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Biomedical subjects

W Sun

Publications and source records attributed to W Sun.

At least 289 records · Page 16Linked to original sources
PubMed1993

Visceral infection caused by Leishmania tropica in veterans of Operation Desert Storm.

BACKGROUND: Visceral leishmaniasis, usually caused by Leishmania donovani, has rarely been reported from eastern Saudi Arabia, so it was not expected to affect the soldiers of Operation Desert Storm. METHODS: We evaluated eight soldiers with visceral leishmanial infection, examining their serum with an immunofluorescent-antibody assay, examining their marrow or biopsy tissue for amastigotes with an indirect immunofluorescent-monoclonal-antibody assay, and culturing the parasites. Cultured promastigotes were isolated and characterized by isoenzyme analysis. RESULTS: None of the eight soldiers had classic signs or symptoms of visceral leishmaniasis (kala-azar). Seven soldiers had unexplained fever, chronic fatigue, malaise, cough, intermittent diarrhea, or abdominal pain that began up to seven months after they returned to the United States; one had no symptoms. Five had adenopathy or mild, transient hepatosplenomegaly. None had cutaneous manifestations. Diagnoses were made by bone marrow aspiration (seven patients) or lymph-node biopsy (one patient). Six isolates have been identified as L. tropica, which usually causes only cutaneous disease. Of the six patients treated with sodium stibogluconate, five improved and one remained symptomatic. CONCLUSIONS: L. tropica can produce visceral infection that can cause unexplained systemic illness in persons returning from areas where this organism is endemic.

Adult↗
PubMed1993

Binding and phasing of Escherichia coli single-stranded DNA-binding protein by the secondary structure of phage G4 origin of complementary DNA strand synthesis (G4oric).

The origin of phage G4 DNA complementary strand synthesis (G4oric) consists of three stem-loop structures (stem loops I, II, and III) that have been proposed as a recognition site for primase during primer RNA (pRNA) synthesis (Godson, G. N., Barrell, B. G., Staden, R., and Fiddes, J. C. (1978) Nat. New Biol. 276, 236-247; Fiddes, J. C., Barrell, B. G., and Godson, G. N. (1978) Proc. Natl. Acad. Sci. U.S.A. 75, 1081-1085; Sims, J., Capon, D., and Dressler, D. (1979) J. Biol. Chem. 254, 12615-12628). It is generally considered that the double-stranded DNA stem-loop structure is not coated with Escherichia coli single-stranded DNA-binding protein (SSB), but is recognized by primase as naked DNA (Kornberg, A., and Baker, J. (1992) DNA Replication, 2nd Ed., p. 280, W. H. Freeman & Co., New York). Using small G4oric single-stranded DNA fragments of various sizes (302, 278, 149, and 100 nucleotides) consisting of the core 100-nucleotide stem-loop region plus differing lengths of 3'- and 5'-flanking sequence as substrates for gel retardation and DNase I and micrococcal nuclease digestion, we show that under conditions of pRNA synthesis, two SSB tetramers bind to the stem-loop structure. With increasing lengths of 5'- and 3'-flanking sequence, more SSB tetramers are added. Regardless of the number of SSB tetramers bound, however, the region of DNA containing the pRNA initiation site is always left accessible to nuclease digestion. In situ copper-phenanthroline footprinting of individual gel shift assembly intermediates shows that on the 302-nucleotide G4oric, the first two SSB tetramers assemble at random, but the addition of more SSB tetramers results in formation of a unique structure. In this structure, SSB tetramers protect both sides of stem loop III plus the intervening region between stem loops III and I, but leave most of stem loop I and the CTG pRNA initiation site accessible to copper-phenanthroline. Primase can only synthesize pRNA when the stem-loop structure is saturated with SSB and presumably in the unique configuration. The G4oric stem-loop structure therefore appears to dictate the phasing of SSB to leave a primase recognition site as free DNA.

Base Sequence↗
PubMed1993

Kinetics and mechanism of the peroxidase-catalyzed iodination of tyrosine.

