IRAP crystal was from the following Morpheus screen condition: 10% ...
Landau R, Laverrière A, Bischof P, Irion O, Morales M, Cohen M. Alteration of circulating Placental Leucine Aminopeptidase (P-LAP) activity in preeclampsia. Neuro Endocrinol Lett. 2010 Jan; 31(1): 63-66 ...
TY - JOUR. T1 - Vimentin binds IRAP and is involved in GLUT4 vesicle trafficking. AU - Hirata, Yohko. AU - Hosaka, Toshio. AU - Iwata, Takeo. AU - Le, Chung T K. AU - Jambaldorj, Bayasgalan. AU - Teshigawara, Kiyoshi. AU - Harada, Nagakatsu. AU - Sakaue, Hiroshi. AU - Sakai, Tohru. AU - Yoshimoto, Katsuhiko. AU - Nakaya, Yutaka. PY - 2011/2/4. Y1 - 2011/2/4. N2 - Insulin-responsive aminopeptidase (IRAP) and GLUT4 are two major cargo proteins of GLUT4 storage vesicles (GSVs) that are translocated from a postendosomal storage compartment to the plasma membrane (PM) in response to insulin. The cytoplasmic region of IRAP is reportedly involved in retention of GSVs. In this study, vimentin was identified using the cytoplasmic domain of IRAP as bait. The validity of this interaction was confirmed by pull-down assays and immunoprecipitation in 3T3-L1 adipocytes. In addition, it was shown that GLUT4 translocation to the PM by insulin was decreased in vimentin-depleted adipocytes, presumably due to ...
The LAP disk is a rapid test for the detection of enzyme lucine amino peptidase.. Leucine-beta-naphthylamide impregnated disk serve as a substrate for the detection of lucine aminopeptidase. Following hydrolysis of the substrate by enzyme, the resulting beta- naphthylamineprodeces a red color upon the addition of cinnamaldehyde reagent ...
Epidemiological studies suggested that cinnamon consist a significant anti insulin resistance(1091)(1092)(1094) and anti metabolic syndrome(1093)(1094)(1095)(1096)(1097) properties, such as lowering total cholesterol(1093), low-density lipoprotein cholesterol(1093) and improving high-density lipoprotein cholesterol(1093), may be due to its antihyperglycaemic (1091)(1093) and potential to reduce postprandial blood glucose levels(1091)(1092), liver fat(1098) and and improved glucose homeostasis(1098) properties, by regulating the mechanisms of-medicated glucose and lipid metabolism(1099), such as decreased the mRNA expression of inflammatory cytokine(TNF-alpha) in adipose tissue(1100) and upregulated mRNA expression of insulin-regulated membrane trafficking(1100) and whole body glucose homeostasi(GLUT-4) in skeletal muscle(1100 ...
Epidemiological studies suggested that cinnamon consist a significant anti insulin resistance(1091)(1092)(1094) and anti metabolic syndrome(1093)(1094)(1095)(1096)(1097) properties, such as lowering total cholesterol(1093), low-density lipoprotein cholesterol(1093) and improving high-density lipoprotein cholesterol(1093), may be due to its antihyperglycaemic (1091)(1093) and potential to reduce postprandial blood glucose levels(1091)(1092), liver fat(1098) and and improved glucose homeostasis(1098) properties, by regulating the mechanisms of-medicated glucose and lipid metabolism(1099), such as decreased the mRNA expression of inflammatory cytokine(TNF-alpha) in adipose tissue(1100) and upregulated mRNA expression of insulin-regulated membrane trafficking(1100) and whole body glucose homeostasi(GLUT-4) in skeletal muscle(1100 ...
Definition of leucine aminopeptidase in the Legal Dictionary - by Free online English dictionary and encyclopedia. What is leucine aminopeptidase? Meaning of leucine aminopeptidase as a legal term. What does leucine aminopeptidase mean in law?
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator, also known as endoplasmic reticulum aminopeptidase 1 (ARTS-1), is a protein which in humans is encoded by the ARTS-1 gene. Endoplasmic reticulum amino peptidase 1 is active in the endoplasmic reticulum, which is involved in protein processing and transport. This protein is an aminopeptidase, which is an enzyme that cleaves other proteins into smaller fragments called peptides. ARTS1 is also known as: ER aminopeptidase 1 (ERAP1) the name accepted by the Hugo Gene Nomenclature Committee ER aminopeptidase associated with antigen processing (ERAAP) Adipocyte-derived leucine aminopeptidase (ALAP) Puromycin-insensitive leucine aminopeptidase (PILS-AP) ERAP1 has two major functions in the immune system: First, ERAP1 cleaves several proteins called cytokine receptors on the surface of cells. Cleaving these receptors reduces their ability to transmit chemical signals into the cell, which affects the process of inflammation. Second, ...
The property of solutions of Triton X-114 to separate into detergent-rich and detergent-poor phases at 30 degrees C has been exploited to investigate the identities of the aminopeptidases in synaptic membrane preparations from pig striatum. When titrated with an antiserum to aminopeptidase N (EC 3.4.11.2), synaptic membranes solubilized with Triton X-100 revealed that this enzyme apparently comprises no more than 5% of the activity releasing tyrosine from [Leu]enkephalin. When assayed in the presence of puromycin, this proportion increased to 20%. Three integral membrane proteins were fractionated by phase separation in Triton X-114. Aminopeptidase activity, endopeptidase-24.11 and peptidyl dipeptidase A partitioned predominantly into the detergent-rich phase when kidney microvillar membranes were so treated. However, only 5.5% of synaptic membrane aminopeptidase activity partitioned into this phase, although the other peptidases behaved predictably. About half of the aminopeptidase activity in ...
