PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “AMINOISOBUTYRIC ACID”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 505 records · Page 28Linked to original sources
PubMed1990

Evidence for an essential sulfhydryl group at the substrate binding site of the A-system transporter of Ehrlich cell plasma membranes.

Plasma membrane suspensions of Ehrlich ascites cells solubilized with cholic acid were used to study the effects of sulfhydryl reagents on Na(+)-dependent amino acid transport. These suspensions were treated with the sulfhydryl binding agents p-chloromercuribenzenesulfonic acid or N-ethylmaleimide prior to reconstitution for the assay of transport activity. The proteoliposomes formed from dissolved membranes treated with p-chloromercuribenzenesulfonic acid showed no Na(+)-dependent alpha-aminoisobutyric acid transport, while N-ethylmaleimide pretreated membranes retained approximately 90% of the original activity. To avoid interference by the N-ethylmaleimide component, further studies were carried out with membranes pretreated with 200 microM N-ethylmaleimide prior to p-chloromercuribenzenesulfonic acid treatment. A concentration of 25 microM p-chloromercuribenzenesulfonic acid inhibited Na(+)-dependent alpha-aminoisobutyric acid transport by 50%. The degree of inhibition was dramatically reduced in the presence of substrates specific for the A transport system. Using an inhibition index to address the efficacy of inhibition in presence and absence of substrates, it could be shown that an index of 1.0 in presence of p-chloromercuribenzenesulfonic acid was reduced to 0.84 with (methylamino)isobutyric acid alone and 0.05 in the presence of 100 mM Na+ and 5 mM (methylamino)isobutyric acid. Na+ alone offered no protection. The results show that sulfhydryl group(s) on the amino acid carrier may be directly involved in substrate binding and that substrate binding sites are functional in the disaggregated membrane state. Furthermore, Na+ directly affects (methylamino)isobutyrate binding, since the degree of protection by the amino acid analogue against p-chloromercuribenzenesulfonic acid inhibition was influenced by the presence of Na+.(ABSTRACT TRUNCATED AT 250 WORDS)

4-Chloromercuribenzenesulfonate↗
PubMed1977

Amino acid transport in isolated hepatocytes: effect of glucagon.

Amino acid transport was studied in freshly isolated adult rat hepatocytes using non-metabolizable alpha-amino-1-[14C] isobutyric acid and 1-aminocyclopentane-1-[14C] carboxylic acid. In the presence of sodium, hepatocytes concentrated alpha-aminoisobutyric acid; this concentrative component of the transport had properties similar to transport system A. The sodium-independent transport of aminocyclopentane carboxylic acid had properties similar to transport system L (facilitated diffusion). Glucagon stimulated the influx of alpha-aminoisobutyric acid into hepatocytes. The glucagon effect (a) occurred rapidly, but its full expression required two hours of exposure of the cells to hormone; (b) involved new protein (and possibly RNA) synthesis; and (c) occurred at low concentrations of glucagon (50% effect with 0.4 nm). Glucagon stimulated only system A. Cyclic AMP also stimulated the transport of alpha-aminoisobutyric acid. Freshly isolated hepatocytes appear conveniently suited to the investigation of various aspects of the regulation of liver amino acid transport in normal and pathophysiological states.

Amino Acids↗
PubMed1975

Puromycin effect on amino acid transport: differential rates of carrier protein turnover.

In fetal rat calvaria, puromycin selectively inhibited the uptake of certain groups of amino acids. Puromycin treatment decreased the uptake of glycine, L-proline, and alpha-aminoisobutyric acid but was without effect on the active uptake of all other amino acids tested. In studies of alpha-aminoisobutyric acid uptake, puromycin decreased the maximal transport velocity by 70% but had no effect on the affinity of the transport system for the amino acid. With puromycin treatment, the fall-off in rates of alpha-aminoisobutyric acid uptake was first order with a half-life of 68 min. Insulin treatment increased this half-life to 118 min. These findings suggest that protein components of specific transport systems are degraded at varying rates after puromycin blockade of protein synthesis. Hormones that stimulate amino acid transport (e.g., insulin) may decrease the rate of degradation of these protein components.

Amino Acids↗
PubMed1983

Analysis of two chloride requirements for sodium-dependent amino acid and glucose transport by intestinal brush-border membrane vesicles of fish.

