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W Shain

Publications and source records attributed to W Shain.

At least 19 recordsLinked to original sources

Regulation of receptor-mediated shape change in astroglial cells.

Activation of adenylate cyclase in astroglial cells in culture results in a rapid change in cell shape that appears to occur by the active movement of cytoplasm from peripheral cell regions to the perinuclear space with processes being formed along regions that remain extended. Three series of experiments were designed to determine how shape change occurred. First, the Ca(2+)-dependency of shape change was determined by reducing intracellular Ca2+ concentrations to less than or equal to 50 nM or increasing intracellular Ca2+ concentrations to greater than or equal to 1 microM. Neither of these changes significantly affected the rate of receptor-mediated shape change. Second the role that longer-lived, acetylated microtubules play in receptor-mediated shape change was assessed by visualizing microtubules using a polyclonal antibody to brain 6S tubulin or a monoclonal antibody to oligomers of tubulin to monitor total tubulin distribution and a monoclonal antibody to acetylated tubulin to describe the distribution of these microtubules. Three-dimensional distribution of microtubules was observed by optical sectioning of cultures using a laser scanning confocal imaging system. The distribution of acetylated tubules in control cells was similar to that observed with the antibodies to tubulin. Following treatment with 100 nM isoproterenol to stimulate shape change, there was a dramatic redistribution of microtubules; however, the distribution of acetylated tubules was again similar to the total microtubules. Analysis of the optical sections recorded using the confocal attachment revealed that while control cells were relatively flat (cell height = 4 microns), the perinuclear region of isoproterenol-treated cells extended much higher above the substrate (cell height = 13 microns). Third, the role of microtubule assembly and disassembly were assessed using colchicine and taxol. Results from these experiments suggest that microtubule reassembly is necessary for receptor-mediated shape change. Control experiments indicated that colchicine or taxol treatment did not inhibit either cAMP synthesis or another cAMP-dependent process, receptor-mediated taurine release. Together these results indicate that receptor-mediated shape change in astroglial cells occurs by a Ca(2+)-independent mechanism that results in active movement of cytoplasm to the perinuclear region. This process is dependent on microtubule reassembly suggesting that shape change may occur by active movement of material along microtubules or by microtubule redistribution.

Acetylation

Electrophysiological properties of human oviduct smooth muscle cells in dissociated cell culture.

Intracellular recordings were made from human oviduct smooth muscle maintained in cell culture. Solitary cells isolated from one another and cells in contact with one another retained electrical properties of smooth muscle in vivo. Membrane potential of solitary cells and connected cells was -35 mV. Connected cells formed electrotonic junctions which transmitted current from one cell to another. This current spread was responsible for differences in input resistance and time constant in solitary cells, 66 Momega and 96 msec, compared to connected cells, 26 Momega and 56 msec. All cells expressed delayed rectification to depolarizing current pulses. Some cells generated action potentials spontaneously or in response to intracellular current pulses. Action potentials were abolished by cobalt or by EGTA. Slow wave potentials, 5 . 20 mV in amplitude, occurred continuously once every 15 to 45 seconds in connected cells.

Action Potentials

Characterization of an 11,000-dalton beta-bungarotoxin: binding and enzyme activity on rat brain synaptosomal membranes.

