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Biomedical subjects

S S Garber

Publications and source records attributed to S S Garber.

At least 19 recordsLinked to original sources

Monitoring Cl- movement in single cells exposed to hypotonic solution.

Self-referencing ion--selective electrodes (ISEs), made with Chloride Ionophore I-Cocktail A (Fluka), were positioned 1-3 microm from human embryonic kidney cells (tsA201a) and used to record chloride flux during a sustained hyposmotic challenge. The ISE response was close to Nernstian when comparing potentials (VN) measured in 100 and 10 mM NaCl (deltaVN = 57 +/- 2 mV), but was slightly greater than ideal when comparing 1 and 10 mM NaCl (deltaVN = 70 +/- 3 mV). The response was also linear in the presence of 1 mM glutamate, gluconate, or acetate, 10 microM tamoxifen, or 0.1, 1, or 10 mM HEPES at pH 7.0. The ISE was approximately 3 orders of magnitude more selective for Cl- over glutamate or gluconate but less than 2 orders of magnitude move selective for Clover bicarbonate, acetate, citrate or thiosulfate. As a result this ISE is best described as an anion sensor. The ISE was 'poisoned' by 50 microM 5-nitro-2-(3phenylpropyl-amino)-benzoic acid (NPPB), but not by tamoxifen. An outward anion efflux was recorded from cells challenged with hypotonic (250 +/- 5 mOsm) solution. The increase in efflux peaked 7-8 min before decreasing, consistent with regulatory volume decreases observed in separate experiments using a similar osmotic protocol. This anion efflux was blocked by 10 microM tamoxifen. These results establish the feasibility of using the modulation of electrochemical, anion-selective, electrodes to monitor anions and, in this case, chloride movement during volume regulatory events. The approach provides a real-time measure of anion movement during regulated volume decrease at the single-cell level.

Cell Line↗

Volume-dependent glutamate permeation depends on transmembrane ionic strength and extracellular Cl-.

Many mammalian cells regulate their volume by the osmotic movement of water directed by anion and cation flux. Ubiquitous volume-dependent anion currents permit cells to recover volume after swelling in response to a hypotonic environment. This study addressed competition between glutamate (Glu) and Cl(-) permeation in volume-activated anion currents in order to provide insight into the ionic requirements for volume regulation, volume-dependent anion channel activity and to the architecture of the channel pore. The effect of changing the intracellular molar fraction (MF) of Glu and Cl(-) on conductance and relative anion permeability was evaluated as a function of the extracellular permeant anion and/or the ionic strength. Relative permeability of Glu to Cl(-) was determined by measuring reversal potentials under defined ionic conditions. Under conditions with high (150 m M) or low (50 m M) ionic strength solutions on both sides of the membrane, Cl(-) was always more permeable than Glu. When a transmembrane ionic strength gradient (150 m M extracellular: 50 m M intracellular) was set to drive water into the cell, and in the presence of extracellular Cl(-), Glu became up to 16-fold more permeable than Cl(-). Replacement of extracellular Cl(-) with Glu abolished this effect. These results indicate that it is possible for Glu to move into the extracellular environment during volume-regulatory events and they support the emerging role of glutamate as a modulator of anion channel activity.

Cell Line↗

Drug design with a new transition state analog of the hydrated carbonyl: silicon-based inhibitors of the HIV protease.

BACKGROUND: Silicon is the element most similar to carbon, and bioactive organosilanes have therefore been of longstanding interest. Design of bioactive organosilanes has often involved a systematic replacement of a bioactive molecule's stable carbon atoms with silicon. Silanediols, which are best known as unstable precursors of the robust and ubiquitous silicone polymers, have the potential to mimic an unstable carbon, the hydrated carbonyl. As a bioisostere of the tetrahedral intermediate of amide hydrolysis, a silanediol could act as a transition state analog inhibitor of protease enzymes. RESULTS: Silanediol analogs of a carbinol-based inhibitor of the HIV protease were prepared as single enantiomers, with up to six stereogenic centers. As inhibitors of this aspartic protease, the silanediols were nearly equivalent to both their carbinol analogs and indinavir, a current treatment for AIDS, with low nanomolar K(i) values. IC(90) data from a cell culture assay mirrored the K(i) data, demonstrating that the silanediols can also cross cell membranes and deliver their antiviral effects. CONCLUSIONS: In their first evaluation as inhibitors of an aspartic protease, silanediol peptidomimetics have been found to be nearly as potent as currently available pharmaceutical agents, in enzyme and cell protection assays. These neutral, cell-permeable transition state analogs therefore provide a novel foundation for the design of therapeutic agents.

