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PubMed1976

Carrier-mediated sodium-dependent and calcium-dependent calcium efflux from pinched-off presynaptic nerve terminals (synaptosomes) in vitro.

The influence of external cations on 45Ca2+ efflux from Ca2+ loaded synaptosomes has been examined. The synaptosomes were pre-loaded with 45Ca2+ by incubating the suspensions in potassium-rich media for 2 min. The suspensions were then diluted into "efflux" media containing a "normal" (5mM) K+ concentration; the content of Na+ and Ca2+ was varied, as noted below. Efflux of 45Ca2+ was measured for a 2-min period (except for "zero-time" samples), and was terminated by filtering the suspensions on 0.3 mum cellulose acetate filters. 45Ca2+ retained on the filters was determined by liquid scintillation spectroscopy. The difference between the 45Ca2+ in the "zero-time" samples (="Ca2+ load") and in the samples incubated for 2 min was taken as the 45Ca2+ efflux. 45Ca2+ loss into Ca2+ -free efflux media containing ethyleneglycol-bis-(beta-aminoethylether)-N,N'-tetraacetic acid (EGTA) was markedly influenced by the Na+ concentration: nearly 80% of the 45Ca2+ was lost from the synaptosomes if the media contained 132 mM Na+, but only about 7% was lost in 2 min if 97% of the Na+ was replaced mol-for-mol by choline. In media containing 1.2 mM Ca2+ and 132 mM Na+, the 45Ca2+ uptake by synaptosomes previously loaded with 40Ca2+ was significantly less than 45Ca2+ loss from synaptosomes loaded with 45Ca2+. Thus there was a net efflux of Ca2+ from the Ca2+ -loaded synaptosomes; this efflux was, presumably, Na+ dependent. In media containing 1.2 mM 40Ca2+ and only 4 mM Na+, the 45Ca2+ efflux from 45Ca2+ -loaded synaptosomes was significantly greater if most of the external Na+ (128 mM) was replaced isomotically by Li+ rather than by choline, guanidine or glucose. This observation may be evidence for a Ca2+ -Ca2+ exchange which is promoted by Li+. Both the Na+ -dependent and the Ca2+ -dependent Ca2+ effluxes were inhibited by Mn2+. The data are consistent with a Ca2+ carrier mechanism which can extrude Ca2+ in exchange for Na+ or for Ca2+, the latter being activated by Li+. These properties bear a striking resemblance to those of a Ca2+ efflux mechanism which has been characterized in squid axons. This mechanism may there fore have evolved fairly early on in the history of the animal kingdom.

Animals↗
PubMed1980

Calcium buffering in presynaptic nerve terminals. Free calcium levels measured with arsenazo III.

The particulate fraction from osmotically shocked synaptosomes ('synaptosomal membrances') sequesters Ca when incubated with ATP]containing solutions. This net accumulation of Ca can reduce the free [Ca2+] of the bathing medium to sub-micromolar levels (measured with arsenazo III). Two distinct types of Ca sequestration site are responsible for the Ca2+ buffering. One site, presumed to be smooth endoplasmic reticulum, operates at low [Ca2+] (less than 1 microM), and has a relatively small capacity. Ca sequestration at this site is prevented by the Ca2+ ionophore, A-23187, but not by mitochondrial poisons. The secone (mitochondrial) site, in contrast, is blocked by the mitochondrial uncoupler carbonyl cyanide p-trifluoromethoxyphenylhydrazone, and oligomycin. Since the intraterminal organelles can buffer [Ca2+] to about 0.3-0.5 microM, this may be an upper limit to the normal resting level of [Ca2+]i in nerve terminals. In the steady state, total cell Ca and [Ca2+]i will be governed principally be Ca transport mechanisms in the plasmalemma; the intracellular organelle transport systems then operate in equilibrium with this [Ca2+]. During activity, however, Ca rapidly enters the terminals and [Ca2+]i rises. The intracellular buffering mechanisms then come into play and help to return [Ca2+]i toward the resting level; the non-mitochondrial Ca sequestration mechanism probably plays the major role in this Ca buffering.

Adenosine Triphosphate↗
PubMed1989

Role of ion channels and intraterminal calcium homeostasis in the action of deltamethrin at presynaptic nerve terminals.

Using a continuous perfusion system, synaptosomes prepared from rat brain released [3H]norepinephrine in a Ca2+-dependent manner when pulse depolarized by briefly elevating external potassium concentrations. Tetrodotoxin (10(-7) M), a sodium channel blocker, inhibited 48% of this pulsed release, and D595 (10(-5) M), a phenethylamine-type calcium channel blocker, inhibited 21%. In combination, these two specific ion channel antagonists appear to function independently of each other in an additive fashion. Addition of deltamethrin to this preparation resulted in an enhanced release of [3H]norepinephrine which occurred in a biphasic fashion. At 10(-7) M, deltamethrin produced a 42% enhancement in the first or initial peak of [3H]norepinephrine release and a 100% enhancement in the second or tailing peak. Addition of deltamethrin to tetrodotoxin-pretreated synaptosomes resulted in a net 37% enhancement of the initial peak release and a net increase of 277% in the tailing peak. Addition of deltamethrin to D595-pretreated synaptosomes produced no significant effect on enhanced [3H]norepinephrine release from either peak. Since tetrodotoxin is a specific sodium channel blocker, deltamethrin may be enhancing [3H]norepinephrine release by increasing the uptake of Ca2 via other voltage-gated channels (e.g. calcium) or exchange mechanisms in addition to its action at voltage-gated sodium channels. To determine whether deltamethrin may also have an effect on intraterminal Ca2+ homeostasis, external Ca2+ was replaced with Ba2+ and synaptosomes were depolarized with pentylenetetrazole (PTZ). At 10(-5) M, deltamethrin produced a 66% increase in neurotransmitter release over that produced by PTZ alone. An estimated EC50 value of deltamethrin for PTZ-induced release was calculated to be 2.4 x 10(-10) M.