Insulin stimulates blood sugar uptake by regulating translocation of the GLUT4 glucose transporter from intracellular compartments to the plasma membrane. mechanism. Consistent with a role impartial of AS160 we showed that IRAP functions in GLUT4 sorting from endosomes to GLUT4-specialized compartments. This is revealed by the relocalization of GLUT4 to endosomes in IRAP knockdown cells. Although IRAP knockdown has profound effects on GLUT4 traffic GLUT4 knockdown does not affect IRAP trafficking demonstrating that IRAP traffics impartial of GLUT4. In sum we show that IRAP is usually both cargo and a key regulator of the insulin-regulated pathway. INTRODUCTION Insulin stimulates glucose uptake into adipose and muscle cells by inducing translocation of glucose transporter 4 (GLUT4) glucose transporters from intracellular compartments to the plasma membrane (PM; Huang and Czech 2007 ; Antonescu for 7 min. GLUT4-made up of compartments were isolated by incubation with GFP beads according to ...
FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes a zinc-dependent aminopeptidase that cleaves vasopressin, oxytocin, lys-bradykinin, met-enkephalin, dynorphin A and other peptide hormones. The protein can be secreted in maternal serum, reside in intracellular vesicles with the insulin-responsive glucose transporter GLUT4, or form a type II integral membrane glycoprotein. The protein catalyzes the final step in the conversion of angiotensinogen to angiotensin IV (AT4) and is also a receptor for AT4. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008 ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Enzymes activities of the Na+K+-and the HCO3−-ATPases, alkaline phosphatase, amino peptidase and 5′ nucleotidase have been measured in 4 different preparations from the cat pancreas a) in the ducts...
IRAP (Interleukin-1 Receptor Antagonist Protein) is an anti-inflammation therapy that is best for patients suffering from Osteoarthritis.
To detect viral infections and tumors, CD8+ T lymphocytes monitor cells for the presence of antigenic peptides bound to MHC class I molecules. The majority of MHC class I-presented peptides are generated from the cleavage of cellular and viral proteins by the ubiquitin-proteasome pathway. Many of the oligopeptides produced by this process are too long to stably bind to MHC class I molecules and require further trimming for presentation. Leucine aminopeptidase (LAP) is an IFN-inducible cytosolic aminopeptidase that can trim precursor peptides to mature epitopes and has been thought to play an important role in Ag presentation. To examine the role of LAP in generating MHC class I peptides in vivo, we generated LAP-deficient mice and LAP-deficient cell lines. These mutant mice and cells are viable and grow normally. The trimming of peptides in LAP-deficient cells is not reduced under basal conditions or after stimulation with IFN. Similarly, there is no reduction in presentation of peptides from precursor
Previous studies of the physiological functions of Ang IV in the brain have required the direct injection of this peptide in the brain ventricles.12,14,31 In addition to being invasive, this strategy precludes the evaluation of long-term effects of this peptide. To explore the role of chronic elevations of Ang IV in brain, we used a fusion protein capable of targeting the direct release of an Ang IV peptide in the brain. The major finding of the present study is that moderate overproduction of Ang IV peptide in the brain of transgenic mice induced hypertension that could be reversed by an AT1 receptor antagonist. We have ruled out several of the more trivial explanations for this finding: First, the m-Ang IV peptides could display an increased affinity for the AT1 receptor or be produced in such large quantities that they are able to bind and activate the AT1 receptor. This is clearly not the case, however, because the m-Ang IV peptides show no capacity to displace Ang II from the AT1B receptor ...
This report presents the results of the 2016-17 evaluation of the Industrial Research Assistance Program (IRAP). It was conducted based on the five-year evaluation cycle mandated by the Financial Administration Act and in accordance with NRCs Evaluation Plan. It examined the relevance and performance of IRAP between fiscal years 2012-13 and 2016-17.
The IUPHAR/BPS Guide to Pharmacology. Leucyl-cysteinyl aminopeptidase - M1: Aminopeptidase N. Detailed annotation on the structure, function, physiology, pharmacology and clinical relevance of drug targets.
Suchen & vergleichen Sie unsere Aspartyl Aminopeptidase Proteine von vielen Spezies. Finden Sie das richtige Produkt auf antikoerper-online.de.
GLUT4 is an insulin-regulated glucose transporter that is responsible for insulin-regulated glucose uptake into fat and muscle cells. In the absence of insulin, GLUT4 is mainly found in intracellular vesicles referred to as GLUT4 storage vesicles (GSVs). Here, we summarise evidence for the existence of these specific vesicles, how they are sequestered inside the cell and how they undergo exocytosis in the presence of insulin. In response to insulin stimulation, GSVs fuse with the plasma membrane in a rapid burst and in the continued presence of insulin GLUT4 molecules are internalised and recycled back to the plasma membrane in vesicles that are distinct from GSVs and probably of endosomal origin. In this Commentary we discuss evidence that this delivery process is tightly regulated and involves numerous molecules. Key components include the actin cytoskeleton, myosin motors, several Rab GTPases, the exocyst, SNARE proteins and SNARE regulators. Each step in this process is carefully orchestrated in a
The present invention relates to isolated polypeptides having aminopeptidase activity and isolated nucleic acid sequences encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the nucleic acid sequences as well as methods for producing and using the polypeptides.