Cells, Cultured↗

Modulation of volume regulated anion current by I(Cln).

I(Cln), a cytosolic protein associated with a nucleotide-sensitive chloride current, may be involved in the regulation of a volume-regulated anion current (VRAC) associated with hypotonic cell swelling. We have determined the nucleic acid sequences of I(Cln) from human tsA201a, colonic (T84) and myeloma (RPMI 8826) cell lines. The amino acid sequences are highly homologous (>/=99%) to each other but less homologous to I(Cln) protein from other species. Using the whole-cell patch clamp technique, we examined the effect of I(Cln) protein expression levels on VRAC properties during a hyposmotic challenge. Overexpression of T84 or RPMI 8226-derived I(Cln) protein in tsA201a cells results in a more than 9-fold increase in the rate of VRAC activation over control values, while having no effect on VRAC inactivation properties. Underexpression of endogenous I(Cln) protein in tsA201a cells using antisense oligonucleotides results in a more than 180-fold decrease in VRAC activation rate as compared to control values. These results indicate that I(Cln) protein expression modulates VRAC activation but not inactivation.

Amino Acid Sequence↗

Anion competition for a volume-regulated current.

We have examined whether the anionic amino acids, glutamate and aspartate, permeate through the same volume-regulated conductance permeant to Cl- ions. Cell swelling was initiated in response to establishing a whole-cell configuration in the presence of a hyposmotic gradient. Volume-regulated anion currents carried by Cl-, glutamate, or aspartate developed with similar time courses and showed similar voltage-dependent inactivation. Permeability ratios (Paa/PCl) calculated from measured reversal potentials were dependent on the mole fraction ratio (MFR) of the permeant anions ([aa]/([aa] + [Cl-])). MFR was varied from 0.00 to 0.97. As the fraction of amino acid increased, Paa/PCl decreased. Current amplitude was similarly dependent on MFR. These results show that the permeation of anionic amino acids and that of Cl- ions are not independent of each other, indicating that the ion channel underlying the volume-regulated conductance can be occupied by more than one ion at a time. Application of Eyring rate theory indicated that the major barrier to Cl- ion permeation is at the intracellular side of the membrane, and that the major barrier to amino acid permeation is at the extracellular side of the membrane. The interactions between these permeant ions may have a physiological modulatory role in volume regulation through a volume-regulated anion conductance.

Anions↗

Cyclic urea amides: HIV-1 protease inhibitors with low nanomolar potency against both wild type and protease inhibitor resistant mutants of HIV.

Cyclic urea amides, a novel series of HIV-1 protease (HIV PR) inhibitors, have increased activity against drug-resistant mutants of the HIV PR. The design strategy for these inhibitors is based on the hypotheses that (i) the hydrogen-bonding interactions between the inhibitor and the protease backbone will remain constant for wild-type and mutant enzymes and (ii) inhibitors which are capable of forming many nonbonded interactions, distributed throughout the active site, will experience a lower percent change in binding energy as a result of mutation in the target enzyme than those that form fewer interactions by partial occupation of the active site. The cyclic urea amide, SD146, forms 14 hydrogen bonds and 191 van der Waals contacts to HIV PR. SD146 is a very potent antiviral agent (IC90 = 5.1 nM) against wild-type HIV and maintains the same or improved level of high potency against a range of mutant strains of HIV with resistance to a wide variety of HIV protease inhibitors.

Amides↗

cAMP promotes gap junctional coupling in T84 cells.

The effect of intracellular adenosine 3',5'-cyclic monophosphate (cAMP) on dye and electrical coupling was studied in T84 cells, a cell line often used as a model for epithelial cell fluid secretion. Injections of lucifer yellow (LY) into single cells within a cluster of control cells resulted in LY localization to 1.3 +/- 0.2 (mean +/- SE) cells within a cluster. Twenty-six percent of control T84 cell pairs were electrically coupled as assayed by the dual patch-clamp technique. Treatment of cells with agents that either increase intracellular cAMP and/or activate protein kinase A (PKA) increased dye localization to 3.8 +/- 0.6 cells and the proportion of electrically coupled cell pairs to 65%. No electrical coupling was observed in the presence of the Rp diastereomer of adenosine-3',5'-cyclic monophosphothioate (Rp-cAMPS), a PKA antagonist. Excess of Rp-cAMPS prevented cell coupling elicited by 20 microM of the Sp diastereomer of adenosine-3',5'-cyclic monophosphothioate. Expression of connexin 32 mRNA, but not of connexins 26, 43, or 45, was detected by reverse transcription-polymerase chain reaction. These results suggest that communication between T84 cells is modulated by PKA, providing a mechanism for regulating multicellular activity, such as fluid secretion.

