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PubMed2001

Natto mucilage containing poly-gamma-glutamic acid increases soluble calcium in the rat small intestine.

We prepared natto (fermented soybeans) mucilage containing poly-gamma-glutamic acid (gamma-PGA) from commercial natto. The effect of natto mucilage on calcium (Ca) solubility in vitro and in vivo was investigated. Ca solubility in vitro increased with an increase in the amount of natto mucilage, due to inhibition of the formation of an insoluble complex of Ca with phosphate by natto mucilage. Rats were fed with 5 g of soybean protein isolate, natto, mucilage-free natto, or natto mucilage diet for 1.5 h. Small intestinal contents were collected 2.5 h after ingestion. In the lower half of the small intestine, both the amount and the percentage of soluble Ca of intestinal contents were significantly higher (P < 0.001) in rats fed with natto mucilage diet than in those fed with the other diets. Natto mucilage also increased Ca solubility in vivo. These results suggested that gamma-PGA is responsible for the increasing effect of natto mucilage on Ca solubility.

Animals↗
PubMed1999

Glutamate excretion as a major kinetic bottleneck for the thermally triggered production of glutamic acid by Corynebacterium glutamicum.

The study was aimed at evaluating the extent of flux control exercised by the amino acid excretion step on the glutamate production flux in C. glutamicum 2262 strain that is induced for glutamate excretion by an upward temperature shift. Cells initially induced to excrete glutamate were cultivated at different controlled temperatures between 33 and 40 degrees C, and changes in glutamate excretion flux and intracellular concentration were determined in response to increased culture temperature. The fastest growth rate of 0.45 h(-1) and the lowest glutamate excretion rate of 1 mmole/g dw x h were observed at 33 degrees C, together with a high intracellular 0.5 mmole/g dw glutamate accumulation. On the contrary, the fastest glutamate excretion rate of 6 mmole/g dw x h was obtained at 40 degrees C, when cell growth was arrested and the internal glutamate level reduced to 0.25 mmol/g dw. The observed sixfold increase in excretion flux as a result of the temperature increase clearly suggests a specific effect of temperature on the glutamate export system which appears as the major kinetic bottleneck for the glutamate production flux. This conclusion is corroborated by the high internal accumulation of glutamate which, even under the fastest excretion conditions, severely inhibits the activity of the glutamate biosynthesis pathway.

Bioreactors↗
PubMed2000

Potentiation of ovarian OCa-1 tumor radioresponse by poly (L-glutamic acid)-paclitaxel conjugate.

PURPOSE: It has been shown that paclitaxel (TXL) can strongly enhance tumor cells' sensitivity to radiation. We examined whether the radiosensitizing effect of paclitaxel can be further enhanced when it is delivered systemically as a polymer-drug conjugate that provides enhanced tumor uptake and prolonged release of TXL in the tumor. METHODS AND MATERIALS: C3Hf/Kam mice bearing 8-mm murine ovarian OCa-1 tumors were treated with i.v.-injected Poly(L-glutamic acid)-paclitaxel (PG-TXL) at an equivalent TXL dose of 80 mg/kg, followed 24 h later by single doses of local radiation ranging from 5 to 15 Gy. To determine how long the radiopotentiation persisted at extended times after PG-TXL administration, mice with OCa-1 tumors were given i.v. PG-TXL and 4, 24, 48, 72, 120, or 168 h later their tumors were irradiated at a dose of 10 Gy. Antitumor activity was determined by delay in tumor growth. Cell cycle distribution was assayed using flow cytometry. Tumor vascular volume was estimated using Tc-99 m-labeled red blood cells. RESULTS: PG-TXL strongly potentiated the radioresponse of the OCa-1 tumor. The enhancement factors ranged from 2.79 to 4.28, depending on radiation dose, when PG-TXL preceded radiation by 24 h. The enhancement factor derived from radiation dose-response curves was as high as 5.13. The radiosensitizing effect of PG-TXL was also dependent on the interval between PG-TXL administration and radiation delivery, with greater enhancement been observed when the interval was decreased. The percentage of G2/M cells was significantly increased to 21.4% 48 h after PG-TXL but declined to a preinjection level of 14.8% 72 h after PG-TXL. PG-TXL only moderately increased the tumor vascular volume by 37% 24 h after PG-TXL administration. CONCLUSION: PG-TXL markedly potentiated response of OCa-1 tumor to radiation. When compared to literature data obtained from the same tumor model used here, PG-TXL exhibited stronger radiosensitization effect than TXL. Although its action is possibly mediated by arrest of cells in G2/M phases of cell cycle and by increased tumor blood supply, PG-TXL may exert its radiopotentiation activity through increased tumor uptake of PG-TXL and sustained release of TXL in the tumor. Our results show that conjugation of TXL to a polymer has the potential to further enhance its radiosensitizing activity and that clinical trials of PG-TXL in combination with radiation is warranted.

