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V T Tran

Publications and source records attributed to V T Tran.

At least 37 records · Page 2Linked to original sources
PubMed1992

Human retinal pigment epithelial cells possess beta 2-adrenergic receptors.

Beta-adrenergic receptors on cultured human retinal pigment epithelium were demonstrated by the binding of [125I]cyanopindolol. Its pharmacologic specificity was also examined. Specific [125I]cyanopindolol binding was saturable, with a dissociation constant of 130 pM and a receptor density of 12 fmol per one-half million cells, which is equivalent to 14,000 receptor sites per retinal pigment epithelial cell. Agonists competed for specific [125I]cyanopindolol binding, with the following rank order of potencies: (-)-isoproterenol > (-)-epinephrine > (-)-norepinephrine. Beta 2-selective antagonist ICI-118551 was approximately 3 log orders more potent than the beta 1-selective antagonist, betaxolol. These receptors were also coupled to an adenylate cyclase. These results suggest strongly that cultured human retinal pigment epithelial cells possess beta 2-adrenergic receptors. The potential significance of these findings with regard to retinal pigment epithelial functions is discussed herein.

Adenylyl Cyclases↗
PubMed1992

Differential localization of dopamine D1 and D2 receptors in rat retina.

Dopamine interacts with distinct receptors on different target neurons in the rat retina. Dopamine receptors were labeled in the rat retina by autoradiography using 3H-SCH-23390 and 3H-spiperone binding to retinal sections. The 3H-SCH-23390 binding to D1 receptors was most concentrated in the inner plexiform, inner nuclear, and ganglion cell layers; it was absent from the outer nuclear layer and the photoreceptor inner and outer segments. Competition studies indicated that 3H-SCH-23390 binding to the inner retina was inhibited with high affinities by the D1-specific agonist and antagonist, SKF-38393 and SCH-23390. The D2-specific compounds were ineffective in competing for 3H-SCH-23390 binding. The 3H-spiperone binding to D2 receptors, however, was most concentrated in the photoreceptor inner and outer segments and in the outer nuclear layer. The D2-specific agonist and antagonists, such as quinpirole, sulpiride, and eticlopride, competed for 3H-binding with high affinities; SCH-23390 and SKF-38393 were ineffective. The D2 receptors on the photoreceptors had a high affinity for clozapine but lower affinities for the modified benzamides. This is characteristic of a novel subtype of D2 receptors. Thus, D1 and D2 dopamine receptors are localized differentially in the rat retina to mediate different physiologic effects of dopamine.

Animals↗
PubMed1991

Guanine nucleotide-binding regulatory proteins in retinal pigment epithelial cells.

The expression of GTP-binding regulatory proteins (G proteins) in retinal pigment epithelial (RPE) cells was analyzed by RNA blot hybridization and cDNA amplification. Both adult and fetal human RPE cells contain mRNA for multiple G protein alpha subunits (G alpha) including Gs alpha, Gi-1 alpha, Gi-2 alpha, Gi-3 alpha, and Gz alpha (or Gx alpha), where Gs and Gi are proteins that stimulate or inhibit adenylyl cyclase, respectively, and Gz is a protein that may mediate pertussis toxin-insensitive events. Other G alpha-related mRNA transcripts were detected in fetal RPE cells by low-stringency hybridization to Gi-2 alpha and Gs alpha protein-coding cDNA probes. The diversity of G proteins in RPE cells was further studied by cDNA amplification with reverse transcriptase and the polymerase chain reaction. This approach revealed that, besides the above mentioned members of the G alpha gene family, at least two other G alpha subunits are expressed in RPE cells. Human retinal cDNA clones that encode one of the additional G alpha subunits were isolated and characterized. The results indicate that this G alpha subunit belongs to a separate subfamily of G proteins that may be insensitive to inhibition by pertussis toxin.

Amino Acid Sequence↗
PubMed1991

A clinical comparison of the Oculab Tono-Pen with the Goldmann applanation tonometer in eyes filled with silicone oil.

Intraocular pressure in 21 eyes filled with silicone oil was measured with two different instruments: the Oculab Tono-Pen and a Goldmann applanation tonometer mounted to a slit lamp biomicroscope. Intraocular pressure ranged from 2 mmHg to 28 mmHg, and the mean difference between readings obtained from the two instruments was 0.64, which was not statistically significant. These results suggest that the Oculab Tono-Pen is an effective instrument with which to measure intraocular pressure in silicone-filled eye.

Cataract Extraction↗
PubMed1986

Somatostatin binding sites in human and monkey brain: localization and characterization.