The kinetics of iodination of tyrosine by hydrogen peroxide and iodide, catalyzed by both horseradish peroxidase (HRP) and lactoperoxidase (LPO), were studied. The initial rates of formation of both molecular I2 and monoiodotyrosine (MIT) were measured with stopped flow techniques. The following reactions occur in both systems. Enzymatic: FeIII + H2O2-->Fev = O + H2O; Fev = O + I(-)-->FeIII-O-I-; FeIII-O-I- + H(+)-->FeIII + HOI; FeIII-O-I- + I- + H(+)-->FeIII + I2 + HO-. Iodine equilibria: I2 + I-<-->I3-; I2 + H2O<-->HOI + I- + H+. Nonenzymatic iodination, one or both of the following: Tyr + HOI-->MIT + H2O; Tyr + I2-->MIT + I- + H+, where FeIII is native peroxidase, Fev = O is compound I and Tyr is tyrosine. The big difference in the two systems is that the following reaction also occurs with LPO: FeIII-O-I- + Tyr-->MIT + FeIII + HO-, which is the dominant mechanism of iodination for the mammalian enzyme. The overall rate of formation of MIT is about 10 times faster for LPO compared to HRP under comparable conditions. A small decrease in rate occurs when D-tyrosine is substituted for L-tyrosine in the LPO reaction. Thus LPO has a tyrosine binding site near the heme. A kinetically controlled maximum is observed in I3- concentration. Once equilibrium is established, I2 is the dominant form of inorganic iodine in solution. However, hypoiodous acid may be the inorganic iodination reagent.

Horseradish Peroxidase↗
PubMed1993

Organization of the extraocular and preganglionic motoneurons supplying the orbit in the lesser Galago.

The retrograde tracer wheat germ agglutinin-conjugated horseradish peroxidase was used to establish the organization of the extraocular muscle motoneuron pools in a prosimian, Galago senegalensis, for comparison with the organization in monkeys and non-primates. Medical rectus motoneurons were distributed in three subgroups in the ipsilateral oculomotor nucleus, a pattern similar to that of the monkey. Furthermore, the other component of the near response system, the preganglionic parasympathetic motoneurons, were confined within the Edinger-Westphal nucleus, as in the monkey. In contrast, the distribution of the levator palpebrae and superior rectus motoneurons was similar to that of the cat. Specifically, the majority of levator palpebrae motoneurons were located contralaterally, in the caudal central subdivision of the oculomotor nucleus, and the superior rectus motoneurons had a dorsocaudal location in the contralateral oculomotor nucleus. The distributions of motoneurons supplying the superior oblique and lateral rectus muscles were similar to those of other mammals. Unlike previously studied species, the galago was found to have two accessory muscles, that lie beneath the medial and lateral rectus muscles. Motoneurons supplying the accessory rectus muscles were found ventrolateral to the main abducens nucleus, in a position similar to that occupied by the cat accessory abducens nucleus; although others may be present in the main nuclei. Taken together, these results suggest that the organization of extraocular and preganglionic motoneurons in the galago exhibits both monkey and non-primate features. These observations are consistent with the notion that the galago is a primate species whose oculomotor organization is more similar to the general mammalian scheme.

Animals↗
PubMed1993

Cloning two isoforms of rat cyclooxygenase: differential regulation of their expression.

Two isoforms of cyclooxygenase (COX) have been identified in eukaryotic cells: COX-1 encoded by a 2.8-kb mRNA, and a mitogen-inducible COX-2 encoded by a 4-kb mRNA. We have cloned the COX-1 and COX-2 cDNAs from the cDNA library constructed from lipopolysaccharide (LPS)-stimulated rat peritoneal macrophages. The deduced amino acid sequence showed that COX-1 contained 602 amino acids, whereas COX-2 contained 604 amino acids. There is 95% conservation of the nucleotide sequence in the open reading frame of COX-1 between the rat and the mouse, while the homology of the 3' untranslated region is 68% except for a 150 bp segment adjacent to the stop codon which is nonhomologous with the mouse. Transfection of both COX cDNAs into Cos-7 cells resulted in increased COX activity. In rat vascular smooth muscle cells, interleukin-1 beta selectively increased the expression of COX-2, but not that of COX-1, as assessed by enzyme activity, immunoprecipitation of COX proteins, and mRNA analysis. Only the brain among tissues tested exhibits basal expression of COX-2 as the major form of the enzyme. However, COX-2 mRNA was expressed in vivo in the lung and kidney, but not in the heart, after systemic administration of LPS, suggesting that COX-2 but not COX-1 plays a major role in producing COX-derived products of arachidonic acid during endotoxic shock. Thus, the two COX isoforms were differentially expressed, and COX-2 was selectively induced in response to inflammatory stimuli in rats.

Amino Acid Sequence↗
PubMed1993

Mapping of the human NMDA receptor subunit (NMDAR1) and the proposed NMDA receptor glutamate-binding subunit (NMDARA1) to chromosomes 9q34.3 and chromosome 8, respectively.