Animals↗
PubMedDate not supplied

Synthesis of poly(epsilon-caprolactone)-b-poly(gamma-benzyl-L-glutamic acid) block copolymer using amino organic calcium catalyst.

A biodegradable two block copolymer, poly(epsilon-caprolactone)-b- poly(gamma-benzyl-L-glutamic acid) (PCL-PBLG) was synthesized successfully by ring-opening polymerization of N-carboxyanhydride of gamma-benzyl-L-glutamate (BLG-NCA) with aminophenyl-terminated PCL as a macroinitiator. The aminophenethoxyl-terminated PCL was prepared via hydrogenation of a 4-nitrophenethoxyl-terminated PCL, which was novelly obtained from the polymerization of epsilon-caprolactone (CL) initiated by amino calcium 4-nitrobenzoxide. The structures of the block copolymer and its precursors from the initial step of PCL were confirmed and investigated by 1H NMR, FT-IR, GPC, and FT-ICRMS analyses and DSC measurements.

Biocompatible Materials↗
PubMed1992

Characterization of hematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences.

Protein tyrosine phosphatases (PTPases) are a family of enzymes important in cellular regulation. Characterization of two cDNAs encoding intracellular PTPases expressed primarily in hematopoietic tissues and cell lines has revealed proteins that are potential regulators of signal transduction. One of these, SHP (Src homology region 2 [SH2]-domain phosphatase), possesses two tandem SH2 domains at the amino terminus of the molecule. SH2 domains have previously been described in proteins implicated in signal transduction, and SHP may be one of a family of nonreceptor PTPases that can act as direct antagonists to the nonreceptor protein tyrosine kinases. The SH2 domains of SHP preferentially bind a 15,000-Mr protein expressed by LSTRA cells. LSTRA cells were shown to express SHP protein by immunoprecipitation, thus demonstrating a potential physiological interaction. The other PTPase, PEP (proline-, glutamic acid-, serine-, and threonine-rich [PEST]-domain phosphatase), is distinguished by virtue of a large carboxy-terminal domain of approximately 500 amino acids that is rich in PEST residues. PEST sequences are found in proteins that are rapidly degraded. Both proteins have been expressed by in vitro transcription and translation and in bacterial expression systems, and both have been demonstrated to have PTPase activity. These two additional members of the PTPase family accentuate the variety of PTPase structures and indicate the potential diversity of function for intracellular tyrosine phosphatases.

Amino Acid Sequence↗
PubMed1996

Structure and the promoter region of the mouse gene encoding the 67-kD form of glutamic acid decarboxylase.

We have cloned and determined the complete structure of the murine gene encoding the 67-kD form of glutamic acid decarboxylase (GAD67), the gamma-aminobutyric acid synthetic enzyme. Its coding region comprises 18 exons spanning 42 kb of genomic DNA. Exon 1 together with 64 bp of exon 2 defines the 5' untranslated region of GAD67 mRNA. Exon 18 specifies the protein's carboxyl terminal and the entire 3' untranslated region. Exons 7/A and 7/B are solely contained in the coding regions of two alternatively spliced bicistronic embryonic mRNAs, which code for the truncated embryonic GAD forms. The promoter region (P1) corresponding to the main group of transcription initiation sites is devoid of TATA and CAAT boxes but has putative binding sites for the transcription factor SP1 and is embedded in a large G + C-rich domain of a CpG island, features shared by the promoters of constitutively expressed housekeeping genes. Primer extension data suggests the existence of additional transcription start sites at 130 bp and 295 bp upstream from the major initiation site that are utilized less frequently in adult brain. The tentative distal promoters (P2 and P3) that correspond to the minor start sites resemble tissue-specific promoters with TATA and CAAT-like boxes. In 1.3 kb of the 5'-upstream region, we identified several putative transcription factor binding sites such as AP2, Hox, E-box, egr-1, and NF-kappaB and putative neuronal-specific regulatory elements, including the neuronal-restrictive silencer element, which may have functional significance in the developmental and tissue-specific expression of the GAD67 gene.

Animals↗
PubMed1999

Conformation-dependent inhibition of gastric H+,K+-ATPase by SCH 28080 demonstrated by mutagenesis of glutamic acid 820.