The binding and phospholipase A2 activity of an 11,000-dalton beta-bungarotoxin, isolated from Bungarus multicincutus venom, have been characterized using rat brain subcellular fractions as substrates. 125I-labeled beta-bungarotoxin binds rapidly (k = 0.14 min-1 and 0.11 min-1), saturably (Vmax = 130.1 +/- 5.0 fmoles/mg and 128.2 +/- 7.1) fmoles/mg), and with high affinity (apparent Kd = 0.8 +/- 0.1 nM and 0.7 +/- 0.1 nM) to rat brain mitochondria and synaptosomal membranes, respectively, but not to myelin. The binding to synaptosomal membranes is inhibited by divalent cations and by pretreatment with trypsin. The binding results suggest that the toxin binds to specific protein receptor sites on presynpatic membranes. The 11,000-dalton toxin rapidly hydrolyzes synaptosomal membrane phospholipids to lysophosphatides and manifests relative substrate specificity in the order phosphatidyl ethanolamine greater than phosphatidyl choline greater than phosphatidyl serine. These results indicate that the 11,000-dalton beta-bungarotoxin is a phospholipase A2 and can use presynaptic membrane phospholipids as substrates. The binding, phospholipase activity and other biological properties of the 11,000-dalton toxin are contrasted with those of the beta-bungarotoxin found in highest concentration in the venom (the 22,000-dalton beta-bungarotoxin), and the two toxins are shown to have qualitatively similar properties. Finally the results are shown to support the hypothesis that beta-bungarotoxins act in a two-step fashion to inhibit transmitter release: first, by binding to a protein receptor site on the presynatic membrane associated with Ca2+ entry, and second, by perturbing through enzymatic hydrolyses the phospholipid matrix of the membrane and thereby causing an increase in passive Ca2+ permeability.

Animals

Purification and biochemical characterization of an 11 000-dalton beta-bungarotoxin.

The chromatographic separation and biochemical characterization of a beta-bungarotoxin is described. This toxin is isolated as the most basic eluting protein of Bungarus multicinctus venom when separated by column chromatography on CM-Sephadex C-25. The protein migrated as a single band on pH 4.3 and sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. The molecular weight of this toxin was estimated to be 10 000 +/- 1000 by analytical sedimentation analysis. This value was consistent with the electrophoretic mobility of the toxin in SDS-polyacrylamide gels. The amino acid composition of this 11 000-dalton beta-bungarotoxin was similar to that of the 22 000-dalton beta-bungarotoxin previously reported (Lee et al. (1972) J. Chromatogr. 72, 71--82; Kelly, R.B. and Brown, III, F.R. (1974) J. Neurobiol. 5, 135--150; Kondo et al. (1978) J. Biochem. Tokyo 83, 91--99), suggesting that the 11 000-dalton toxin may be one of the polypeptide chains of the larger toxin. The 11 000-dalton beta-bungarotoxin was toxic to mice when injected intravenously. Animals that received lethal doses exhibited hyperexcitability followed by ataxia, convulsions, and death. The minimum lethal dose was 0.12 microgram/g body weight. This beta-bungarotoxin exhibited Ca2+-dependent phospholipase A activity comparable to that of the 22 000-dalton beta-bungarotoxin. The enzyme exhibited phospholipid substrate specificity in the rank order of phosphatidyl-choline, phosphatidylserine, phosphatidylethanolamine, and phosphatidyl-inositol. The enzyme activity was destroyed by boiling for 3 min at pH 8.6. In addition, an enzymatically inactive quantity of the 11 000-dalton toxin, equivalent to five times the minimum lethal dose of enzymatically active toxin, was not lethal when injected into mice. To test whether phospholipase A activity is responsible for lethality, bee venom phospholipase A2 was injected into mice at similar and greater concentrations with no toxic effect. Thus, while phospholipase A activity may be required for the lethal effect of the 11 000-dalton beta-bungarotoxin, the specificity of action of the toxin is not determined by its enzyme activity.

Amino Acids

Blockade of neuromuscular transmission by enzymatically active and inactive beta-bungarotoxin.

beta-Bungarotoxins have been shown to be presynaptic blockers of neuromuscular transmission. This paper reports experiments using the most positively charged beta-bungarotoxin that elutes from a CM-Sephadex C-25 column. The toxin is shown to be a single polypeptide with a molecular weight of approximately 11,000 and has phospholipase A2 activity. The application of the enzymatically active toxin to the frog sciatic nerve-sartorius muscle preparation results in an initial decrease in the average endplate potential amplitude followed by a temporary rebound in endplate potential amplitude, and finally a complete inhibition of endplate potentials. Similarly, minature endplate potential frequency is initially reduced upon toxin application but then increases dramatically. After the phospholipase A2 of the toxin is inactivated, treatment with the toxin results in only the initial decrease in transmitter release. There results suggest that this beta-bungarotoxin acts in two functionally separate steps: (i) by binding to a specific presynaptic site possibly associated with calcium entry, and (ii) by perturbing the presynaptic membrane by its enzyme action, which results in an increase and then a failure in transmitter release.