A role for the N-methyl-D-aspartate (NMDA) receptor in the molecular pathology underlying Huntington disease (HD) has been proposed on the basis of neurochemical studies in HD and the ability of the NMDA receptor to mediate neuronal cell death. The molecular cloning of the human NMDA receptor subunit (NMDAR1) and a proposed glutamate-binding subunit of the NMDA receptor (NMDARA1) have provided an opportunity to test the hypothesis that either of these genes might be directly involved in the causation of HD. We have mapped NMDAR1 to 9q34.3 using in situ hybridization studies and NMDARA1 to human chromosome 8 using a somatic cell hybrid panel. Because the gene causing HD has been localized to chromosome 4p16.3, the chromosome assignments reported here are inconsistent with either of these genes playing a causative role in the molecular pathology of HD. However, it is noteworthy that the gene for torsion dystonia has also been localized by genetic studies to 9q34.3, the same regional map location as NMDAR1.

Animals↗
PubMed1993

Cloning the partial cDNAs of mu-calpain and m-calpain from porcine skeletal muscle.

Calpains are non-lysosomal proteases involved in myofibrillar protein degradation. To facilitate studying the expression of the porcine calpain genes and their influence on protein accretion, we have cloned partial cDNAs for mu- and m-calpain from porcine skeletal muscle via PCR amplification. A 289 bp fragment for mu-calpain and a 629 bp fragment for m-calpain were cloned into the EcoRV site of pBluescript II KS+ vector. The nucleotide sequence for porcine mu-calpain and m-calpain were 92% and 90% identical to corresponding regions of rabbit mu- and m-calpain, respectively. The deduced amino acid sequences for both mu- and m-calpain share 94% identity with respective rabbit mu- and m-calpains. Isoform specificity was validated by Southern hybridization of mu- and m-calpain probes with cloned mu- and m-calpain fragments and Northern hybridization with pig muscle mRNA. These clones will be used to evaluate the role of calpain expression in muscle hypertrophy.

Amino Acid Sequence↗
PubMed1993

Effects of various supplements on voluntary intake and performance by growing cattle consuming forage moderate to high in crude protein.

Growing cattle were supplemented with substances to lessen or increase ruminal ammonia level to determine if consumption of moderate- to high-crude protein (CP) forage is limited by high ruminal ammonia absorption. In Experiment 1 (5 x 5 Latin square), five Holstein steers (198 kg) had ad libitum access to alfalfa cubes (17% CP) without supplementation or with corn at 0.25 or 0.75% body weight (BW) alone (LC or HC) or with 0.06% BW of zeolite (chabazite; LC-Z and HC-Z). Total daily organic water (OM) intake was not affected by treatment (6.08, 6.14, 6.11, 6.19 and 6.09 kg for control, LC, LC-Z, HC and HC-Z, respectively; SE 0.25). In Experiment 2, Simmental crossbred beef calves grazed fescue-clover paddocks in the spring (clipped forage: 21 to 27% CP) for 84 days and were supplemented with 0.25 or 0.75% BW corn alone or with added zeolite (0.06% BW) or lasalocid (0.5 mg/kg BW). Daily gain did not differ among treatments (1.24 to 1.31 kg/day). In Experiment 3 (6 x 6 Latin square), six Holstein steer calves (168 kg) had ad libitum access to medium-quality, orchardgrass-clover hay (15% CP). Steers received one of the following six treatments: no supplement (Control), 0.35% BW ground corn (C), corn plus 0.049% BW urea (C-U), 0.35% BW soybean meal (S), 0.205% BW feather meal (F) or 0.103% BW feather meal, 0.052% BW blood meal and 0.067% BW corn gluten meal (F-BG). Total daily OM intake was 5.00, 5.14, 5.00, 5.11, 4.84 and 4.70 kg for control, C, C-U, S, F and F-BG, respectively (SE 0.13). In Experiment 4 (6 x 6 Latin square), six Holstein steer calves (226 kg) were fed 0.75% BW of alfalfa cubes (19% CP) plus ad libitum access to medium- to high-quality orchardgrass hay (16% CP). Steers received one of the following six treatments: no supplement (Control), corn at 0.25% BW alone (c) or mixed with 0.12% BW peanut skins (C-PSK), a mix of high-CP feedstuffs high in ruminal escape protein (0.029% BW blood meal, 0.038% BW corn gluten meal and 0.028% BW feather meal; C-REP), 0.139% soybean meal (C-S) or soybean meal plus peanut skins (C-PSK-S). Total daily OM intake was 6.16, 6.25, 6.13, 6.52, 6.50 and 6.60 kg for control, C, C-PSK, C-REP, C-S and C-PSK-S, respectively (SE 0.10).(ABSTRACT TRUNCATED AT 400 WORDS)

Absorption↗
PubMed1993

Digestion characteristics by beef cattle consuming bermudagrass or bromegrass hay alone or with alfalfa and(or) corn.