Compare arginyl aminopeptidase (aminopeptidase B)-like 1 ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews, and more.
Malarial aminopeptidase molecule. Computer model showing the structure of the M18 aspartyl aminopeptidase with a dodecameric assembly arranged via dimer and trimer units forming a tetrahedron shape. From Plasmodium falciparum. - Stock Image C035/8499
This chapter describes the approaches used to identify Gram-negative rods, with emphasis on the greater difficulty in identifying non-glucose-fermenting organisms. We amplify what was presented in the 9th edition of this Manual by presenting a scheme to identify these organisms that is centered around three enzymatic activities, i.e., oxidase, trypsin (benzyl-arginine arylamidase or benzyl-arginine aminopeptidase), and pyrrolidonyl aminopeptidase. These enzymatic reactions are fast and easy to interpret, and they are stable markers in almost all taxa discussed; i.e., there are few species for which these tests yield variable intraspecies results.
The Nutshell Putative Gay Genes Identified, Questioned A genomic interrogation of homosexuality turns up speculative links between genetic elements and sexual orientation, but researchers say the study is too small to be significant. ...
Angiotensin IV (Ang IV), as an effector peptide of the rennin-angiotensin system, possesses many biological properties yet not completely known. In this study, we aimed to investigate the role of Ang IV in the development of Ang II-induced abdominal aortic aneurysm (AAA) in apolipoprotein E-knockout mice. We used Ang II infusion to induce AAA, and animals were treated with Ang II (1.44 mg/kg per day) plus no treatment, Ang II (1.44 mg/kg per day) plus low-, medium-, and high-dose Ang IV (0.72, 1.44, and 2.88 mg/kg per day, respectively). The incidence of AAA was 87.5%, 66.7%, 37.5%, and 83.3% in the no treatment, the low-, medium-, or high-dose Ang IV group, respectively. Compared with the no treatment group, medium-dose Ang IV treatment markedly reduced macrophage infiltration; levels of proinflammatory cytokines, including monocyte chemoattractant protein 1, interleukin 6, and intercellular adhesion molecule 1; the expression and activity of metalloproteinases 2 and 9; but increased smooth ...
Looking for online definition of aminopeptidase microsomal in the Medical Dictionary? aminopeptidase microsomal explanation free. What is aminopeptidase microsomal? Meaning of aminopeptidase microsomal medical term. What does aminopeptidase microsomal mean?
PRP (Platelet Rich Plasma) is used to treat tendons, ligaments and wounds. Platelets are rich in growth factors that help repair tissue and ligaments more quickly. Blood is drawn from the horse and spun in a centrifuge where PRP is cultivated and harvested. The platelet rich serum is then used to treat the injury or wound. The PRP increases the effectiveness and efficiency of the growth factors speeding up the healing process.. IRAP is an effective intra-articular treatment for joint disease. The IRAP system has been designed to stimulate the horses own white blood cells to produce anti-inflammatory mediators and enzymes that can reduce the inflammation present as a result of degenerative joint disease. IRAP works by amplifying the production of anti-inflammatory and regenerative proteins already found in the patients own blood. The large amount of "good" proteins are then extracted and injected into the affected joint of the horse to assist in the repair and recovery of the joint.. Equine ...
Aminopeptidase definition, any of several intestinal hydrolytic enzymes that remove an amino acid from the end of a peptide chain having a free amino group. See more.
Reaktivität: Rind (Kuh), Hund, Human and more. 39 verschiedene XPNPEP1 Antikörper vergleichen. Alle direkt auf antikörper-online bestellbar!
Recombinant protein of human X-prolyl aminopeptidase (aminopeptidase P) 1, soluble (XPNPEP1), 20 ug available for purchase from OriGene - Your Gene Company.
In this study, we determined serum aminopeptidase N/CD13 concentrations in patients with NSCLC using an aminopeptidase N/CD13-specific mAb (MH8-11), which inhibits cell motility and angiogenesis in vitro (10). Serum aminopeptidase N/CD13 concentrations were significantly elevated in patients with advanced-stage NSCLC. When the serum aminopeptidase N/CD13 values corresponding to the best diagnostic accuracy to separate the healthy controls and the patients with NSCLC were used as the cutoff value, the sensitivity of aminopeptidase N/CD13 was poorer than that of serum carcinoembryonic antigen; this suggests that serum aminopeptidase N/CD13 is not valuable as a diagnostic marker. However, a high serum aminopeptidase N/CD13 was significantly associated with established adverse prognostic factors in NSCLC, such as advanced stage, poor performance status, and poor response to chemotherapy. Serum aminopeptidase N/CD13 levels were also associated with overall survival in univariate analyses and had an ...
