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Query: CAS:107-95-9 (beta-alanine)
2,037 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This study describes the influx of taurine and beta-alanine across the brush-border membrane of rabbit distal ileum. The kinetics of JmcTau [concentration at which half-maximal activation occurs (K1/2) = 41 microM and Jmax = 24] are consistent with the kinetics of taurine uptake by jejunal brush-border vesicles. The taurine carrier differs from the beta-alanine carrier by being insensitive to leucine inhibition and by the jejunoileal variation of influx along the small intestine. The K1/2 for sodium and chloride activation of the beta-alanine carrier (48 and 8 mM, respectively) differ markedly from the values reported for the taurine carrier. In addition, taurine is not transported by the beta-alanine carrier. Thus the study demonstrates that the taurine and beta-alanine carriers are separate entities, and it adds to the imino and the taurine carriers the beta-alanine carrier as a third chloride-dependent intestinal transporter of amino acids.
PMID:Distinction between chloride-dependent transport systems for taurine and beta-alanine in rabbit ileum. 156 43

Amino acids are actively transported across the plasma membrane of plant cells by proton-coupled symports. Previously, we identified four amino acid symports in isolated plasma membrane vesicles, including two porters for the neutral amino acids. Here we investigated the effect of amino acid analogues on neutral amino acid transport to identify structural features that are important in molecular recognition by Neutral System I (isoleucine) and Neutral System II (alanine and leucine). D-Isomers of alanine and isoleucine were not effective transport antagonists of the L-isomers. These data are characteristic of stereospecificity and suggest that the positional relationship between the alpha-amino and carboxyl groups is an important parameter in substrate recognition. This conclusion was supported by the observation that beta-alanine and analogues with methylation at the alpha-carbon, at the carboxyl group, or at the alpha-amino group were not effective transport inhibitors. Specific binding reactions were also implicated in these experiments because substitution of the alpha-amino group with a space filling methyl or hydroxyl group eliminated transport inhibition. In contrast, analogues with various substitutions at the distal end of the amino acid were potent antagonists. Moreover, the relative activity of several analogues was influenced by the location of sidechain branches and Neutral Systems I and II were resolved based on differential sensitivity to branching at the beta-carbon. The kinetics of azaserine and p-nitrophenylalanine inhibition of leucine transport were competitive. We conclude that the binding site for the carboxyl end of the amino acid is a well-defined space that is characterized by compact, asymmetric positional relationships and specific ligand interactions. Although the molecular interactions associated with the distal portion of the amino acid were less restrictive, this component of the enzyme-substrate complex is also important in substrate recognition because the neutral amino acid symports are able to discriminate between specific neutral amino acids and exclude the acidic and basic amino acids.
PMID:Structural determinants in substrate recognition by proton-amino acid symports in plasma membrane vesicles isolated from sugar beet leaves. 156 8

The jejuno-ileal variation of amino and imino acid transport across the brush-border membrane of intact rabbit small intestine was studied. For the amino acids tested--beta-alanine, leucine, lysine, MeAIB, proline--and for D-glucose, the rates of transport at constant concentrations increase from very low values in the proximal jejunum to maximum values in the most distal 30 cm of the ileum. The apparent affinity constant for jejunal taurine transport is identical to that of the distal ileum, while the jejunal transport capacity is less than half. In the jejunum, as in the distal ileum, leucine and lysine share both sodium-dependent and sodium-independent carriers. Approx. 50% of the quantitative difference in transport capacity is accounted for by the absence of the beta-alanine carrier in the jejunum. These data indicate that the gradients of transport along the small intestine reflect gradients of transport capacities rather than affinities. In comparison with hamster, man and rat, the rabbit seems unique with respect to the location of transport maximum and the steepness of the gradient along the intestine.
PMID:Variation in amino acid transport along the rabbit small intestine. Mutual jejunal carriers of leucine and lysine. 158 48

Treatment of two cultured renal tubule epithelial cell lines, MDCK and LLC-PK1, with ionomycin produced rapidly evolving models of lethal cell injury characterized by increases of cytosolic free calcium to the microM level within 15 minutes followed by lactate dehydrogenase release and failure to exclude vital dyes that began between 30 and 60 minutes and became extensive after 60 minutes. The pattern of injury was similar when the mitochondrial uncoupler, carbonyl cyanide-m-chlorophenylhydrazone, was added to ionomycin. Carbonyl cyanide-m-chlorophenylhydrazone alone produced severe ATP depletion but not lactate dehydrogenase release. Inclusion of glycine in the experimental medium at concentrations ranging from 0.25 mM to 5 mM did not affect the increases of cytosolic free calcium or ATP depletion but was protective against enzyme release and failure to exclude vital dyes for 180 minutes. Maximal protection was achieved at glycine concentrations between 1 and 5 mM. Several other small neutral amino acids including alanine, beta-alanine, L-serine, 1-aminocyclopropane-1-carboxylic acid, and alpha-aminoisobutyric acid also had protective effects but, glucose, pyruvate, glutamate, glutamine, leucine, valine, and taurine did not. These data indicate that potent protective effects of glycine and other small neutral amino acids previously shown in fresh tubule preparations are fully expressed in cultured tubule cells of diverse origin when appropriate acute injury models are used and the protective effects are sustained for long durations. The suitability of cultured cell lines for prolonged exposure studies will provide a powerful way of further exploring mechanisms of these effects.
PMID:Amino acid protection of cultured kidney tubule cells against calcium ionophore-induced lethal cell injury. 175 12