Action Potentials

Immune surveillance and tumors of the nervous system.

The theory of immune surveillance postulates that one function of the immune system is to eliminate small numbers of malignant cells that arise spontaneously within the organism. Although there has been a great deal of both clinical and experimental evidence in favor of thistheory as it applies to general oncology, the question of whether or not such a surveillance system would be effective for tumors arising within the nervous system has never been studied. The young of pregnant rats which had been exposed to the neurocarcinogen ethylnitrosourea (ENU) were divided into control, immunosuppressed, and immunoenhanced groups. These lifetime alterations of the immune system had no effect on the course of nervous system tumor fromation. We believe that the most likely explanation for our results is that the "immunological privilege" of the brain prevents the usual interaction of the neoplasm and the immune system from occurring.

Animals

Characterization of a depolarizing dopamine response in a vertebrate neuronal somatic cell hybrid.

The physiology and pharmacology of a depolarizing dopamine response was studied in the vertebrate neuronal somatic cell hybrid TCX11. The average resting membrane potential was -50 mV (S.D.=+/-7) with a membrane resistance of 40.5 mOhms (S.D.=+/-8) as determined from intracellular recordings. Depolarizing current pulses did not elicit an action potential. Cells displayed a linear current-voltage relationship when artificially depolarized up to +30 mV. Iontophoretically applied dopamine elicited a depolarizing response with a conductance increase and a reversal potential of -15 mV (S.D.=+/-4.7). Experiments altering medium ion concentrations demonstrated the conductance increase was to sodium and most likely potassium. The dopamine agonist ET495 (Piribedil) and the analogue epinine mimicked dopamine, while closely related biogenic amines, with the exception of noradrenaline, elicited no response. Apomorphine also elicited a depolarizing response but was much less efficacious than Piribedil. Noradrenaline was less potent than dopamine and appeared to act at the dopamine receptor. Methylation (3-methoxytyramine) or absence of the 3-hydroxy group (tyramine) of dopamine resulted in total loss of activity. The dopamine antagonists chlorpromazine, trifluoperazine, promazine, and bulbocapnine reversibly blocked the response to dopamine at medium concentrations less than 5 micronM. The adrenergic antagonist phentolamine blocked the response while phenoxybenzamine only reduced the response at higher concentrations. The acetylcholine antagonists alpha-bungarotoxin, hexamethonium, and scopolamine did not block the dopamine response. Both d-tubocurarine and atropine acted as antagonists. Collectively, these results demonstrate the presence of a receptor on a cultured cell line that is specific for dopamine, mediates a depolarizing and conductance increase response to dopamine, and displays the pharmacology most closely associated with dopamine receptors.

Acetylcholine

Neuronal properties of hybrid neuroblastoma X sympathetic ganglion cells.

Clonal mouse neuroblastoma cells without tyrosine 3-monooxygenase [EC 1.14.16.2; tyrosine hydroxylase; L-tyrosine, tetrahydropteridine:oxygen oxidoreductase (3-hydroxylating)] activity were fused with normal cells from embryonic mouse sympathetic ganglia. One of the 37 hybrid cell lines obtained possesses high tyrosine 3-monooxygenase activity and synthesizes dopamine. These cells also have excitable membranes and generate action potentials in response to electrical stimuli. Thus hybrid cells, generated by fusion of neuroblastoma cells with normal cells from the nervous system, can acquire neural properties not found with the parental neuroblastoma cells.

Action Potentials