Aminopeptidase N (Myeloid Plasma Membrane Glycoprotein CD13 or Alanyl Aminopeptidase or Aminopeptidase M or Microsomal Aminopeptidase or gp150 or CD13 or ANPEP or EC 3.4.11.2) - Market research report and industry analysis - 11296626
Thank you for sharing this Journal of Pharmacology and Experimental Therapeutics article.. NOTE: We request your email address only to inform the recipient that it was you who recommended this article, and that it is not junk mail. We do not retain these email addresses.. ...
The protein encoded by this gene is an aminopeptidase which prefers acidic amino acids, and specifically favors aspartic acid over glutamic acid. It is thought to be a cytosolic protein involved in general metabolism of intracellular proteins. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2016 ...
The worlds first wiki where authorship really matters. Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts.
1W7V: Structural and Functional Implications of Metal Ion Selection in Aminopeptidase P, a Metalloprotease with a Dinuclear Metal Center.
In skeletal muscle, acute insulin treatment results in the recruitment of the GLUT4 glucose transporter from intracellular vesicular structures to the plasma membrane. The precise nature of these intracellular GLUT4 stores has, however, remained poorly defined. Using an established skeletal-muscle fractionation procedure we present evidence for the existence of two distinct intracellular GLUT4 compartments. We have shown that after fractionation of crude muscle membranes on a discontinuous sucrose gradient the majority of the GLUT4 immunoreactivity was largely present in two sucrose fractions (30 and 35%, w/w, sucrose; denoted F30 and F35 respectively) containing intracellular membranes of different buoyant densities. Here we show that these fractions contained 44±6 and 49±7% of the crude membrane GLUT4 reactivity respectively, and could be further discriminated on the basis of their immunoreactivity against specific subcellular antigen markers. Membranes from the F30 fraction were highly ...
Aspirus Network serves people through Aspirus Wausau Hospital, more than 30 primary and specialty clinics, an affiliated hospital and physician network, and regional home health and hospice services.
1lam: Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallography.
The worlds first wiki where authorship really matters. Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts.
XPNPEP1 - XPNPEP1 (untagged)-ORIGENE UNIQUE VARIANT 1 of Human X-prolyl aminopeptidase (aminopeptidase P) 1, soluble (XPNPEP1), available for purchase from OriGene - Your Gene Company.
2BN7: Structural and Functional Implications of Metal Ion Selection in Aminopeptidase P, a Metalloprotease with a Dinuclear Metal Center.
RNPEPL1 antibody (arginyl aminopeptidase (aminopeptidase B)-like 1) for IHC-P, WB. Anti-RNPEPL1 pAb (GTX111563) is tested in Human, Mouse samples. 100% Ab-Assurance.
In living organisms, enzymes work in complicated networks to perform various biological functions. To analyse such functions, specific enzyme inhibitors are needed. Such inhibitors would be of great...
3 Weeks ago you performed gall bladder surgery on our 11 /12 year old Shih Tzu, Chloe. We just wanted to let you know that she is doing remarkably well! Her recovery was smooth and rapid and she is back to being her "royal" self again. We cant thank you enough for giving us back our girl. She means the world to us and you and your staff were extremely accommodating, sympathetic and supportive - no matter how often we called to check in on her ...
TY - JOUR. T1 - Immunoelectron microscopic demonstration of insulin-stimulated translocation of glucose transporters to the plasma membrane of isolated rat adipocytes and masking of the carboxyl-terminal epitope of intracellular GLUT4. AU - Smith, Robert M.. AU - Charron, Maureen J.. AU - Shah, Neelima. AU - Lodish, Harvey F.. AU - Jarett, Leonard. PY - 1991/8/1. Y1 - 1991/8/1. N2 - Polyclonal antibodies to the amino- or carboxyl-terminal peptide sequences of the GLUT4 transporter protein were used in immunoelectron microscopic studies to demonstrate the location and insulin-induced translocation of GLUT4 in intact isolated rat adipocytes. Labeling of untreated adipocytes with the amino-terminal antibody revealed 95% of GLUT4 was intracellular, associated with plasma membrane invaginations or vesicles contiguous with or within 75 nm of the cell membrane. Insulin treatment increased plasma membrane labeling ≈13-fold, to 52% of the total transporters, and decreased intracellular labeling ...
Strain JC140T exhibited a catalase activity but no oxidase activity. Using the API Rapid ID 32A system, positive reactions were observed for arginine arylimidase, tyrosine arylamidase, histidine arylamidase and indole production. Weak reactions were observed for leucyl glycine arylamidase and glycine arylamidase. All other assays were negative. P. senegalensis is susceptible to penicillin G, amoxicillin + clavulanic acid, imipeneme, vancomycin, clindamycin and metronidazole. By comparison with other phylogenetically closely related Peptoniphilus species, P. senegalensis differed in leucine arylamidase, phenylalanine arylamidase and serine arylamidase activities with P. gorbachii [22], in tyrosine arylamidase activity with P. harei [18] and in α-galactosidase, serine arylamidase, leucine arylamidase, phenylalanine arylamidase, glycine arylamidase and glycine arylamidase activities with P. timonensis [10].. Matrix-assisted laser-desorption/ionization time-of-flight (MALDI-TOF) MS protein analysis ...