Intestinal brush border vesicles of a Mediterranean sea fish (Dicentrarchus labrax) were prepared using the Ca2+-sedimentation method. The transport of glucose, glycine and 2-aminoisobutyric acid is energized by an Na+ gradient (out greater than in). In addition, amino acid uptake requires Cl- in the extravesicular medium (2-aminoisobutyric acid more than glycine). This Na+- and Cl--dependent uptake is electrogenic, since it can be stimulated by negative charges inside the vesicles. The specific Cl- requirement of glycine and 2-aminoisobutyric acid transport is markedly influenced by pH, a change from 6.5 to 8.4 reducing the role played by Cl-. In the presence of Cl-, the Km of 2-aminoisobutyric acid uptake is reduced and its Vmax is enhanced. Cl- affects also a non-saturable Na+-dependent component of this amino acid uptake. Amino acid transport is also increased by intravesicular Cl- (2-aminoisobutyric acid less than glycine). This effect is more concerned with glucose uptake, which can be then multiplied by 2.3. A concentration gradient (in greater than out) as well as the presence of Na+ in the incubation medium seems to enter into this requirement. This intravesicular Cl- effect is not influenced by pH between 6.5 and 8.4.

Amino Acids↗
PubMed1986

Nonspecific adaptation of jejunal amino acid uptake in the rat.

Luminal nutrients are a major effector of intestinal adaptation. Amino acids are trophic to the intestine, but their role in regulating amino acid transport is not well documented. The presence of several distinct amino acid transport systems raises the question of whether adaptation is class-specific. Studies were carried out in parenterally nourished rats receiving a 7-day jejunal infusion of a 3% solution of either aminoisobutyric acid, aspartic acid, glutamine, histidine, lysine, or valine. While all amino acids were trophic to the intestine, their effects on the in vitro uptake of 0.1, 1.0 and 10.0 mM aspartic acid, lysine, and valine (representative acid, basic, and neutral amino acids) were variable and nonspecific. Compared to controls receiving either total parenteral nutrition alone or total parenteral nutrition plus luminal saline, prior lysine and aspartic acid infusion significantly increased in vitro uptake of all three amino acids tested, whereas valine had little effect on transport. No effect on transport was seen with glutamine (actively metabolized by the intestine as is aspartic acid), aminoisobutyric acid (a nonmetabolizable amino acid congener), or histidine (the most trophic amino acid). In conclusion, while individual amino acids cause an adaptation of amino acid uptake, the effects are nonspecific and independent of their metabolic or trophic potential.

Amino Acids↗
PubMed1965

Inhibition of Growth, Synthesis, and Permeability in Neurospora crassa by Phenethyl Alcohol.

Lester, Gabriel (Reed College, Portland, Ore.). Inhibition of growth, synthesis, and permeability in Neurospora crassa by phenethyl alcohol. J. Bacteriol. 90: 29-37. 1965.-Inhibition of the growth of Neurospora crassa in still culture was detected at 0.05% and was complete at a level of 0.2% phenethyl alcohol (PEA). Benzyl alcohol was less inhibitory, and 3-phenyl-1-propanol and phenol were more inhibitory, than PEA; benzylamine and phenethylamine were less inhibitory than the analogous hydroxylated compounds. Inhibition by PEA was not reversed by synthetic mixtures of purines and pyrimidines or vitamins, or by casein digests, yeast extract, or nutrient broth. The germination of conidia was inhibited by PEA, but after an exposure of 8.5 hr no loss of viability was observed. The addition of PEA to growing shake cultures caused a simultaneous inhibition of growth and of the syntheses of ribonucleic and deoxyribonucleic acids and protein; the relationships of these compounds to mycelial dry weight and to one another were constant in growing mycelia, and PEA did not significantly affect these relationships. PEA partially inhibited the uptake of glucose, but severely restricted the accumulation of l-leucine, l-tryptophan, or alpha-aminoisobutyric acid in germinated conidia. The efflux of alpha-aminoisobutyric acid from germinated conidia was somewhat enhanced by PEA, but this effect was not so pronounced as the (complete) inhibition of alpha-aminoisobutyric acid accumulation by PEA. It is suggested that PEA affects primarily the initial influx of alpha-aminoisobutyric acid rather than the subsequent retention of alpha-aminoisobutyric acid.

Journal Article↗
PubMed1970

Amino acid transport in hepatoma cell cultures during tyrosine aminotransferase induction.

Alpha-aminoisobutyric acid transport in hepatoma cells in culture was increased by insulin but not by hydrocortisone. Both of these agents induce tyrosine aminotransferase activity in this system. The apparent increase in alpha-aminoisobutyric acid transport and tyrosine aminotransferase activity produced by glucagon is probably caused by insulin contamination. Insulin did not increase transport in this system until after tyrosine aminotransferase activity had reached maximum levels. The mechanisms underlying increased alpha-aminoisobutyric acid transport appear to differ from those for tyrosine aminotransferase induction with hydrocortisone despite their close association in previous whole animal experiments.