A radioiodinated analogue of somatostatin 28, 125I [Leu8,D-Trp22,Tyr25] SS-28, was used to localize and characterize somatostatin binding sites in both human and monkey brain. High-affinity binding sites (approximately 1 nM) were found in cerebral cortex. The highest binding was in cerebral cortex with intermediate binding found in hippocampus, striatum, and amygdala and low binding in hypothalamus and brainstem. There was a rough correlation between somatostatin receptor binding and concentrations of somatostatin-like immunoreactivity (SLI) in human brain. Somatostatin receptors were stable for up to 24 h in an animal model simulating human autopsy conditions and there was no correlation between postmortem interval and receptor binding in human brain. Pharmacologic characterization in human cortex showed that there was a correlation between the inhibition of receptor binding by somatostatin analogues and their known abilities to inhibit growth hormone secretion. These findings demonstrate that a highly specific membrane-associated receptor for somatostatin is present in both monkey and human brain. Examination of somatostatin receptor binding in Alzheimer's disease and Huntington's disease may improve understanding of the role of somatostatin in both these illnesses.

Animals↗
PubMed1985

Reduced numbers of somatostatin receptors in the cerebral cortex in Alzheimer's disease.

Somatostatin receptor concentrations were measured in patients with Alzheimer's disease and controls. In the frontal cortex (Brodmann areas 6, 9, and 10) and temporal cortex (Brodmann area 21), the concentrations of somatostatin in receptors in the patients were reduced to approximately 50 percent of control values. A 40 percent reduction was seen in the hippocampus, while no significant changes were found in the cingulate cortex, postcentral gyrus, temporal pole, and superior temporal gyrus. Scatchard analysis showed a reduction in receptor number rather than a change in affinity. Somatostatin-like immunoreactivity was significantly reduced in both the frontal and temporal cortex. Somatostatin-like immunoreactivity was linearly related to somatostatin-receptor binding in the cortices of Alzheimer's patients. These findings may reflect degeneration of postsynaptic neurons or cortical afferents in the patients' cerebral cortices. Alternatively, decreased somatostatin-like immunoreactivity in Alzheimer's disease might indicate increased release of somatostatin and down regulation of postsynaptic receptors.

Adult↗
PubMed1985

Two types of somatostatin receptors differentiated by cyclic somatostatin analogs.

Somatostatin receptors in rat brain, pituitary, and pancreas were labeled with two radioiodinated analogs of somatostatins 14 and 28. Two cyclic analogs of somatostatin, SMS201-995 and cyclo(Ala-Cys-Phe-D-Trp-Lys-Thr-Cys), showed biphasic displacement of binding to somatostatin receptors by these radioligands. In contrast, all other somatostatin analogs, including somatostatin-14, competed for the receptor sites with monophasic displacement of radioligand receptor binding. Thus two types of somatostatin receptors were identified. It was found that the pituitary and pancreas have predominantly one type of somatostatin receptor whereas the brain has both, and that different regions of the brain have various proportions of the two types. These findings suggest methods to characterize other types of somatostatin receptors subserving somatostatin's diverse physiological functions, including a potential role in cognitive function and extrapyramidal motor system control.

Animals↗
PubMed1985

[Salmonella osteomyelitis in sickle cell anemia].

Case report of a 28-year old black sickle cell anemia patient with salmonella osteomyelitis of the radius. Aside from sickle cell anemia patients this skeletal complication of enteric salmonellosis is an extreme rarity. Description of the typical roentgenological features including intracortical fissures and sequestration.

Adult↗
PubMed1981

[3H]doxepin interactions with histamine H1-receptors and other sites in guinea pig and rat brain homogenates.

[3H]Doxepin, a tricyclic antidepressant, binds to brain homogenates with two saturable components. The high affinity component, with a dissociation constant (KD) of 0.26 nM, is associated with histamine H1-receptors. This high affinity binding shows stereospecificity in that d-chlorpheniramine is 100 times more potent than the pharmacologically less active l-isomer. Its drug specificity and regional variation closely parallel those exhibited by [3H]mepyramine binding. The drug specificity of the low affinity component is distinct from that of histamine H1-receptors, with no stereospecificity for chlorpheniramine isomers. Furthermore, all the H1-histamine antagonists tested display micromolar potency at the low-affinity doxepin sites but nanomolar potency at the high-affinity doxepin sites associated with a physiological histamine H1-receptor. The drug specificity of the low affinity site does not correspond to that of any known neurotransmitter receptor. Tricyclic antidepressants display IC50 values of 30-600 nM for the inhibition of [3H]doxepin binding to the low-affinity component with most values in the 0.1-0.3 microM affinity range.

Animals↗
PubMed1981

Histidine decarboxylase. Purification from fetal rat liver, immunologic properties, and histochemical localization in brain and stomach.

Histidine decarboxylase from fetal rat liver was purified to near-homogeneity. The purified enzyme has a molecular weight of 210,000, and appears to contain two subunits with molecular weights of 145,000 and 66,000, respectively. The enzyme is inhibited by heavy metals such as Hg2+ and Zn2+ and sulfhydryl-reactive compounds such as 5,5'-dithiobis-2-nitrobenzoic acid. The enzyme is partially dependent on exogenous pyridoxal phosphate. Extensive dialysis results in 50% loss of enzyme activity which can be fully recovered by adding pyridoxal phosphate. Affinity of pyridoxal phosphate for the apoenzyme is 0.1 microM at pH 6.8. Antibody against purified histidine decarboxylase was raised in rabbits. The antibody has been employed in immunohistochemical studies to visualize histidine decarboxylase containing cells and neuronal processes in rat stomach and brain, respectively. Immunologic studies indicate that histidine decarboxylase from brain, gastric mucosa, and fetal rat liver share common antigenic properties.