Previous studies have demonstrated defects in the trafficking and translocation of GLUT4 glucose transporter in skeletal muscle and adipose tissue to be a major cause of insulin resistance in humans. IRAP (Secreted Insulin Regulated AminoPeptidase) is a protein which collocalizes and is translocated with GLUT4 to the plasma membrane in response to insulin. The extracellular domain of IRAP is cleaved and released in the bloodstream.. Therefore, IRAP plasma concentration could be a good marker of insulin sensitivity.. In this study the investigators seek to confirm this hypothesis by using the gold standard of insulin sensitivity assessment: the hyperinsulinemic-euglycemic clamp.. It is a multicenter descriptive study. ...
Cummins, P., M.; O'connor, B., 1996: Bovine brain pyroglutamyl aminopeptidase (type-1): Purification and characterisation of a neuropeptide-inactivating peptidase
Background Check Brain Alert is not the most famous of supplement brands out there, but interestingly we have gotten a few customer requests on this product.
The present study provides new information regarding the GLUT4 translocation process by directly monitoring the dynamic trafficking of GLUT4 depots during early translocation, steady-state recycling, and re-internalization of GLUT4 in skeletal muscle in situ in a living animal on insulin injection. We have previously studied the early translocation phase (15), but the present study adds considerably to the former by monitoring at higher magnification and higher time resolution. A major new finding is that the majority of insulin-mediated GLUT4 translocation does not involve any high degree of movement of GLUT4 storage vesicles (,1 μm) over longer or even shorter distances, e.g., from the cell interior to the sarcolemma. Surprisingly, the storage vesicles, whether located in the perinuclear region, at the sarcolemma, or at the t-tubules, remain stationary and "melt" away as they are depleted locally without any significant movement away from their original position (Figs. 2 and 3). Another major ...
引用Abcams Anti-Glucose Transporter GLUT1抗体(ab652)的参考文献列表。为您列举引用本产品的发表文章,并提供信息包括论文文献数据库中的检索编号以便您搜寻文章
引用Abcams Anti-Glucose Transporter GLUT3抗体(ab15311)的参考文献列表。为您列举引用本产品的发表文章,并提供信息包括论文文献数据库中的检索编号以便您搜寻文章
Build: Wed Jun 21 18:33:50 EDT 2017 (commit: 4a3b2dc). National Center for Advancing Translational Sciences (NCATS), 6701 Democracy Boulevard, Bethesda MD 20892-4874 • 301-435-0888. ...
Mouse Monoclonal Anti-Aminopeptidase N/CD13 Antibody (CC81) [DyLight 488]. Validated: Flow. Tested Reactivity: Bovine. 100% Guaranteed.
... has been shown to interact with GRB14, TERF1 and Cystinyl aminopeptidase. GRCh38: Ensembl release 89: ENSG00000107854 - ... insulin-responsive aminopeptidase)". Biochem. J. England. 361 (Pt 3): 451-9. doi:10.1042/0264-6021:3610451. ISSN 0264-6021. PMC ... insulin-responsive aminopeptidase)". Biochem. J. 361 (Pt 3): 451-9. doi:10.1042/0264-6021:3610451. PMC 1222327 . PMID 11802774 ...
The most well-characterized oxytocinase is leucyl/cystinyl aminopeptidase, which is also an enkephalinase. Other oxytocinases ... Enkephalinase inhibitor Tsujimoto M, Hattori A (2005). "The oxytocinase subfamily of M1 aminopeptidases". Biochim. Biophys. ... role of aminopeptidases and endopeptidases". Peptides. 12 (5): 1119-25. doi:10.1016/0196-9781(91)90068-z. PMID 1800950. Itoh C ... L-cystine aminopeptidase) in human placenta: purification and characterization". Biol. Pharm. Bull. 20 (1): 20-4. doi:10.1248/ ...
Leucyl/cystinyl aminopeptidase (LNPEP) Angiotensin-converting enzyme (ACE) Enkephalinase inhibitor Oxytocinase Thanawala V, ... They include: Aminopeptidase N (APN) Neutral endopeptidase (NEP) Dipeptidyl peptidase 3 (DPP3) Carboxypeptidase A6 (CPA6) ...
... leucyl/cystinyl aminopeptidase. Other oxytocinases are also known to exist. Amastatin, bestatin (ubenimex), leupeptin, and ... Tsujimoto M, Hattori A (August 2005). "The oxytocinase subfamily of M1 aminopeptidases". Biochimica et Biophysica Acta. 1751 (1 ... role of aminopeptidases and endopeptidases". Peptides. 12 (5): 1119-25. doi:10.1016/0196-9781(91)90068-z. PMID 1800950. Itoh C ... L-cystine aminopeptidase) in human placenta: purification and characterization". Biological & Pharmaceutical Bulletin. 20 (1): ...
... cystinyl aminopeptidase MeSH D08.811.277.656.350.100.373 --- glutamyl aminopeptidase MeSH D08.811.277.656.350.100.511 --- ... cystinyl aminopeptidase MeSH D08.811.277.656.350.555.500 --- glutamate carboxypeptidase ii MeSH D08.811.277.656.350.555.600 ... cystinyl aminopeptidase MeSH D08.811.277.656.675.555.500 --- glutamate carboxypeptidase ii MeSH D08.811.277.656.675.555.600 ... glutamyl aminopeptidase MeSH D08.811.277.656.350.555.700 --- leucyl aminopeptidase MeSH D08.811.277.656.350.555.700.400 --- ...
... a software suite for geomodelling and designing reservoirs Insulin responsive aminopeptidase, an alias for Leucyl/cystinyl ...