Animals↗
PubMed1982

Transmitter release by graded local depolarization of presynaptic nerve terminals at the crayfish neuromuscular junction.

Synaptic currents were recorded at single nerve terminals on the crayfish opener muscle by means of a patch-clamp electrode. Current pulses depolarizing the terminal were applied through the electrode which caused release of transmitter quanta. Such 'pulse-elicited excitatory postsynaptic currents' (pEPSCs) were not affected by the presence of tetrodotoxin, and no antidromic action potentials were detected in the motor nerve fiber after terminal depolarizations eliciting maximal pEPSCs. The amplitude of pEPSCs was graded in a wide range depending on amplitude and duration of the pulse, with different quantitative relationships for 'fast' and 'slow' synapses. It appears that these nerve terminals are inexcitable and are depolarized by the electronic spread of the motor nerve action potential.

Animals↗
PubMed1983

Evidence that transmitter can be released from regions of the nerve cell other than presynaptic axon terminal: axonal release of acetylcholine without modulation.

Release of acetylcholine from isolated preganglionic axons of sympathetic nerve trunk (cervical preganglionic sympathetic branch) of the cat was studied. In response to depolarization (KCl, 48.4 mM) acetylcholine was released into the eserinized Krebs solution. This release was shown to be dependent on extracellular Ca2+. Electrical stimulation (1 Hz) enhanced the release of acetylcholine from the isolated axonal preparation. The release by stimulation proved to be tetrodotoxin-sensitive and Ca2+-dependent. Evidence has been obtained that the acetylcholine released from sympathetic nerve trunks originates from the axon and not from Schwann cells: 5 days after section of the nerve, there was no release in response to stimulation. The release of acetylcholine from the axon is unlike that from axon terminals in that the rate of release cannot be enhanced by the inhibition of Na, K-adenosine 5'-triphosphatase (ouabain 2 X 10(-5) M) and cannot be modulated by noradrenaline (10(-6) M) or by morphine. Furthermore, although isolated nerve trunks took up [3H]choline by a hemicholinium-sensitive process, no radioactivity could be released upon electrical stimulation. It is suggested that the release of acetylcholine is not confined to axon terminals, but that it can be non-synaptically released by depolarization from axons provided Ca2+ is present.

Acetylcholine↗
PubMed1992

[18F]fluoro-beta-fluoromethylene-m-tyrosine analogs, potential PET agents for presynaptic dopamine terminals: synthesis and spectroscopic characterization.

18F-labeled (E)-beta-fluoromethylene-DL-m-tyrosine (FMMT) was prepared by the direct reaction of FMMT with [18F]acetylhypofluorite (AcOF) resulting into three product isomers. Extensive 1H, 13C and 19F-NMR spectroscopic analysis identify these products to be 2-fluoro, 6-fluoro-FMMT and 2,6-difluoro-FMMT. The HPLC isolated radiochemical EOB yields of these products were 22, 25 and 14%, respectively, based on starting [18F]AcOF. The specific activity at the end of a synthesis time of an hour was ca 200 mCi/mmol. With the possible advantage of "metabolic trapping" in dopamine nerve terminals via covalent binding to MAO and reduced metabolite formation, [18F]F-FMMT may potentially be the optimal PET tracer for CNS dopamine nerve terminals.

Brain↗
PubMed1994

Presynaptic control of neurones in pattern-generating networks.

Recent studies have revealed presynaptic influences on neurones that participate in rhythmic motor patterns. Although there is still little direct information about the effects of these inputs at presynaptic terminals, their functional consequences are being unraveled. These presynaptic influences gate sensory input to pattern-generating networks and locally alter the synaptic strength and/or the activity pattern of network neurones.

Animals↗
PubMed2000

Zinc-enriched (ZEN) terminals in mouse olfactory bulb.