Animals↗
PubMed1981

GABA receptors are increased in brains of alcoholics.

gamma-Aminobutyric acid (GABA) receptor binding was increased in postmortem brain samples of chronic alcoholic patients compared to control patients. Numbers of binding sites were augmented in alcoholic brain, with no change in affinity. Muscarinic cholinergic and benzodiazepine receptors did not differ between controls and alcoholic brains, while a modest reduction in beta-adrenergic receptors may have been related to postmortem receptor changes. The results suggest that GABAergic mechanisms might play a role in chronic alcoholism.

Adult↗
PubMed1981

Brain peptidase with a unique neuronal localization: the histochemical distribution of dipeptidyl-aminopeptidase II.

To assess whether specific peptidases regulate neuropeptide disposition, we have examined histochemically the localization of dipeptidyl-aminopeptidase II (DAP II). With beta-naphthylamide (beta-NA) substrates, this enzyme has a selectivity for lysyl-alanyl-beta-NA. DAP II staining is highly localized to specific neuronal populations with no staining over glia. Areas in the brain with high densities of DAP II staining include the mitral cells in the olfactory bulb, polymorphic cells in the hippocampus, the paraventricular nucleus of the hypothalamus, and the anterior dorsal thalamus, Purkinje cells, and deep nuclei in the cerebellum. Staining occurs in virtually all cell groups in the inferior colliculus, red nucleus, oculomotor nucleus, and mesencephalic nucleus of the trigeminal nerve, the stratum album of the superior colliculus, as well as most cells in the cochlear and superior olivary nuclei. DAP II localizations do not correlate fully with those on any known neuropeptide. Of the numerous peptides evaluated, only glucagon competes substantially for the DAP Ii substrate, reducing enzymatic activity by 50% at a 2 x 10(-5) M concentration.

Animals↗
PubMed1980

Histamine H1-receptors labeled in vivo: antidepressant and antihistamine interactions.

3H-Mepyramine labels specific histamine H1-receptors in brains of mice after intravenous injection. The potencies of H1-antihistamines in reducing 3H-mepyramine binding in vivo correspond to their pharmacological activities and show parallels with their affinities for 3H-mepyramine binding sites in isolated brain membranes. Several antidepressants are potent in competing for 3H-mepyramine binding in vivo as well as in vitro.

Animals↗
PubMed1980

Neurotransmitter receptor localizations: brain lesion induced alterations in benzodiazepine, GABA, beta-adrenergic and histamine H1-receptor binding.

Selective neuronal lesions have been utilized in efforts to localize binding sites in rat brain for beta-adrenergic, gamma-aminobutyric acid (GABA), histamine H1 and benzodiazepine receptors. The various receptors respond differentially to lesions both in extent of change and in time course. After kainate lesions in the corpus striatum, benzodiazepine receptors are depleted up to 45% at 45--78 days but are unaffected after 7 days. By contrast striatal GABA receptors are increased at 7 days but depleted at later times. Thus both striatal benzodiazepine and GABA receptors appear to be associated at least in part with intrinsic neurons. In the cerebellum both benzodiazepine and GABA receptors are reduced in kainate treated rats and in Nervous mice, mutants which lack Purkinje cells. The most pronounced dissimilarity between benzodiazepine and GABA receptors occurs in Weaver mice, which selectively lack granule cells and display a 60% reduction in GABA receptors but a 40% augmentation in benzodiazepine receptors. A major portion of cerebellar GABA receptors, therefore, appear to be localized to granule cells. Striatal beta-adrenergic receptors are reduced following intrastriatal kainate injections but are unaffected by cerebral cortex ablation, suggesting an association with intrinsic neurons but not with axon terminals of the corticostriate pathway. While intraventricular injections of 6-hydroxydopamine enhance [3H]dihydroalprenolol binding to beta-adrenergic receptors in the cerebral cortex and hippocampus, such binding is not augmented in the corpus striatum, brain stem, midbrain or thalamus-hypothalamus by this treatment. Moreover, medial forebrain bundle lesions, which destroy ascending adrenergic neurons, fail to alter cerebral cortical or striatal beta-adrenergic receptors. Thus denervation-elicited increases in beta-adrenergic receptors vary with brain region and the type of denervating lesion. Histamine H1-receptors are the most resistant of all to neuronal lesions. In the corpus striatum [3H]mepyramine binding is unaffected by cerebral cortex ablation, nigral injections of 6-hydroxydopamine or brain stem hemisection. In the hippocampus, medial forebrain bundle lesions, intrahippocampal kainate injection, and fimbria and fornix transection largely fail to alter [3H]mepyramine binding. Accordingly, a major portion of these receptors may be associated with nonneuronal elements such as glia or blood vessels.

Animals↗