... , also known as cystinyl aminopeptidase (CAP), insulin-regulated aminopeptidase (IRAP), human ... Mutations in this gene have been associated to psoriasis risk.(doi:10.1038/jid.2013.317) Cystinyl aminopeptidase has been shown ... The MEROPS online database for peptidases and their inhibitors: M01.011 Cystinyl aminopeptidase at the US National Library of ... "Entrez Gene: LNPEP leucyl/cystinyl aminopeptidase". Sbodio, Juan I; Chi Nai-Wen (August 2002). "Identification of a tankyrase- ...
... alanyl aminopeptidase (aminopeptidase M/N), leucyl/cystinyl aminopeptidase (oxytocinase/vasopressinase), and membrane ... It is an inhibitor of arginyl aminopeptidase (aminopeptidase B), leukotriene A4 hydrolase (a zinc metalloprotease that displays ... Bauvois, B; Dauzonne, D (January 2006). "Aminopeptidase-N/CD13 (EC 3.4.11.2) inhibitors: Chemistry, biological evaluations, and ... an inhibitor of aminopeptidase B, produced by actinomycetes" (29): 97-99. Muskardin, D.T.; Voelkel, N.F.; Fitzpatrick, F.A. ( ...
... cystinyl aminopeptidase EC 3.4.11.4: tripeptide aminopeptidase EC 3.4.11.5: prolyl aminopeptidase EC 3.4.11.6: aminopeptidase B ... aspartyl aminopeptidase EC 3.4.11.22: aminopeptidase I EC 3.4.11.23: PepB aminopeptidase EC 3.4.11.24: aminopeptidase S EC 3.4. ... Clostridial aminopeptidase EC 3.4.11.14: cytosol alanyl aminopeptidase EC 3.4.11.15: aminopeptidase Y EC 3.4.11.16: X-Trp ... tryptophanyl aminopeptidase EC 3.4.11.18: methionyl aminopeptidase EC 3.4.11.19: D-stereospecific aminopeptidase EC 3.4.11.20: ...
... aminopeptidase M/N), bacterial leucyl aminopeptidase (Aeromonas proteolytica aminopeptidase), leucyl/cystinyl aminopeptidase ( ... aminopeptidase A), as well as other aminopeptidases. It does not inhibit arginyl aminopeptidase (aminopeptidase B). Amastatin ... competitive and reversible aminopeptidase inhibitor that was isolated from Streptomyces sp. ME 98-M3. It specifically inhibits ... "Immunoaffinity purification and characterization of native placental leucine aminopeptidase/oxytocinase from human placenta". ...
... s are a catalytic type of protease enzymes that use an activated water molecule bound to one or more aspartate residues for catalysis of their peptide substrates. In general, they have two highly conserved aspartates in the active site and are optimally active at acidic pH. Nearly all known aspartyl proteases are inhibited by pepstatin. Aspartic endopeptidases EC 3.4.23. of vertebrate, fungal and retroviral origin have been characterised.[1] More recently, aspartic endopeptidases associated with the processing of bacterial type 4 prepilin[2] and archaean preflagellin have been described.[3][4] Eukaryotic aspartic proteases include pepsins, cathepsins, and renins. They have a two-domain structure, arising from ancestral duplication. Retroviral and retrotransposon proteases (retroviral aspartyl proteases) are much smaller and appear to be homologous to a single domain of the eukaryotic aspartyl proteases. Each domain contributes a catalytic Asp residue, with an extended active ...
Dick TP, Nussbaum AK, Deeg M, Heinemeyer W, Groll M, Schirle M, Keilholz W, Stevanović S, Wolf DH, Huber R, Rammensee HG, Schild H (October 1998). "Contribution of proteasomal beta-subunits to the cleavage of peptide substrates analyzed with yeast mutants". The Journal of Biological Chemistry. 273 (40): 25637-46. doi:10.1074/jbc.273.40.25637. PMID 9748229 ...
aminopeptidase activity. • protein binding. • serine-type endopeptidase activity. Cellular component. • lamellipodium membrane ...
Some detach the terminal amino acids from the protein chain (exopeptidases, such as aminopeptidases, carboxypeptidase A); ...
Strisciuglio P, Sly WS, Dodson WE, et al. (1991). "Combined deficiency of beta-galactosidase and neuraminidase: natural history of the disease in the first 18 years of an American patient with late infantile onset form". Am. J. Med. Genet. 37 (4): 573-7. doi:10.1002/ajmg.1320370431. PMID 2148053 ...
Several companies are in the early stages of development and testing of this potential class of treatment.[13][14] In March 2008 phase I results were reported for CoMentis Inc's candidate CTS-21166.[15] In April 2012 Merck & Co., Inc reported phase I results for its candidate verubecestat (MK-8931).[16] Merck began a Phase II/III trial of MK-8931 in December, 2012 estimated to be completed in July 2019.[17] In February 2017, Merck halted its late-stage trial of verubecestat for mild to moderate Alzheimer's disease after it was reported as having "virtually no chance" of working according to an independent panel of experts. This came just three months after Eli Lilly & Co. announced its own setback with solanezumab. The results of Merck's trial of verubecestat on patients with early stage Alzheimer's are still expected in February 2019. In September 2014 AstraZeneca and Eli Lilly and Company announced an agreement to codevelop lanabecestat (AZD3293).[18] A pivotal Phase II/III clinical trial of ...