Gastric H+,K+-ATPase can be inhibited by imidazo pyridines like 2-methyl-8-[phenylmethoxy] imidazo-(1,2a) pyridine 3-acetonitrile (SCH 28080). The drug shows a high affinity for inhibition of K+-activated ATPase and for prevention of ATP phosphorylation. The inhibition by SCH 28080 can be explained by assuming that SCH 28080 binds to both the E2 and the phosphorylated intermediate (E2-P) forms of the enzyme. We observed recently that some mutants, in which glutamic acid 820 present in transmembrane domain six of the catalytic subunit had been replaced (E820Q, E820N, E820A), lost their K+-sensitivity and showed constitutive ATPase activity. This ATPase activity could be inhibited by similar SCH 28080 concentrations as the K+-activated ATPase of the wild-type enzyme. SCH 28080 also inhibited ATP phosphorylation at 21 degrees C of the mutants E820D, E820N, and E820A, although with varying efficacy and affinity. ATP-phosphorylation of mutant E820Q was not inhibited by SCH 28080; in contrast, the phosphorylation level at 21 degrees C was nearly doubled. These findings can be explained by assuming that mutation of Glu820 favors the E1 conformation in the order E820Q >E820A >E820N >wild-type = E820D. The increase in the phosphorylation level of the E820Q mutant can be explained by assuming that during the catalytic cycle the E2-P intermediate forms a complex with SCH 28080. This intermediate hydrolyzes considerably slower than E2-P and thus accumulates. The high tendency of the E820Q mutant for the E1 form is further supported by experiments showing that ATP phosphorylation of this mutant is rather insensitive towards vanadate, inorganic phosphate, and K+.

Adenosine Triphosphate↗
PubMed1989

Region specific regulation of glutamic acid decarboxylase mRNA expression by dopamine neurons in rat brain.

In situ hybridization histochemistry and RNA blots were used to study the expression of glutamic acid decarboxylase (GAD) mRNA in rats with or without a unilateral lesion of midbrain dopamine neurons. Two populations of GAD mRNA positive neurons were found in the intact caudate-putamen, substantia nigra and fronto-parietal cortex. In caudate-putamen, only one out of ten of the GAD mRNA positive neurons expressed high levels, while in substantia nigra every second of the positive neurons expressed high levels of GAD mRNA. Relatively few, but intensively labelled neurons were found in the intact fronto-parietal cerebral cortex. In addition, one out of six of the GAD mRNA positive neurons in the fronto-parietal cortex showed a low labeling. On the ipsilateral side, the forebrain dopamine deafferentation induced an increase in the number of neurons expressing high levels of GAD mRNA in caudate-putamen, and a decrease in fronto-parietal cortex. A smaller decrease was also seen in substantia nigra. However, the total number of GAD mRNA positive neurons were not significantly changed in any of these brain regions. The changes in the levels of GAD mRNA after the dopamine lesion were confirmed by RNA blot analysis. Hence, midbrain dopamine neurons appear to control neuronal expression of GAD mRNA by a tonic down-regulation in a fraction of GAD mRNA positive neurons in caudate-putamen, and a tonic up-regulation in a fraction of GAD mRNA positive neurons in fronto-parietal cortex and substantia nigra.

Animals↗
PubMed2005

Highly enantioselective synthesis of (2S)-alpha-(hydroxymethyl)-glutamic acid by the catalytic Michael addition of 2-naphthalen-1-yl-2-oxazoline-4-carboxylic acid tert-butyl ester.

[reaction: see text]. Highly enantioselective synthesis of a potent metabotropic receptor ligand, (2S)-alpha-(hydroxymethyl)-glutamic acid (2, HMG) was accomplished by the catalytic Michael addition of 2-naphthalen-1-yl-2-oxazoline-4-carboxylic acid tert-butyl ester (3b), using the phosphazene base, BEMP, in CH(2)Cl(2) at -60 degrees C in the presence of (S)-binaphthyl quaternary ammonium salt 4.

Combinatorial Chemistry Techniques↗
PubMed1997

Double-label immunofluorescence study of glutamic acid decarboxylase in the fetal and adult ovine pancreas by light and confocal microscopy: evidence for predominant beta-cell coexpression.