Aminoisobutyric Acids↗
PubMedDate not supplied

A nonribosomal peptide synthetase involved in the biosynthesis of ampullosporins in Sepedonium ampullosporum.

Recently, the saprophytic ascomycete Sepedonium ampullosporum strain HKI-0053 was isolated from a basidiomycete on account of its premature induction of pigment formation in Phoma destructiva, a process often related to the neuroleptic activity of the inducing compound. The active substance was identified as the 15-membered peptaibol type peptide Ampullosporin. Although to date more than 300 peptaibols have been discovered, their biosynthetic machinery has not been characterized yet. By improving the culture conditions it was possible to grow S. ampullosporum in a submerged culture and to increase Ampullosporin production by more than three times to 33 mg/l at reduced fermentation times. The appearance of two high molecular weight proteins, HMWP1 (1.5 MDa) and HMWP2 (350 kDa) was closely related to the production of Ampullosporin during the course of fermentation. Both proteins showed a cross-reaction with antibodies against a core fragment of nonribosomal peptide synthetases (NRPSs). Biochemical characterization of the partially purified enzymes exhibited selectivity for the substrate amino acid alpha-aminoisobutyric acid (Aib). substantiating their involvement in Ampullosporin biosynthesis. Our data suggest that Ampullosporin synthetase has been isolated, and provides the basis for the characterization of the entire biosynthetic gene cluster. Furthermore, this knowledge will enable the manipulation of its NRPS template, in order to engineer mutant strains of Sepedonium ampullosporum which could produce more potent analogues of Ampullosporin.

Amino Acid Sequence↗
PubMed2003

Analysis of peptaibol sequence composition: implications for in vivo synthesis and channel formation.

The sequence entries in the Peptaibol Database were analysed to provide information on compositional features of this unusual family of peptides. The non-standard amino acid alpha-aminoisobutyric acid represents almost 40% of the residues in all the known sequences. Glutamine is the only significant polar residue in peptaibols, and the position and number of these residues appear to be related to their functional properties as ion channels. Aromatic residues are clustered at the termini, which may contribute to stabilization of the peptide vertically within the bilayer. The peptide chain length is strongly weighted towards the longer members of the family (16-20 residues) and likely to be an important feature in their mode of action as transmembrane permeabilizers. The significant skewing towards even numbers of residues and the bias in pairwise distributions of amino acids have implications for the nature of the in vivo synthesis of these peptides via large non-ribosomal protein complexes.

Amino Acid Sequence↗
PubMed1972

Prebiotic synthesis of hydrophobic and protein amino acids.

The formation of amino acids by the action of electric discharges on a mixture of methane, nitrogen, and water with traces of ammonia was studied in detail. The presence of glycine, alanine, alpha-amino-n-butyric acid, alpha-aminoisobutyric acid, valine, norvaline, isovaline, leucine, isoleucine, alloisoleucine, norleucine, proline, aspartic acid, glutamic acid, serine, threonine, allothreonine, alpha-hydroxy-gamma-aminobutyric acid, and alpha,gamma-diaminobutyric acid was confirmed by ion-exchange chromatography and gas chromatography-mass spectrometry. All of the primary alpha-amino acids found in the Murchison Meteorite have been synthesized by this electric discharge experiment.

Alanine↗
PubMed1982

Amino acid transport and protein synthesis in energetically-stable calcium-tolerant isolated cardiac myocytes.

Myocytes isolated by enzymic dispersion from adult rat ventricular tissue are shown to be energetically stable in the presence of 0.5 mM CaCl2. ATP and ADP content and rates of lactate production are comparable with those of intact myocardial tissue and consistent with these cells being tightly coupled. Addition of 2,4-dinitrophenol precipitates rapid changes in adenine nucleotide concentrations and a 10-fold increase in lactate production. Cardiac myocytes selectively transport neutral amino acids of the A and L classes. Transport of the amino acid analogue alpha-aminoisobutyric acid is an active, temperature-dependent and insulin-sensitive process. The apparent Km for alpha-aminoisobutyric acid transport is similar to that determined for embryonic cardiac cells. Mature myocytes incorporate labelled amino acids into cytoplasmic proteins with molecular weights ranging from 10 000 to 150 000. Newly synthesised protein is metabolically stable. The data establishes calcium-tolerant myocytes as an experimental system offering many advantages over whole hearts for short- and long-term studies of protein synthesis and catabolism.

Adenosine Diphosphate↗
PubMed1977

Urinary amino acid excretion by patients with beta-thalassemia.