Smulevitch, S.V.; Osterman, A.L.; Galperina, O.V.; Matz, M.V.; Zagnitko, O.P.; Kadyrov, R.M.; Tsaplina, I.A.; Grishin, N.V.; Chestukhina, G.G.; Stepanov, V.M. (1991). "Molecular cloning and primary structure of Thermoactinomyces vulgaris carboxypeptidase T: a metalloenzyme endowed with dual substrate specificity". FEBS Lett. 291: 75-78. doi:10.1016/0014-5793(91)81107-j. PMID 1936254 ...
Leucyl/cystinyl aminopeptidase, also known as cystinyl aminopeptidase (CAP), insulin-regulated aminopeptidase (IRAP), human ... Mutations in this gene have been associated to psoriasis risk.(doi:10.1038/jid.2013.317) Cystinyl aminopeptidase has been shown ... The MEROPS online database for peptidases and their inhibitors: M01.011 Cystinyl aminopeptidase at the US National Library of ... "Entrez Gene: LNPEP leucyl/cystinyl aminopeptidase". Sbodio, Juan I; Chi Nai-Wen (August 2002). "Identification of a tankyrase- ...
It has been proposed that the insulin-regulated aminopeptidase (IRAP) is the main target of Ang IV. This paper discusses ... IRAP has been identified as cystinyl aminopeptidase (CAP, EC 3.4.11.3), placental leucine aminopeptidase (P-LAP, soluble human ... "Angiotensin AT4 receptor ligand interaction with cystinyl aminopeptidase and aminopeptidase N: [125I]Angiotensin IV only binds ... H. Laeremans, H. Demaegdt, J. P. De Backer et al., "Metal ion modulation of cystinyl aminopeptidase," Biochemical Journal, vol ...
Identification of an oxytocinase/vasopressinase-like leucyl-cystinyl aminopeptidase (LNPEP) in teleost fish and evidence for ...
Cystinyl aminopeptidase Homo sapiens 0.901 CHEMBL2608 Lysosomal alpha-glucosidase Homo sapiens 0.877 ...
... transcription factor ZSCAN9 and aminopeptidase ERAP2. The analysis confirmed 50 eSNP-eGenes pairs reported by Peng et al. (2017 ... transcription factor ZSCAN9 and aminopeptidase ERAP2. The analysis confirmed 50 eSNP-eGenes pairs reported by Peng et al. (2017 ... leucyl and cystinyl aminopeptidase; NKAPL, NFKB activating protein like; PE, preeclampsia; PGBD1, piggyBac transposable element ... Endoplasmic Reticulum Aminopeptidase 1; ERAP2, endoplasmic reticulum aminopeptidase 2; GWAS, genome-wide association study; IBD ...
Given that aminopeptidases (APs) play a major role in the metabolism of ... Aminopeptidases; EC 3.4.11.3/Cystinyl Aminopeptidase; EC 3.4.11.7/Glutamyl Aminopeptidase ... Cystinyl Aminopeptidase / metabolism. Drinking / drug effects. Glutamyl Aminopeptidase. Hypertension, Renovascular / enzymology ... Given that aminopeptidases (APs) play a major role in the metabolism of local peptides involved in blood pressure control, ...
Leucyl/cystinyl aminopeptidase. Aliases:. 2010309L07Rik, 4732490P18Rik, CAP, IRAP, PLAP, gp160, vp165. RefSeq:. NC_000083.6 NT_ ...
Leucyl/cystinyl aminopeptidase Assay Type: EvaGreen Application: Gene Expression Unique Assay ID: dMmuEG5065992 Info: EG; Same ... Leucyl/cystinyl aminopeptidase Assay Type: EvaGreen Application: Gene Expression Unique Assay ID: dMmuEG5083246 Info: EG; Same ... Leucyl/cystinyl aminopeptidase Assay Type: Probe Application: Gene Expression Unique Assay ID: dMmuCPE5095614 Info: FAM; Same ... Leucyl/cystinyl aminopeptidase Assay Type: Probe Application: Gene Expression Unique Assay ID: dMmuCPE5095615 Info: HEX; Same ...
Leucyl-cystinyl aminopeptidase Show on y-axis - References (HTP + LTP). References (LTP). References (HTP). Mutation Frequency ...
7. Leucyl-cystinyl aminopeptidase. General function:. Involved in proteolysis. Specific function:. Release of an N-terminal ...
3. Leucyl-cystinyl aminopeptidase. General function:. Involved in proteolysis. Specific function:. Release of an N-terminal ...
TNKS2 has been shown to interact with GRB14, TERF1 and Cystinyl aminopeptidase. GRCh38: Ensembl release 89: ENSG00000107854 - ... insulin-responsive aminopeptidase)". Biochem. J. England. 361 (Pt 3): 451-9. doi:10.1042/0264-6021:3610451. ISSN 0264-6021. PMC ... insulin-responsive aminopeptidase)". Biochem. J. 361 (Pt 3): 451-9. doi:10.1042/0264-6021:3610451. PMC 1222327 . PMID 11802774 ...
