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At least 595 records · Page 33Linked to original sources
PubMed2001

Tissue-specific expression and gabapentin-binding properties of calcium channel alpha2delta subunit subtypes.

We report here the tissue-specific expression and gabapentin-binding properties of calcium channel alpha2delta subunits. Northern blot analysis demonstrated that human alpha2delta-1, -2, and -3 mRNA all had high levels of expression in brain, heart and skeletal muscle. However, the highest expression of human alpha2delta-2 mRNA was found in lung. Human alpha2delta-1, -2, and -3 mRNAs were detected in all portions of brain tested. Western blotting revealed that alpha2delta-2 protein was predominantly expressed in cerebellar cortex (brain) and undetectable in lung. The dissociation between mRNA and protein levels of human alpha2delta-2 in lung suggests possible post-transcriptional regulation. Although mouse alpha2delta-1 proteins exhibited a similar tissue distribution profile as that of human, tissue distribution of mouse alpha2delta-2 and -3 mRNA revealed a different profile. Mouse alpha2delta-3 mRNA was restricted to brain and mouse alpha2delta-2 mRNA was not detectable in lung. Gel electrophoresis under a reduced condition resulted in a mobility shift of both alpha2delta-1 and alpha2delta-2 proteins, suggesting that alpha2 and delta of alpha2delta-2 protein are linked by disulfide bond as are alpha2 and delta of alpha2delta-1. Scatchard plots revealed a single population of gabapentin binding sites for human alpha2delta-2 with the KD value twofold higher than that of porcine alpha2delta-1 (156 +/- 25 nm vs. 72 +/- 9 nm). Inhibition of gabapentin binding to alpha2delta-2 by selected amino acids and gabapentin analogs produced a binding profile similar, but not identical to that of alpha2delta-1.

Acetates↗
PubMed1986

Cerebral endothelial GABA-T activity: effects of in vivo GABA-T inhibition.

The effects of gamma-aminobutyric acid transaminase (GABA-T) inhibitors on rat endothelial GABA-T activity has been studied utilizing a modified tetrazolium salt histochemical technique. Blue-diformazan staining of cerebrovascular and parenchymal sites of GABA catabolism in normal brain was almost completely prevented in unfixed frozen brain sections from rats subjected to 'in vivo' GABA-T inhibition using aminooxyacetic acid or gabaculine. These results provide histochemical evidence for the efficacy of using systemically administered GABA-T inhibitors to inhibit endothelial GABA-T activity.

4-Aminobutyrate Transaminase↗
PubMed1975

Biosynthesis of p-aminophenylalanine: part of a general scheme for the biosynthesis of chorisimic acid derivatives.

p-Aminophenylalanine is biosynthesized in Vigna vexillata (L.) A. Rich. from shikimic acid through a pathway different from that giving phenylalanine and tyrosine. Experiments with 1,6-14C-labelled shikimic acid demonstrate that the C3-side chain in p-aminophenylalanine is attached to the original C-1 in shikimic acid. The biosynthesis of p-aminophenylalanine in Vigna vexillata probably follows the same pathway as the biosynthesis of this amino acid in Streptomyces species where it is known to be an intermediate in the biosynthesis of chloramphenicol. It is proposed that the biosynthesis takes place through chorismic acid, 4-amino-3-enolpyruvylcyclohexa-1,5-dienecarboxylic acid, 3-(4-amino-1-carboxycyclohexa-2,5-dienyl) pyruvic acid, and 4'-aminophenyl-yruvic acid. It is proposed that chorismic acid can gave rise to 4-amino-3-enolpyruvylcyclohexa-1,5-dienecarboxylic acid, 2-amino-3-enolpyruvylcyclohexa-4,6-dienecarboxylic acid, and isochorismic acid, and that these three compounds and chorismic acid itself by simple rearrangements and elimination reactions can give rise to most known chorismic acid derivatives, i. e.p-hydroxybenzoic acid, 3,4-dihydroxy-3,4-dihydrobenzoic acid, phenylalanine, tyrosine, p-aminobenzoic acid, p-aminophenylalanine, anthranilic acid, 2-amino-3-hydroxy-2,3-dihydrobenzoic acid, 3-(3-carobxyphenyl) alanine, 3-(3-carbocy-4-hydrocyphenyl) alanine, salicylic acid, and 2,3-dihydroxy2,3-dihydrobenzoic acid.