Twenty-four hour urinary amino acid excretion has been studied in patients with beta-thalassemia (four adult major, two adult intermedia, and three children major). beta-Aminoisobutyric acid was found to be increased (14-fold on the average) in patients with beta-thalassemia without evidence for increase in the excretion of most other amino acids. No correlation of beta-aminoisobutyric acid excretion with the hematological status of the patient was found. Elevated taurine excretion (2-fold) was also noted in the adult patients with beta-thalassemia. Greatly increased excretion of beta-aminoisobutyric acid appears to correlate with a poor prognosis and may reflect generalized tissue catabolism rather than being a specific indicator of ineffective erythropoiesis.

Adolescent↗
PubMed2003

Mitochondrial and metabolic effects of nucleoside reverse transcriptase inhibitors (NRTIs) in mice receiving one of five single- and three dual-NRTI treatments.

Although treatments with nucleoside reverse transcriptase inhibitors (NRTIs) can modify fat metabolism and fat distribution in humans, the mechanisms of these modifications and the roles of diverse NRTIs are unknown. We studied the mitochondrial and metabolic effects of stavudine (d4T), zidovudine (AZT), didanosine (ddI), lamivudine (3TC), zalcitabine (ddC), and three combinations (AZT-3TC, d4T-3TC, and d4T-ddI) in mice treated for 2 weeks with daily doses equivalent to the human dose per body area. Concentrations of AZT and d4T in plasma were lower when these drugs were administered with 3TC or ddI. Whatever the treatment, mitochondrial DNA was not significantly decreased in muscle, heart, brain, or white adipose tissue but was moderately decreased in liver tissue after the administration of AZT, 3TC, or d4T alone. Blood lactate was unchanged, even when NRTIs were administered at supratherapeutic doses. In contrast, the level of plasma ketone bodies increased with the administration of AZT or high doses of d4T but not with ddC, 3TC, or ddI, suggesting that the thymine moiety could be involved. Indeed, the levels of plasma ketone bodies increased in mice treated with beta-aminoisobutyric acid, a thymine catabolite. Treatment with AZT, d4T, or beta-aminoisobutyric acid increased hepatic carnitine palmitoyltransferase I (CPT-I) mRNA expression and the mitochondrial generation of ketone bodies from palmitate. In conclusion, therapeutic doses of NRTIs have no or moderate effects on mitochondrial DNA and no effects on plasma lactate in mice. However, AZT and high doses of d4T increase the levels of hepatic CPT-I, mitochondrial fatty acid beta-oxidation, and ketone bodies, and these catabolic effects are reproduced by beta-aminoisobutyric acid, a thymine metabolite.

Aminoisobutyric Acids↗
PubMed1973

Loss of membrane transport ability in leaf cells and release of protein as a result of osmotic shock.

Osmotic shock severely reduces the ability of aged strips of Phaseolus vulgaris leaves to take up alpha-aminoisobutyric acid, an amino acid analogue which is known to be transported by a specific mechanism. Cold osmotic shock, i.e., transfer from 0.5 m sucrose at 25 C to H(2)O at 2 C, decreases alpha-aminoisobutyric acid uptake almost to zero. Substitution of 10(-3)m ethylenediaminetetraacetate for the sucrose, i.e., treatment which does not involve plasmolysis, produces a similar, but less severe, effect.About 3.5% of the total cell protein is released as a result of cold osmotic shock, by far the greater proportion being liberated into the water during the second stage of the shock treatment. Ethylenediaminetetraacetate and other shock treatments also bring about protein release, and the amount released is correlated with degree of depression of subsequent alpha-aminoisobutyric acid uptake.Shock tissue is capable of recovering a large proportion of its uptake capacity during subsequent immersion in 10(-4)m CaSO(4).Separate estimation of alpha-aminoisobutyric acid influx and efflux showed that the marked effect of shock on net flux is largely attributable to a reduction in influx, and not to an increase in efflux. This and other results indicate that the shock effect on net flux is not due to nonspecific damage to membranes bringing about "leakiness."The fact that alpha-aminoisobutyric acid uptake is reduced to near zero by treatment which allows the cells to retain over 95% of their protein suggests that the shock phenomenon is analogous to that in bacteria, and that the small fraction of protein lost may be closely involved in the transport mechanism.

Journal Article↗
PubMed1979

Relationship of insulin binding to amino acid transport by cultured 14-day embryonic chick heart cells.