The JAR human placental choriocarcinoma cell line transports taurine, concentrating it over 1000-fold inside the cell. The transport system is energized by a Na+ gradient and exhibits an absolute requirement for Cl-. Neutral beta-amino acids such as beta-alanine and hypotaurine effectively compete with the system, whereas neutral alpha-amino acids such as alanine, leucine and alpha-aminoisobutyric acid do not. The transport system interacts with gamma-aminobutyric acid to an appreciable extent. Kinetic analysis reveals that the taurine transport system in this cell line is of a high-affinity and low-capacity type (apparent dissociation constant 2.3 +/- 0.3 microM; maximal velocity 88.5 +/- 5.0 pmol/3 min per mg of protein). Pretreatment of the JAR choriocarcinoma cells with phorbol 12-myristate 13-acetate results in the inhibition of the taurine transport system in a dose-dependent manner. The inhibition is blocked by co-treatment of the cells with staurosporine, an inhibitor of protein kinase C. The inactive phorbol ester, 4 alpha-phorbol 12,13-didecanoate, has no effect on the transport system. These data show that the choriocarcinoma cells express a taurine transporter with characteristics similar to those of the taurine transporter described in the normal human placenta, and that the activity of the transporter in these cells is under the regulatory control of protein kinase C.
PMID:Transport of taurine and its regulation by protein kinase C in the JAR human placental choriocarcinoma cell line. 185 47

Incorporation of beta-alanine or gamma-aminobutyric acid in position P2 of ACHPA or Leu psi [CHOHCH2]Val-based tetrapeptides gave highly active renin inhibitors (compounds V, VI, and XVII) with high specificity for renin and a remarkable stability against chymotrypsin. Replacement of the amide bond between P2 and P3 by isosteres (ketomethylenes, hydroxyethylenes, and the corresponding thio-insertion analogues) led to compounds (VIII-XIII, XVIII, and XIX) with renin inhibitory activity in the nanomolar range. Oral activity was achieved by incorporation of polar functionalities at the N-terminus of beta-alanine-containing tetrapeptides. One of these compounds (XXVIII) was chosen for further studies. This inhibitor demonstrated excellent efficacy and a long duration of action after intravenous and oral administration to cynomolgus monkeys.
PMID:Substrate analogue renin inhibitors containing replacements of histidine in P2 or isosteres of the amide bond between P3 and P2 sites. 195 45

Chloride-dependence of influx across the brush-border membrane of distal rabbit ileum was examined for beta-alanine, 2-methylaminoisobutyric acid (MeAIB), leucine, lysine, proline and D-glucose. Influx of leucine at 2 mM and of D-glucose at 0.5 mM was chloride-independent indicating that substitution of isethionate for chloride has no unspecific effect on sodium gradient driven transport processes. In contrast influx of beta-alanine and MeAIB was totally dependent on the presence of chloride ions. In the absence of chloride, proline transport was reduced to 20% of its control level. This remaining transport can be accounted for by the function of the carrier of alpha-amino-monocarboxylic acids. Transport of leucine at 0.1 mM was reduced by absence of chloride. This is in accordance with the observation of leucine transport by the beta-alanine carrier. The kinetics of chloride and sodium activation of transport of MeAIB were examined at 1 mM MeAIB. Chloride activation was characterized by a Hill coefficient of 1 and a K1/2 of 23.5 mM, and sodium activation by a Hill coefficient of 2 and a K1/2 of 51 mM. Thus cotransport of chloride with an imino acid would be compatible with the known rheogenic nature of this transport. This study adds the imino acid carrier and the beta-alanine carrier to the group of chloride-dependent, epithelial amino acid transport systems.
PMID:Chloride-dependence of amino acid transport in rabbit ileum. 211 6