Amines↗
PubMed1993

13C NMR studies of the enzyme-product complex of Bacillus subtilis chorismate mutase.

The chorismate mutase reaction is a rare enzyme-catalyzed 3,3-sigmatropic rearrangement of chorismate to prephenate. Bacillus subtilis chorismate mutase was overproduced and purified from Escherichia coli XL1-Blue (pBSCM2) using a modification of the procedure of Gray et al. (Gray, J. V., Grolinelli-Pimpaneau, B., & Knowles, J. R. (1990) Biochemistry 29, 376-383); the modification leads to minimal contaminating prephenate dehydratase activity (< 0.001%). The native molecular mass of B. subtilis chorismate mutase was determined by gel filtration to be approximately 44 kDa, indicative of a homotrimer of the 14.5-kDa subunits as determined by electrospray mass spectrometry. 13C NMR was used to study the structure of [U-13C]prephenate bound at the active site of B. subtilis chorismate mutase. All the enzyme-bound 13C NMR resonances of [U-13C]prephenate were assigned, and where possible, 1JC,Cs were quantified; [1,3,5,8-13C]prephenate and [2,6,9-13C]prephenate, prepared respectively from [1,3,5,8-13C]chorismate and [2,6,9-13C]chorismate, aided the 13C NMR resonance assignments. Enzyme-bound prephenate exhibits remarkably different chemical shifts relative to free prephenate; the chemical shift changes range from -6.6 ppm for the C6 resonance to 5.6 ppm for the C5 resonance, suggesting a strong perturbation of the C5-C6 bond. 13C NMR studies of model compounds at various pH values and in various solvents suggest that the observed 13C chemical shift changes of enzyme-bound prephenate cannot be rationalized solely on the basis of changes in the pKas of the carboxylic acid groups or hydrophobic solvation at the active site.(ABSTRACT TRUNCATED AT 250 WORDS)

Bacillus subtilis↗
PubMed2004

Total synthesis of (+)-acanthodoral by the use of a Pd-catalyzed metal-ene reaction and a nonreductive 5-exo-acyl radical cyclization.

[reaction: see text] The first total synthesis of the antibiotic acanthodoral (1) has been achieved from 3-methyl-2-cyclohexen-1-one in 19 steps in 2.1% overall yield. The synthesis features the use of a Pd-ene reaction in the presence of CO to form the endocyclic alkene 8, a nonreductive acyl radical cyclization reaction, and a ring contraction reaction by the Wolff rearrangement. (+)-Acanthodoral has also been synthesized starting from (+)-S-2,2-dimethyl-6-methylenecyclohexanecarboxylic acid.

Animals↗
PubMed1999

Transport of pregabalin in rat intestine and Caco-2 monolayers.

PURPOSE: The purpose of this study was to determine if the intestinal transport of pregabalin (isobutyl gamma-aminobutyric acid, isobutyl GABA), a new anticonvulsant drug, was mediated by amino acid carriers with affinity for large neutral amino acids (LNAA). METHODS: Pregabalin transport was studied in rat intestine and Caco-2 monolayers. An in vitro Ussing/diffusion chamber model and an in situ single-pass perfusion model were used to study rat intestinal transport. An in vitro diffusion chamber model was used to evaluate Caco-2 transport. RESULTS: In rat ileum, pregabalin transport was saturable and inhibited by substrates of intestinal LNAA carriers including neurontin (gabapentin), phenylalanine, and proline. Weak substrates of intestinal LNAA carriers (beta-alanine, gamma-aminobutyric acid, and methyl aminoisobutyric acid) did not significantly change pregabalin transport. In Caco-2 monolayers that showed a high capacity for phenylalanine transport, pregabalin transport was concentration- and direction-independent and equivalent in magnitude to the paracellular marker, mannitol. The in vitro and in situ rat ileal permeabilities of the LNAA carrier-mediated compounds neurontin, pregabalin, and phenylalanine correlated well with the corresponding in vivo human oral absorption. CONCLUSIONS: The transport of pregabalin was mediated by LNAA carriers in rat ileum but not in Caco-2 monolayers. Caco-2 was not an appropriate model for evaluating the in vivo human oral absorption of pregabalin and neurontin.

Acetates↗