Cell Line↗

Modulation of a volume-regulated chloride current by F-actin.

We have examined whether F-actin integrity is involved in activation of a volume-regulated Cl- current (VRChlC) in B-lymphocytes. VRChlC activation was initiated in response to establishing a whole cell recording in the presence of a hyposmotic gradient. Parallel confocal microscopy experiments using Rhodamine-Phalloidin (R-P) as a specific marker of F-actin showed that the submembrane actin ring is reversibly disrupted in response to an hyposmotic gradient. Disruptions of cortical F-actin integrity by 50 microM cytochalasin B (CB) does not trigger activation of VRChlC under isosmotic conditions or potentiate the rate of activation when the osmolarity of the extracellular solution was decreased by 75%. However, incubation with CB increased the rate of VRChlC activation in response to a 90% hyposmotic gradient. Phalloidin, a stabilizer of F-actin, decreases the rate of VRChlC activation in response to a 90% gradient, but has no effect in response to a 75% gradient. These observations suggest that disassembly of cortical F-actin is not critical for VRChlC activation in B-lymphocytes. The integrity of cortical F-actin, however, can exert a modulatory effect on the rate of VRChlC activation in the presence of a hyposmotic gradient.

Actins↗

Voltage-dependent inactivation of volume-regulated Cl- current in human T84 colonic and B-cell myeloma cell lines.

The voltage-dependent inactivation of a volume-regulated Cl- current (VRChlC) in an epithelial (T84), and a B cell myeloma (RPMI-8226) cell lines were compared. Both cell types exhibited similar time and voltage-dependent current inactivation when recorded using standard whole cell patch technique, with a NaCl external solution that was approximately 90 mOsm hypotonic to the Cs-Glutamate internal solution. The time course of voltage-dependent current inactivation was fit by the sum of a slow, dominant voltage-dependent and a faster voltage-independent components. Recovery from inactivation was approximated by a single exponential process and was dependent on the recovery voltage. The major difference was that the voltage-dependent current inactivation in myeloma cells was shifted to a approximately 30mV more depolarized value than that in T84 cells although the effective charge movement of inactivation was similar. These results indicate that the macroscopic volume-regulated Cl- current in these two cell lines is functionally similar.

B-Lymphocytes↗

Membrane chloride conductance and capacitance in Jurkat T lymphocytes during osmotic swelling.

Video microscopy and whole-cell patch-clamp recording were used to monitor changes in relative cell volume (V/Vo), chloride conductance (gCl), and membrane capacitance (Cm) during osmotically induced swelling in Jurkat T lymphocytes. Cellular swelling was initiated with hyperosmotic pipette solutions. Simultaneous evaluation of V/Vo and gCl revealed a 59-s delay between the inception of swelling and the activation of outwardly rectifying, ATP-dependent Cl- channels. Following the delay, increases in V/Vo and gCl progressed in parallel. In contrast, Cm, a measure of cell surface area, fell gradually at a rate of approximately 150 fF/min after whole-cell access was achieved. The decline in Cm lasted 200 s and was followed by a rapid rise (approximately 750 fF/min). The rise in Cm coincided with a variable increase in "leak" current, gCl increased at a slower rate and reached lower peak values in experiments performed without ATP; ATP had no effect on the biphasic Cm time course. The temporal separation of conductance and capacitance during swelling suggests that gCl and Cm vary independently, supporting the hypothesis that a large portion, if not all, of the whole-cell Cl- conductance activated during swelling is provided by volume-sensitive Cl- channels preexisting in the plasma membrane.

Cell Line↗

Outwardly rectifying chloride channels in lymphocytes.