The present study was designed to localize zinc-enriched (ZEN) terminals in mouse olfactory bulb by means of ZnT3 immunocytochemistry (ICC) and zinc autometallography (AMG). The immunocytochemical staining of ZnT3 was closely correlated with the AMG pattern. ZEN terminals were defined as terminals showing both ZnT3 immunoreactivities and AMG granules. At the light microscopic level, dense staining patterns for ZnT3 immunoreactivity were seen in the granule cell layer and the olfactory glomerular layer. At the ultrastructural level, ZEN terminals were restricted to presynaptic terminals with single or multiple postsynaptic thickenings. The postsynaptic profiles contacting ZEN terminals appeared to be dendrites or somata of granule cells in the granule cell layer and periglomerular cells and mitral/tufted (M/T) cells in the olfactory glomerular layer. This suggests that two main sources of ZEN terminals are present in mouse olfactory bulb: (1) centrifugal fibres making asymmetrical synapses with granule cells and periglomerular cells, and (2) olfactory receptor terminals contacting dendritic profiles of M/T cells or periglomerular cells. The close correlation between ZEN terminals and the glutamatergic system is discussed.

Animals↗
PubMed1978

Calcium buffering in presynaptic nerve terminals. II. Kinetic properties of the nonmitochondrial Ca sequestration mechanism.

The kinetic properties of the nonmitochondrial ATP-dependent Ca sequestering mechanism in disrupted nerve terminal (synaptosome) preparations have been investigated with radioactive tracer techniques; all solutions contained DNP, NaN3, and oligomycin, to block mitochondrial Ca uptake. The apparent half-saturation constant, KCa, for the nonmitochondrial Ca uptake is approximately 0.4 micrometer Ca; the Hill coefficient is approximately 1.6. Mg is also required for the Ca uptake, and the apparent KMg is approximately 80 micrometer. ATP and deoxy-ATP, but not CTP, GTP, ITP, UTP, ADP, or cyclic AMP, promote Ca uptake; the KATP, is approximately 10 micrometer. ATP analogs with blocked gamma-phosphate groups are unable to replace ATP. Particulate fractions from the disrupted synaptosomes possess Ca-dependent ATPase activity in the presence of Mg; the apparent KCa for this activity is 0.4--0.8 micrometer Ca, and the Hill coefficient is approximately 1.6. The Ca uptake and ATPase kinetic data suggest that the hydrolysis of 1 ATP may energize the transport of two Ca2+ ions into the storage vesicles. The second part of the article concerns the intraterminal distribution of Ca in "intact" terminals. When the terminals are disrupted after 45Ca loading, about one-half of the 45Ca is retained in the particulate material; some of this Ca, presumably stored in mitochondria, is released by the uncoupler, FCCP. Some of the 45Ca is released by A-23187, but not by FCCP; this fraction may be Ca stored in the nonmitochondrial sites described above. The proportion of 45Ca stored in the nonmitochondrial sites is increased when the Ca load is reduced or when the mitochondria are blocked with ruthenium red. These data indicate that the nonmitochondrial Ca storage sites are involved in intraterminal Ca buffering; they may play an important role in synaptic facilitation and post-tetanic potentiation, which result from Ca retention after neural activity.

Adenosine Triphosphate↗
PubMed1980

Sodium channels in presynaptic nerve terminals. Regulation by neurotoxins.

Regulation of Na+ channels by neurotoxins has been studied in pinched-off nerve endings (synaptosomes) from rat brain. Activation of Na+ channels by the steroid batrachotoxin and by the alkaloid veratridine resulted in an increase in the rate of influx of 22Na into the synaptosomes. In the presence of 145 mM Na+, these agents also depolarized the synaptosomes, as indicated by increased fluorescence in the presence of a voltage-sensitive oxacarbocyanine dye [diO-C5(3)]. Polypeptide neurotoxins from the scorpion Leiurus quinquestriatus and from the sea anemone Anthopleura xanthogrammica potentiated the stimulatory effects of batrachotoxin and veratridine on the influx of 22Na into synaptosomes. Saxitoxin and tetrodotoxin blocked the stimulatory effects of batrachotoxin and veratridine, both in the presence and absence of the polypeptide toxins, but did not affect control 22Na influx or resting membrane potential. A three-state model for Na+ channel operation can account for the effects of these neurotoxins on Na+ channels as determined both by Na+ flux measurements in vitro and by electrophysiological experiments in intact nerve and muscle.

Animals↗
PubMed1990

The effects of (-)-daurisoline on Ca2+ influx in presynaptic nerve terminals.

1. The effects of (-)-daurisoline on 45Ca2+ uptake and [3H]-gamma-aminobutyric acid ([3H]-GABA) release from synaptosomes of rat cerebral cortex and on contractile activity of rat aorta were examined. 2. Application of (-)-daurisoline (1-100 microM) produced concentration-related inhibition of high K(+)-stimulated 45Ca2+ uptake and [3H]-GABA release (IC50 = 7.7 +/- 0.9 microM and 10.0 +/- 1.5 microM, respectively) in synaptosomes but verapamil was only weakly active. 3. Neither (-)-daurisoline (100 microM) nor verapamil (100 microM) modified 45Ca2+ uptake in control medium (5 mM K+, resting uptake) and [3H]-GABA release in Ca-free medium (45 mM K+ basal release). 4. High K+ and noradrenaline-evoked contractions of rat aorta were inhibited by both (-)-daurisoline and verapamil. 5. In conclusion, (-)-daurisoline, which differed from verapamil in its mode of blocking Ca2+ influx may be a potent Ca2+ antagonist of Ca2+ channels in neurones.

Alkaloids↗