Glutamic acid decarboxylase (GAD) is present in the central nervous system and in several nonneuronal tissues including the pancreatic islets. There are two isoforms with molecular weights of 65 kDa (GAD65) and 67 kDa (GAD67). The cellular specificity of the two molecular forms of GAD and their levels within the mammalian islets may be species-dependent, being coexpressed in both beta and in non-beta cells. We have examined the ovine pancreas, from the adult and fetal stages of late gestation, for the expression of GAD65 within the islet cells by double-label immunofluorescence light and confocal microscopy. In the adult tissue, GAD65 was colocalized in a majority of the beta cells (> 95%), with only a few glucagon and somatostatin cells (< 5%) showing immunolocalization. During the fetal stages GAD65 also showed a similar predominant beta-cell coexpression. The enzyme was also detected in a few fetal glucagon (< 5%) but not somatostatin cells. In the degenerating large fetal islets, GAD65 was also observed in the majority of the residual beta cells. These results demonstrate that in the ovine pancreas GAD65 is expressed during fetal development and is predominantly beta-cell-restricted. This pattern of expression is maintained during adult life. However, the physiological role of pancreatic GAD and/or its biosynthetic product, gamma-aminobutyric acid, in islet function in the sheep and in other ruminants remains unclear.

Aging↗
PubMed1985

[Increase in the maximum intensity of myocardial contractile function using glutamic acid].

In experiments on 54 isolated papillary muscles from guinea-pig hearts a rise in contraction velocity and amplitude was induced by the increment in stimulation rate. Maximal contractile indices and the rate at which they were observed were the less the greater the muscle thickness limiting oxygen supply. At any rate the relaxation velocity of thin muscles (cross sectional area 0.38 mm2) was approximately twice higher than the contraction velocity. The difference became smaller as the muscle thickness increased and completely disappeared in experiments on thick muscles (cross sectional area 1.34 mm2). Addition of glutamic acid (3.5 mM) to perfusate did not influence contraction and relaxation values at a rate of 0.5-2.0 Hz but prevented their depression at a rate of 2.5-3.5 Hz, which was typical of thick muscles. This effect seems to be related to improved energy production by myocardial cells during hypoxia or ischemia.

Animals↗
PubMed1987

Glutamic acid decarboxylase activity in discrete hypothalamic nuclei during the development of rats.

We have assessed the activity (nmol/mg protein/h) of glutamic acid decarboxylase (GAD) in discrete hypothalamic nuclei before and after sexual maturation in the developing female rat. Activity in other brain regions including the cortex, septum and caudate-putamen was also assessed. While there appears to be a general rise (approximately 30%), with age, in GAD activity, the rise is most marked, and highly significant (P less than 0.001), in the anterior portion of the hypothalamus (56%). In contrast, no significant increase of GAD activity was found in the medical basal hypothalamus.

Animals↗
PubMed2006

[Influence of different light source on the laser Raman spectra in determination of sodium glutamic acid].

The influences of different laser source and different light power on laser Raman spectra were studied for the sodium glutamic acid. The results show that some influences existed using different wavelength and power of light source the peak shifting 6 cm(-1). As UV laser has great light power, the samples were destroyed, making the Raman spectra- reduce or disappear. The attenuation of light was needed. The linear relation existed between the Raman intensity and the power of laser light source, and the correlation coefficient was more then 0.999. The Raman intensity per light power unit was related to the wavelength, and was not related to the power of laser source.

Sodium Glutamate↗
PubMed2000

Glutamic acid mutagenesis of retinoblastoma protein phosphorylation sites has diverse effects on function.

The retinoblastoma tumor suppressor gene (Rb) has many functions within the cell including regulation of transcription, differentiation, apoptosis, and the cell cycle. Regulation of these functions is mediated by phosphorylation at as many as 16 cyclin-dependent kinase (CDK) phosphorylation sites in vivo. The contribution of these sites to the regulation of the various Rb functions is not well understood. To characterize the effect of phosphorylation at these sites, we systematically mutagenized the serines or threonines to glutamic acid. Thirty-five mutants with different combinations of modified phosphorylation sites were assayed for their ability to arrest the cell cycle and for their potential to induce differentiation. Only the most highly substituted mutants failed to arrest cell cycle progression. However, mutants with as few as four modified phosphorylation sites were unable to promote differentiation. Other mutants had increased activity in this assay. We conclude that modification of Rb phosphorylation sites can increase or decrease protein activity, that different Rb functions can be regulated independently by distinct combinations of sites, and that the effects of modification at any one site are context dependent.

Bone Neoplasms↗
PubMed1997

Glutamic acid decarboxylase gene expression in the dopamine-denervated striatum: effects of intrastriatal fetal nigral transplants or chronic apomorphine treatment.