We examined the cytoprotective action of individual amino acids in isolated perfused kidneys during perfusion with either 10 mM lactate or 5 mM glucose. In the absence of amino acids inulin clearance fell rapidly, whereas fractional excretion of phosphate, lactate, or glucose increased to more than 30%; lactate dehydrogenase was released into perfusate and alkaline phosphatase into the urine. Functional deterioration was less in kidneys from rats rendered chronically water diuretic by drinking 5% glucose. Adding 5 mM glycine, L-alanine, beta-alanine, or D-alanine to the perfusate also prevented functional deterioration and release of enzymes. Glycine perfusion increased total phospholipid per microgram DNA by 6%. Aspartate, glutamate, glutamine, taurine, isoleucine, leucine, and valine were not protective. Serine, proline, and alpha-aminoisobutyric acid had small protective effects. Micropuncture measurements of proximal tubular free- and stop-flow pressures showed no effect of L-alanine on glomerular hemodynamics. L-Alanine increased oxygen consumption by both glucose- and lactate-perfused kidneys and increased gluconeogenesis by lactate-perfused kidneys but did not alter renal ATP content or energy charge. L-Alanine was not consumed during 70 min of perfusion and its protective action was not inhibited by blocking transamination with 0.5 mM amino-oxyacetate. The protective action of glycine was not inhibited by blocking glycine metabolism with 0.1 mM cysteamine. Thus the beneficial effects of L-alanine and glycine do not require their metabolism. These observations suggest that small neutral amino acids prevent tubular disruption through their physicochemical effects, which can stabilize membrane protein tertiary structure.
PMID:Mechanisms of perfused kidney cytoprotection by alanine and glycine. 237 94

The amino acid compositions of extracts from the venom sacs of Vespa mandarinia, V. xanthoptera, V. tropica, V. analis and Vespula lewisi were analyzed. omega-Amino acids, which are inhibitory neurotransmitters, such as gamma-amino-n-butyric acid, taurine, beta-alanine and glycine, were predominant components in Vespa, but a minor component in Vespula. Glutamic acid, an aminergic excitatory neurotransmitter, was present in large quantities. Leucine, an insect autotoxin, was detected. Arginine was found in all the venoms and glutamine was also abundant. Tryptophan and histidine, precursors of serotonin and histamine, respectively, were also found. Thus, neuroactive amino acids that may exert inhibitory effects on insects neuronal axons and neuromuscular junctions were present in large amounts, and may facilitate paralysis of insect prey.
PMID:Comparative study of amino acid composition in an extract from hornet venom sacs: high content of neuroactive amino acids in Vespa. 256 3

1. Nutrient transport in cultured human umbilical vein endothelial cells was characterized using a rapid dual-isotope dilution technique. Microcarrier beads with confluent endothelial cells were perfused in small columns, and uptake and efflux were assessed relative to D-mannitol (extracellular tracer) during a single transit through the column. 2. At tracer concentrations significant unidirectional uptakes were measured for L-leucine (53 +/- 2%), L-phenylalanine (73 +/- 2%), L-serine (40 +/- 4%), L-arginine (42 +/- 3%) and L-ornithine (26 +/- 3%). Uptake for L-proline, D-glucose, dopamine and serotonin was lower (6-10%), whereas uptake for the system A analogue 2-methylaminoisobutyric acid (2-MeAIB) was negligible. Uptakes rapidly decreased with time due to tracer efflux. 3. Endothelial cell transport of L-leucine was markedly inhibited during perfusion with 1 mM-BCH (beta-2-aminobicyclo-(2,2,1)-heptane-2-carboxylic acid, system L analogue), L-leucine, D-leucine, L-phenylalanine, L-methionine and L-DOPA. 2-MeAIB, L-cysteine, glycine, L-proline, hydroxy-L-proline, L-aspartate and beta-alanine were poor inhibitors, while L-serine and the cationic substrates L-lysine and L-arginine inhibited uptake by 10-35%. 4. When the kinetics of L-leucine transport were examined over a wide range of substrate concentrations (0.025-1 mM) transport was saturable. A single entry site analysis gave a half-maximal saturation constant Kt = 0.24 +/- 0.08 mM (mean +/- S.E.M., n = 5) and a Vmax = 27.8 +/- 4.6 nmol/min per column (approximately 3 x 10(6) cells). 5. Removal of sodium from the perfusate inhibited tracer uptake of L-leucine, L-serine and L-arginine by respectively 20 +/- 5% (n = 3), 77 +/- 5% (n = 3) and 35 +/- 4% (n = 3). 6. Our results provide the first evidence that cultured human endothelial cells of venous origin express a saturable transport system for large neutral amino acids resembling system L described in brain microvascular endothelium. Detection of Na+-dependent and Na+-independent L-arginine uptake is of interest in view of recent reports that this cationic amino acid may be the physiological precursor for nitric oxide released by endothelium.
PMID:Expression of amino acid transport systems in cultured human umbilical vein endothelial cells. 267 20

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