Outwardly rectifying Cl- channels in cultured human Jurkat T-lymphocytes were activated by excising a patch of membrane using the inside-out (i/o) patch-clamp configuration and holding at depolarized voltages for prolonged periods of time (1-6 min at +80 mV, 20 degrees C). The single-channel current at +80 mV was 4.5 +/- 0.3 pA and at -80 mV, it was 1.0 +/- 0.4 pA. After activation, the probability of being open (Po) for the lymphocyte channel was voltage independent. Activation of the Cl- channel in lymphocytes was temperature dependent. Nineteen percent of i/o recordings from lymphocytes made at 20 degrees C exhibited Cl- channel activity. In contrast, 49% of recordings made at 30 degrees C showed channel activity. The number of channels in an active patch was not significantly different at the two temperatures. Channel activation in excised, depolarized patches also occurred 20-fold faster at 30 degrees C than at 20 degrees C. There was no marked change in the single-channel conductance at 30 degrees C. Open-channel conductance was blocked by 200 microM indanyloxyacetic acid (IAA) or 1 mM SITS when applied to the intracellular side of the patch. The characteristics of this channel are similar to epithelial outwardly rectifying Cl- channels thought to be involved in fluid secretion.

4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfo↗

Interaction of forskolin with voltage-gated K+ channels in PC12 cells.

Forskolin (FSK) directly blocks a distinct class of voltage-dependent K+ channels in pheochromocytoma cells. We have studied the biophysical mechanism of FSK action on these channels. The mean open duration decreased linearly with [FSK], indicating that a single molecule of FSK interacts with a single open K+ channel. FSK did not alter the voltage dependence of activation or the latency to first opening. Whole-cell currents in the presence of FSK did not show a rising phase in tail currents, suggesting that FSK-bound channels can close. We used a kinetic scheme in which FSK binds preferentially to the open state of the channel to describe its interaction with the K+ channel. This scheme is analogous to the modulated receptor hypothesis used to describe the interaction of local anesthetics with voltage-dependent Na+ channels.

Adrenal Gland Neoplasms↗

Properties of ShB A-type potassium channels expressed in Shaker mutant Drosophila by germline transformation.

We have used P element-mediated germline transformation to express ShB channels in Shaker mutant Drosophila and have examined their properties by patch-clamp of embryonic myotubes. The transformed ShB cDNA was placed under the transcriptional control of a heat shock promoter (hsp70). Northern blots revealed that transformed DNA is efficiently transcribed in response to heat shock. Cultured myotubes from the transformants produced large A-type potassium currents in response to heat shock. Although qualitatively similar to native Shaker A-currents in wild-type myotubes, transformant A-current inactivates more rapidly and recovers from inactivation more rapidly, similar to ShB channels expressed in Xenopus oocytes. Unlike the channels in oocytes, however, the transformant A-current is insensitive to 50 nM charybdotoxin.

Animals↗

Regulation of ionic currents in pheochromocytoma cells by nerve growth factor and dexamethasone.

Growth factors and hormones induce differentiation of clonal pheochromocytoma (PC12) cells, which are derived from rat adrenal medulla chromaffin cells. On application of nerve growth factor (NGF), PC12 cells extend neurites and express properties characteristic of autonomic ganglion cells. In contrast, incubation of PC12 cells with a corticosteroid, dexamethasone (DEX), does not induce neurite formation but causes an increase in tyrosine hydroxylase activity, suggesting that the cells become chromaffin cell-like. The ability of NGF and DEX to regulate ionic currents has been less well studied. Therefore, we examined how long-term NGF and DEX treatments affected voltage-dependent Na, Ca, and K currents in PC12 cells. Voltage-dependent Na currents were observed only in a small fraction of the PC12 cells in the absence of NGF or DEX. Virtually all NGF-treated cells expressed Na currents within 7 d. DEX increased the number of cells expressing voltage-dependent Na current slowly over 3 weeks, but, unlike NGF, DEX did not change Na current density. Both NGF and DEX also affected the expression of voltage-dependent Ca currents. Most of the untreated cells had only sustained, high-threshold voltage-dependent Ca currents. Chronic application of NGF or DEX increased the fractions of the cells that showed transient, low-threshold T-type Ca currents in addition to the high-threshold currents. The T-type Ca current density, however, increased significantly only in NGF-treated cells. Neither DEX nor NGF affected the voltage-dependent K currents. These results suggest that the expression of voltage-dependent Na and Ca currents are differentially regulated by NGF and DEX. The distinction between treated and untreated cells decreased after 3 weeks in culture as older untreated cells showed increases in the fraction of cells expressing both Na and low-threshold Ca currents. A PC12 subline selected for adherence to uncoated plastic also showed increased fraction of cells expressing these currents, suggesting that interactions with substrate may also influence ionic current expression.