Glutamic acid decarboxylase mRNA expression was studied in the striatum of rats subjected to a unilateral 6-hydroxydopamine lesion of the nigrostriatal dopamine projection, followed by either intrastriatal transplants of fetal nigral neurons or chronic apomorphine treatment. For in situ hybridization histochemistry, a 35S-labelled cRNA probe selective for the mRNA encoding the 67-kDa isoform of the enzyme (GAD67) was used. The results show that fetal dopaminergic grafts in the dopamine-denervated striatum restore an inhibitory control on GAD67 gene expression in the host neurons and also counteract the up-regulation of GAD67 mRNA levels induced by chronic apomorphine treatment.

Animals↗
PubMed1993

The rat nucleus accumbens: two levels of complexity in the distribution of glutamic acid decarboxylase (67 kDa) and preproenkephalin messenger RNA.

The distribution of messenger RNAs (mRNAs) encoding the 67 kDa isoform of glutamic acid decarboxylase (GAD67), a rate-limiting enzyme in the biosynthesis of gamma-aminobutyric acid, and preproenkephalin (PPE), the precursor of enkephalin, was analysed in the rat nucleus accumbens (NAS) taking in account its compartmentation in 'core' (NAS(core)) and 'shell' (NASshell). While GAD67 mRNA levels were more abundant (+48%) in NASshell than in NAS(core), hybridization signals for PPE mRNA were mainly found in NAScore. At a cellular level, hybridization signals for GAD67 mRNA were present in 75% and 80% of neurons NASshell and NAS(core), respectively. The level of GAD67 mRNA found higher in the NASshell corresponds in fact to a greater density of neurons in NASshell than in the NAS(core). The hybridization signals for PPE mRNA were observed in very few neurons of NASshell and in around half of the neurons in NAS(core). Besides this medio to lateral difference, GAD67 and PPE mRNAs were distributed in NAS(core) according to a rostro-caudal gradient, the content of both mRNAs being higher in the rostral part than the caudal part of this area.

Animals↗
PubMed1988

Cholinergic neurons containing GABA-like and/or glutamic acid decarboxylase-like immunoreactivities in various brain regions of the rat.

The coexistence of immunoreactivities for choline acetyltransferase (ChAT) and glutamic acid decarboxylase (GAD) and/or gamma-aminobutyric acid (GABA) was revealed in some brain regions of the rat, using the peroxidase-antiperoxidase method. Consecutive 40 micron thick vibratome sections were incubated in different antisera and those cells which were bisected by the plane of sectioning so as to be included at the paired surfaces of two adjacent sections were identified. The coexistence of the immunoreactivities for ChAT and GAD or GABA in the same cell could thus be determined by observing the immunoreactivity of the two halves of the cell incubated in two different antisera. In the retina, cerebral cortex, basal forebrain and spinal cord, colocalization of ChAT-like and GAD-like or GABA-like immunoreactivities was observed in some cell types, whereas no such colocalization was observed in cells in the striatum or brainstem. In the retina, the majority of ChAT-like immunoreactive (ChAT-LI) amacrine cells contained GABA-like or GAD-like immunoreactivity. About half of the ChAT-LI neurons in the cerebral cortex showed GABA-like immunoreactivity. In the basal forebrain only a small proportion of ChAT-LI neurons (0.6%) contained GAD-like immunoreactivity. In the spinal cord, about one-third of ChAT-LI central canal cluster cells and about half of ChAT-LI dorsal horn cells showed GAD-like and/or GABA-like immunoreactivities. These observations indicate the possible coexistence of two classical transmitters, GABA and acetylcholine, in various brain regions and spinal cord of the rat.

Animals↗
PubMed1981

Sodium dependence of high affinity glutamic acid transport in cortical synaptosomes--a comparison of Long-Evans and Sprague-Dawley rats.

The sodium dependence of high affinity glutamic acid transport has been studied in cortical synaptosomes from Sprague-Dawley rats and compared to previous studies with Long-Evans rats. Initial velocity of uptake was measured as a function of both glutamate and sodium concentration, and the data fitted to the rate equations for the same set of models that was utilized in the Long-Evans studies. The minimal best-fit model was found to be identical to that found previously for Long-Evans animals. Thus there are no fundamental differences in the basis of the sodium dependence of high affinity glutamate transport between the two groups. However, since the constants describing the best fit model are different for the two groups of animals, there are quantitative differences in the transport mechanism between the two groups. The rate equation for the minimal best-fit model permits certain functions to be defined in terms of dissociation and translocation constants, substrate, sodium, and total carrier concentrations. These functions were calculated and then utilized to demonstrate the quantitative differences in the transport mechanism in the two groups.

Animals↗