The characteristics of insulin receptors were studied in cultured embryonic chick heart cells which demonstrated insulin-responsive amino acid transport. Binding of [125I]iodoinsulin was time dependent, reversible, saturable, species specific, and proportional to cell number. Optimum binding occurred at pH 7.8 in the presence of 0.1% bovine serum albumin. Curvilinear Scatchard plots were found for chicken and bovine insulin binding at 15 and 30 C. Equilibrium association constants (Kas) and maximum capacities were calculated based on a two-receptor model. When studied at 15 C, chicken insulin was bound with Kas of 5.0 and 0.026 nM-1 for the high and low affinity receptors, respectively. Bovine insulin bound with Kas of 2.1 and 0.03 nM-1. The binding capacities of 600 and 9000 molecules/cell for the high and low affinity receptors, respectively, were the same for both species of ligand. At 30 C, the Ka of the high affinity chicken insulin receptor interaction decreased to 1.6 nM-1, whereas the low affinity Ka was not changed. In competitive binding assays, chicken insulin was 4 and 250 times more potent than bovine and guinea pig insulin, respectively. Human GH and mouse epidermal growth factor did not compete with chicken insulin. Although mouse epidermal growth factor did not compete with insulin, it did stimulate 2-aminoisobutyric acid accumulation. The maximal stimulation by this hormone was less than and additive to that produced by the maximal stimulation of insulin. These data indicate that insulin and epidermal growth factor acted through different receptors to stimulate amino acid transport. When insulin-stimulated functional response was compared to calculated receptor occupancy in this two-receptor model, stimulation of amino acid transport paralleled occupancy of the low affinity receptor such that at half-maximal transport stimulation, approximately 50% of these receptors were occupied. Half-maximal stimulation of 2-aminoisobutyric acid transport occurred at 18- and 20-nM concentrations of bovine and chicken insulins, respectively. Guinea pig insulin failed to stimulate 2-aminoisobutyric acid uptake even at 350 nM. Both the affinity of binding in the low affinity class and the insulin concentration for half-maximal stimulation of 2-aminoisobutyric acid transport were independent of temperature in the temperature ranges studied. We conclude that 14-day embryonic chick heart cells possess at least two classes of receptors which bind insulin. Occupancy of the lower affinity class of insulin receptors correlates quantitatively with insulin stimulation of 2-aminoisobutyric acid transport.

Aminoisobutyric Acids↗
PubMed1981

Synthesis and body distribution of alpha-aminoisobutyric acid-L-11C in normal and prostate cancer-bearing rat after chemotherapy.

This paper describes the synthesis of alpha-aminoisobutyric acid-11C (11C-AIB) and studies its body distribution in healthy and tumor-bearing animals. High tissue levels of 11C-AIB were found in organs with high metabolic activity (pancreas, liver, kidney). The prostate tumor 11C-AIB concentrations are significantly lower than that of pancreas, liver, and kidney, but increased when compared with normal prostate levels. Effective chemotherapy, which reduces tumor growth of two different prostate adenocarcinoma cell lines (R-3327-H, R-3327-G) also decreases 11C-AIB levels and the 11C-AIB prostate to tumor ratio.

Adenocarcinoma↗
PubMed1978

Early transport changes during erythroid differentiation of Friend leukemic cells.

Early transport changes occurring during Friend erythroleukemic cell differentiation are reported. A decrease in the rate of 86Rb transport was observed beginning approximately five hours after stimulation with 1.5% dimethylsulfoxide (DMSO), a potent inducer of Friend cell differentiation. By 12 to 14 hours after DMSO addition, the transport rate had stabilized at close to 60% of control level. This decrease in the rate of 86Rb transport preceded a previously reported decrease in cell volume. Other chemical inducers of Friend cells, such as hypoxanthine and ouabain, also caused early decreases in 86Rb influx. In contrast, xanthine, which does not induce Friend cell differentiation, also did not affect 86Rb influx. The transport of two amino acid analogues, alpha-aminoisobutyric acid and 2-aminobicyclo [2,2,1]-heptane-2-carboxylic acid, which differ in their mode of uptake, was also measured following induction by DMSO. The transport rates of both compounds decreased after a 12-hour exposure to DMSO. In contrast, the uptake of 3H-colchicine, a drug which diffuses passively across the cell membrane, was not significantly affected. Studies with several variant cell lines which do not synthesize hemoglobin in response to DMSO indicate that these non-inducible cells can be divided into two classes--those that demonstrate early changes in transport very similar to the changes observed in inducible cell lines and those which exhibit only small changes in transport. Results obtained using a revertant clone have helped to distinguish between those transport changes which are associated with the induction of hemoglobin synthesis and those which are not. In addition, these early transport changes may be useful in defining the stage in the differentiation process at which a particular variant line is blocked.

Amino Acids↗