Cannulated beef cattle (four cows: 556 kg initial weight; four steers: 504 kg initial weight) were used in an experiment with two simultaneous Latin squares to determine effects of substituting alfalfa and(or) corn for vegetative bermudagrass (BER; 77% neutral detergent fibre and 5.5% acid detergent lignin) or mature bromegrass (BRO; 70% neutral detergent fibre and 6.6% acid detergent lignin) hay on digestion characteristics. For Controls, BER or BRO was fed at 1.32 or 1.54% body weight of cows and steers, respectively; other treatments entailed substitution for hay DM of alfalfa cubes (17%) or ground corn (33%). A protein supplement was given to all animals. In vitro neutral detergent fibre (NDF) digestion was slightly greater for BER than BRO. Supplement treatments did not affect the concentration of total volatile fatty acids or the molar proportion of propionate in ruminal fluid. True ruminal organic matter (OM) digestion was similar among diets; greater duodenal microbial OM flow and postruminal NDF digestion for BRO than BER diets were responsible for higher (P < 0.05) postruminal OM digestion for BRO diets. Supplement treatment did not affect duodenal microbial nitrogen flow or efficiency of microbial growth. Corn supplementation increased total tract OM digestion (P < 0.05). Alfalfa addition depressed total tract OM and NDF digestibilities more when added to BER than BRO; depressions in total tract NDF digestion with alfalfa and corn substitutions were additive. With constant DM intake, slightly less than ad libitum, alfalfa or corn substituted alone or together for hay did not improve characteristics of digestion by cattle consuming vegetative bermudagrass or mature bromegrass other than increased postruminal and total tract OM digestibilities with corn.

Animal Feed↗
PubMed1993

Two factors that bind to highly conserved sequences in mammalian type C retroviral enhancers.

The transcriptional enhancers of the Moloney and Friend murine leukemia viruses (MLV) are important determinants of viral pathogenicity. We used electrophoretic mobility shift and methylation interference assays to study nuclear factors which bind to a region of these enhancers whose sequence is identical between Moloney and Friend viruses and particularly highly conserved among 35 mammalian type C retroviruses whose enhancer sequences have been aligned (E. Golemis, N. A. Speck, and N. Hopkins, J. Virol. 64:534-542, 1990). Previous studies identified sites for the leukemia virus factor b (LVb) and core proteins in this region (N. A. Speck and D. Baltimore, Mol. Cell. Biol. 7:1101-1110, 1987) as well as a site, overlapping those for LVb and core, for a third factor (N. R. Manley, M. A. O'Connell, P. A. Sharp, and N. Hopkins, J. Virol. 63:4210-4223, 1989). Surprisingly, the latter factor appeared to also bind two sites identified in the Friend MLV enhancer, Friend virus factor a and b1 (FVa and FVb1) sites, although the sequence basis for the ability of the protein to bind these diverse sites was not apparent. Here we describe the further characterization of this binding activity, termed MCREF-1 (for mammalian type C retrovirus enhancer factor 1), and the identification of a consensus sequence for its binding, GGN8GG. We also identify a factor, abundant in mouse T-cell lines and designated LVt, which binds to two sites in the Moloney MLV enhancer, overlapping the previously identified LVb and LVc binding sites. These sites contain the consensus binding site for the Ets family of proteins. We speculate on how distinct arrays of these factors may influence the disease-inducing phenotype.

Animals↗
PubMed1993

Characterization of a protein that binds multiple sequences in mammalian type C retrovirus enhancers.

Mammalian type C retrovirus enhancer factor 1 (MCREF-1) is a nuclear protein that binds several directly repeated sequences (CNGGN6CNGG) in the Moloney and Friend murine leukemia virus (MLV) enhancers (N. R. Manley, M. O'Connell, W. Sun, N. A. Speck, and N. Hopkins, J. Virol. 67:1967-1975, 1993). In this paper, we describe the partial purification of MCREF-1 from calf thymus nuclei and further characterize the binding properties of MCREF-1. MCREF-1 binds four sites in the Moloney MLV enhancer and three sites in the Friend MLV enhancer. Ethylation interference analysis suggests that the MCREF-1 binding site spans two adjacent minor grooves of DNA.