Adrenal Gland Neoplasms↗

Effect of forskolin on voltage-gated K+ channels is independent of adenylate cyclase activation.

Forskolin is commonly used to stimulate adenylate cyclase in the study of modulation of ion channels and other proteins by adenosine 3',5'-monophosphate (cAMP)-dependent second messenger systems. In addition to its action on adenylate cyclase, forskolin directly alters the gating of a single class of voltage-dependent potassium channels from a clonal pheochromocytoma (PC12) cell line. This alteration occurred in isolated cell-free patches independent of soluble cytoplasmic enzymes. The effect of forskolin was distinct from those of other agents that raise intracellular cAMP levels. The 1,9-dideoxy derivative of forskolin, which is unable to activate the cyclase, was also effective in altering the potassium channel activity. This direct action of forskolin can lead to misinterpretation of results in experiments in which forskolin is assumed to selectively activate adenylate cyclase.

1-Methyl-3-isobutylxanthine↗

Symmetry and asymmetry of permeation through toxin-modified Na+ channels.

Single Na+ channels from rat skeletal muscle were inserted into planar lipid bilayers in the presence of either 200 nM batrachotoxin (BTX) or 50 microM veratridine (VT). These toxins, in addition to their ability to shift inactivation of voltage-gated Na+ channels, may be used as probes of ion conduction in these channels. Channels modified by either of the toxins have qualitatively similar selectivity for the alkali cations (Na+ approximately Li+ greater than K+ greater than Rb+ greater than Cs+). Biionic reversal potentials, for example, were concentration independent for all ions studied. Na+/K+ and Na+/Rb+ reversal potentials, however, were dependent on the orientation of the ionic species with respect to the intra- or extracellular face of the channel, whereas Na+/Li+ biionic reversal potentials were not orientation dependent. A simple, four-barrier, three-well, single-ion occupancy model was used to generate current-voltage relationships similar to those observed in symmetrical solutions of Na, K, or Li ions. The barrier profiles for Na and Li ions were symmetric, whereas that for K ions was asymmetric. This suggests the barrier to ion permeation for K ions may be different than that for Na and Li ions. With this model, these hypothetical energy barrier profiles could predict the orientation-dependent reversal potentials observed for Na+/K+ and Na+/Rb+. The energy barrier profiles, however, were not capable of describing biionic Na/Li ion permeation. Together these results support the hypothesis that Na ions have a different rate determining step for ion permeation than that of K and Rb ions.

Animals↗

Single Na+ channels activated by veratridine and batrachotoxin.

Voltage-sensitive Na+ channels from rat skeletal muscle plasma membrane vesicles were inserted into planar lipid bilayers in the presence of either of the alkaloid toxins veratridine (VT) or batrachotoxin (BTX). Both of these toxins are known to cause persistent activation of Na+ channels. With BTX as the channel activator, single channels remain open nearly all the time. Channels activated with VT open and close on a time scale of 1-10 s. Increasing the VT concentration enhances the probability of channel opening, primarily by increasing the rate constant of opening. The kinetics and voltage dependence of channel block by 21-sulfo-11-alpha-hydroxysaxitoxin are identical for VT and BTX, as is the ionic selectivity sequence determined by bi-ionic reversal potential (Na+ approximately Li+ greater than K+ greater than Rb+ greater than Cs+). However, there are striking quantitative differences in open channel conduction for channels in the presence of the two activators. Under symmetrical solution conditions, the single channel conductance for Na+ is about twice as high with BTX as with VT. Furthermore, the symmetrical solution single channel conductances show a different selectivity for BTX (Na+ greater than Li+ greater than K+) than for VT (Na+ greater than K+ greater than Li+). Open channel current-voltage curves in symmetrical Na+ and Li+ are roughly linear, while those in symmetrical K+ are inwardly rectifying. Na+ currents are blocked asymmetrically by K+ with both BTX and VT, but the voltage dependence of K+ block is stronger with BTX than with VT. The results show that the alkaloid neurotoxins not only alter the gating process of the Na+ channel, but also affect the structure of the open channel. We further conclude that the rate-determining step for conduction by Na+ does not occur at the channel's "selectivity filter," where poorly permeating ions like K+ are excluded.

Animals↗