LNPEP encodes leucyl/cystinyl aminopeptidase; the four positively selected sites were found to be located in the C-terminal ... EnenkelC, WolfDH (1993) BLH1 codes for a yeast thiol aminopeptidase, the equivalent of mammalian bleomycin hydrolase. J Biol ... KimE, KwakH, AhnK (2009) Cytosolic aminopeptidases influence MHC class I-mediated antigen presentation in an allele-dependent ... 2010) Genetic diversity at endoplasmic reticulum aminopeptidases is maintained by balancing selection and is associated with ...
Evaluation of enzyme inhibitors of cystinyl aminopeptidase and application to the measurement of immunoreactive atrial ...
Metalloexopeptidases: Aminopeptidase (Alanine, Cystinyl, Leucyl, Glutamyl) - Carboxypeptidase (A, B, C, E, Glutamate II). ...
Leucyl-cysteinyl aminopeptidase - M1: Aminopeptidase N. Detailed annotation on the structure, function, physiology, ... Otase , Oxytocinase , placental leucine aminopeptidase , cystinyl aminopeptidase , aminopeptidase Vp165 , angiotensin IV ... Leucyl/cystinyl aminopeptidase (LNPEP) is a zinc-dependent aminopeptidase that cleaves vasopressin, oxytocin, lys-bradykinin, ... M1: Aminopeptidase N: Leucyl-cysteinyl aminopeptidase. Last modified on 11/08/2015. Accessed on 07/06/2020. IUPHAR/BPS Guide to ...
It was considered unlikely that the main metabolizing enzyme for OT in plasma, cystinyl aminopeptidase/oxytocinase20 was ...
... leucyl/cystinyl aminopeptidase/insulin-regulated aminopeptidase (IRAP)]. ...
Measurement of cystinyl aminopeptidase activity. Cystinyl aminopeptidase activity was measured fluorometrically using an ... Oxytocinase (cystinyl aminopeptidase, EC 3.4.11.3) is an enzyme that inactivates oxytocin via hydrolysis of the peptide bonds ... RogiTTsujimotoMNakazatoHMizutaniSTomodaY1996Human placental leucine aminopeptidase/oxytocinase. A new member of type II ... RogiTTsujimotoMNakazatoHMizutaniSTomodaY1996Human placental leucine aminopeptidase/oxytocinase. A new member of type II ...
Rabbit Polyclonal Anti-Glut4 Antibody [DyLight 488]. Validated: WB, Flow, ICC/IF, IHC, IHC-P. Tested Reactivity: Human, Mouse, Rat. 100% Guaranteed.
Mouse Monoclonal Anti-IL-1ra/IL-1F3/IL1RN Antibody (OTI2B1) [Alexa Fluor® 647]. Validated: WB, IHC. Tested Reactivity: Human. 100% Guaranteed.
Angiotensin IV, Insulin-regulated aminopeptidase (IRAP), Cystinyl aminopeptidase (CAP), Aminopeptidase N (AP-N), Structure- ... The analogues inhibited the proteolytic activity of cystinyl aminopeptidase (CAP), frequently referred to as the insulin- ... regulated aminopeptidase (IRAP), and were found less efficient as inhibitors of aminopeptidase N (AP-N). The best Ang IV ... The insulin-regulated aminopeptidase (IRAP) localized in areas of the brain associated with memory and learning is emerging as ...
Leucyl And Cystinyl Aminopeptidase. Protein Coding. 18.04. Novoseek inferred 55 9201003 7. GNRH1 ...
Leucyl/Cystinyl Aminopeptidase Gene Variants in Septic Shock CHEST Nakada, T., Russell, J. A., Wellman, H., Boyd, J. H., Nakada ... leucyl/cystinyl aminopeptidase [LNPEP], and oxytocin receptor [OXTR]), rs18059 in LNPEP (also known as vasopressinase) was ...
leucyl/cystinyl aminopeptidase. Synonyms. gp160, 4732490P18Rik, 2010309L07Rik, IRAP, vp165. MMRRC Submission. 038796-MU ... This summary is for the human ortholog.] This gene encodes a zinc-dependent aminopeptidase that cleaves vasopressin, oxytocin, ...
  • Proteolytic cleavage by glutamyl aminopeptidase A (AP-A) and membrane alanyl aminopeptidase N (AP-N), for example, results in the sequential removal of single amino acid residues from the N-terminal end of the peptide, to form Ang III (Ang II(2-8)) and Ang IV (Ang II(3-8)), respectively [ 6 ]. (hindawi.com)
  • Bestatin (or ubenimex), an antibiotic of natural origin, is a specific, competitive inhibitor of many aminopeptidases, though it does not inhibit aminopeptidase A. Due to its low toxicity it has been administered to cultured cells, animals and humans. (bachem.com)
  • Aminopeptidase N is important for the inactivation in the kidney of blood-borne polypeptidases such as enkephalins, substance P and interleukin 8, and contributes to proteolysis in the small intestine. (ebi.ac.uk)
  • We are not aware of any member of family M1 that hydrolyses Xaa-Pro-bonds, and some that are normally aminopeptidases release the Xaa-Pro dipeptide. (ebi.ac.uk)
  • Peptidase family M1 contains mainly aminopeptidases. (ebi.ac.uk)
  • The peptidases of family M1 are dependent on a single zinc ion for activity, and all members of the family act on the N-terminus of polypeptides, many of them being aminopeptidases. (ebi.ac.uk)