Animals↗
PubMed1993

Feed intake and digestibility by cattle consuming bermudagrass or orchardgrass hay supplemented with soybean hulls and(or) corn.

Effects of supplementing cattle consuming tropical or temperate grass with corn and (or) soybean hulls on feed intake and digestibility were determined. In Exp. 1, eight Holstein steer calves (210 +/- 9.2 and 269 +/- 9.4 kg initial and final BW, respectively), in two simultaneous Latin squares, were given ad libitum access to bermudagrass (B) or orchardgrass (O) hay without supplementation or with (DM basis) .5% of BW of ground corn (C), .7% of BW of soybean hulls (H), or .25% of BW of corn plus .35% of BW of soybean hulls (CH). Total OM intake was greater (P < .05) with than without supplementation (5.05, 6.04, 5.95, 6.06, 6.04, 6.81, 6.61, and 6.69 kg/d), and digestible OM intake was affected by forage source (P < .05), mixing of supplement types (CH versus the mean of C and H; P < .09), and the forage source x supplementation interaction (P < .09; 2.65, 3.40, 3.33, 3.46, 3.71, 4.14, 3.98, and 4.30 kg/d for B, B-C, B-H, B-CH, O, O-C, O-H, and O-CH, respectively). Total tract NDF digestibility was greater (P < .05) for O than for B diets and for H than for C (56.4, 53.9, 58.1, 56.9, 68.5, 64.9, 67.7, and 69.6% for B, B-C, B-H, B-CH, O, O-C, O-H, and O-CH, respectively). In Exp. 2, mature cannulated beef cattle (524 +/- 1.6 kg BW) were used in a design similar to Exp. 1 with comparable dietary supplement levels.(ABSTRACT TRUNCATED AT 250 WORDS)

Animal Feed↗
PubMed1993

[Interaction between r-aminobutyric acid content of the brain regions and cell immunity in the analgesic effect of adrenocorticotropic hormone in rats].

After intraperitoneal injection of ACTH, the content of GABA in hippocampus and the pain threshold were increased. This effect could be decreased by cyclosporin. ACTH decreased SI of MSBT and production of IL-II, and this suppression could be reversed by GABA synthesis inhibitor isoniazid, or GABA receptor blocker picrotoxin. These results suggest that: the analgesic effect of ACTH is related with the increase of GABA content in hippocampus, and cell immunity could be involved the regulation of GABA content in the brain regions. ACTH inhibited the effect of cell immunity, and this effect related to GABA content. Above effect is at least partly mediated by GABA synthesis and GABA receptor.

Adrenocorticotropic Hormone↗
PubMed1992

Selective expression of mitogen-inducible cyclooxygenase in macrophages stimulated with lipopolysaccharide.

Two forms of cyclooxygenase are known to be present in eukaryotic organisms: a cyclooxygenase (COX-1) first purified from ram seminal vesicles encoded by a 2.8-kilobase mRNA, and a newly discovered mitogen-inducible cyclooxygenase (COX-2) encoded by a 4-kilobase mRNA. Expression of these two forms of the enzyme in rat alveolar macrophages stimulated with lipopolysaccharide was investigated by 1) determining the activity of newly synthesized enzyme after inactivating the endogenous enzyme with aspirin; 2) comparing levels of newly synthesized enzyme proteins in cells treated with or without lipopolysaccharide; and 3) assessing the expression of the mRNAs encoding COX-1 and COX-2. Levels of enzyme proteins were assessed by Western blot analysis and immunoprecipitation of 35S-labeled enzyme using two different antibodies, one specific for COX-2 and the other recognizing both forms of the enzyme but preferentially recognizing COX-1. We report here that the enhanced cyclooxygenase activity induced by the bacterial lipopolysaccharide in rat alveolar macrophages is caused by selective expression of the COX-2. Expression of COX-2 in macrophages stimulated by lipopolysaccharide was completely inhibited by dexamethasone, whereas COX-1 was unaffected. In resting unstimulated macrophages, only COX-1 but not COX-2 was detected. Levels of mRNA for the COX-2 in macrophages were increased, but those of the COX-1 were not affected by lipopolysaccharide as assessed by reverse transcription coupled with polymerase chain reaction. These results indicate that increased synthesis of prostaglandins and thromboxanes in lipopolysaccharide-stimulated macrophages results from selective expression of COX-2.

Animals↗
PubMed1992

Proficiency of the Tradescantia-micronucleus image analysis system for scoring micronucleus frequencies and data analysis.

The Tradescantia-micronucleus (Trad-MCN) bioassay is an efficient short-term test for genotoxicity of pollutants. In order to increase the efficiency and to standardize the micronucleus (MCN) scoring process, an automated scoring system was developed using the principle of image analysis in computer science. This assemblage is called the Tradescantia-micronucleus image analysis (Trad-MCNIA) system. The MCN frequencies scored by this system were compared with those scored by human observation for its proficiency. A set of low MCN frequency (around 5 MCN/100 tetrads) slides prepared from a control group, a set of medium MCN frequency (around 20 MCN/100 tetrads) slides prepared from sodium azide treated plant cuttings and a set of high MCN frequency (around 50 MCN/100 tetrads) slides prepared from X-ray treated materials were used for this study. In the low MCN frequency slides, the Trad-MCNIA system scored about the same value as human observation. In the medium and high frequency slides, MCN frequencies scored by the system were lower than those scored by human observers. This discrepancy was corrected by increasing the power of the objective of the microscope in the system. The MCN frequencies scored by the system attained 90% congruity with those scored by human observers after the correction. The scoring speed of the system was about 3.5 times as fast as that by human observers, and the data could be statistically analyzed immediately after the data scores were recorded. Further improvements can be made by upgrading the video camera and the computer speed.

Azides↗
PubMed1992

Cloning of the cDNA encoding a neuronal myosin heavy chain from mammalian brain and its differential expression within the central nervous system.

The complete amino acid sequence of a neuronal myosin heavy chain (MHC) from mammalian brain (1999 amino acids, 230 kDa) has been deduced by sequencing cDNA clones isolated from a rat brain cDNA library. The library was screened using an affinity-purified polyclonal antibody that had been raised against myosin purified from a neuronally-derived cell line (Neuro-2A). Restriction digests of genomic DNA from Neuro-2A cells and rat brain are consistent with an identity of the sequenced isoform from these two sources. RNA blot analysis demonstrates this myosin to exhibit differential expression within the cerebral cortex and spinal cord. No expression was observed in liver, kidney, heart, spleen or skeletal muscle, or even within other regions of the brain. The sequence of this neuronal MHC is compared with those of other non-muscle MHCs, to which it shows an overall similarity of structure, especially with respect to conserved regions within the head (ATP binding site, actin binding site, reactive thiols) and the presence of an alpha-helical coiled-coil tail that can be arranged as 28-residue repeating units plus four skip residues. A unique non-helical tailpiece composed of 72 amino acid residues marks the C-terminus of this neuronal myosin isoform.

Amino Acid Sequence↗
PubMed1992

Molecular cloning, chromosomal mapping, and functional expression of human brain glutamate receptors.

A full-length cDNA clone encoding a glutamate receptor was isolated from a human brain cDNA library, and the gene product was characterized after expression in Xenopus oocytes. Degenerate PCR primers to conserved regions of published rat brain glutamate receptor sequences amplified a 1-kilobase fragment from a human brain cDNA library. This fragment was used as a probe for subsequent hybridization screening. Two clones were isolated that, based on sequence information, code for different receptors: a 3-kilobase clone, HBGR1, contains a full-length glutamate receptor cDNA highly homologous to the rat brain clone GluR1, and a second clone, HBGR2, contains approximately two-thirds of the coding region of a receptor homologous to rat brain clone GluR2. Southern and PCR analysis of a somatic cell-hybrid panel mapped HBGR1 to human chromosome 5q31.3-33.3 and mapped HBGR2 to chromosome 4q25-34.3. Xenopus oocytes injected with in vitro-synthesized HBGR1 cRNA expressed currents activated by glutamate receptor agonists with the following specificity sequence: domoate greater than kainate much greater than quisqualate greater than or equal to alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid greater than or equal to L-glutamate much greater than N-methyl-D-aspartate. The kainate-elicited currents were specifically blocked by 6-cyano-7-nitroquinoxaline-2,3-dione but were insensitive to 2-amino-5-phosphonovalerate and kynurenic acid. These results indicate that clone HBGR1 codes for a glutamate receptor of the kainate subtype cognate to members of the glutamate receptor family from rodent brain.

Amino Acid Sequence↗