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At least 451 records · Page 25Linked to original sources
PubMed1979

Divalent cation dependent phosphorylation of proteins in squid giant axon.

In vitro and in situ (after intracellular infusion) incubation of axoplasm from the squid giant axon with [gamma-32P]ATP produces a phosphorylation of primarily two proteins (of mol.wt. 200,000 and greater than 400,000). The phosphorylation of these proteins is stimulated by Mg2+, inhibited by Ca2+, and unaffected by 10(-7) to 10(-5) M cyclic nucleotides. The 200 kdalton and greater than 400 kdalton phosphorylated peaks appear to be neurofilament proteins, and phosphorylation of these peaks in situ is decreased by electrical stimulation of the axon.

Adenosine Triphosphate↗
PubMed1982

Flurazepam interaction with sodium and potassium channels in squid giant axon.

External application of 0.05-1.0 mM flurazepam was found to partially block both sodium and potassium currents in voltage-clamped squid giant axons. At the same concentration the fractional block of the potassium current was found to be 3 times greater than that of the sodium current. In the presence of the drug the potassium current appeared to "inactivate', as flurazepam block became more profound during the course of the depolarization. The decay of the potassium current can be explained by a model in which flurazepam enters and blocks the potassium channels only after they have opened. Once bound in the potassium channel, removal of flurazepam from its binding site develops slowly (tau = 48 ms). Thus repetitive stimulation of the nerve produced a cumulative block. When applied inside the axon flurazepam was found to be 1.5 (n = 4) times more potent blocker of potassium channels than following external application. This result suggests that when applied externally, a neutral form of the drug diffuses across the membrane and blocks occurs from the inner end of the channel.

Animals↗
PubMed1983

Bodian's silver method reveals molecular variation in the evolution of neurofilament proteins.

The recent demonstration that Bodian's silver method specifically stains mammalian neurofilament subunits (NFs), but not other intermediate filament proteins (IFs), provides a specific marker for the identification of neurofilament polypeptides. We have applied the Bodian stain to SDS-PAGE separated polypeptides in nervous tissues from 9 species, representing neuronal evolution in 4 major phyla: chordata, mollusca, arthropoda and annelida. Every species tested except the arthropod showed intense silver staining of a set of polypeptides, each subsequently identified as NFs by immunomethods. These results demonstrate that the affinity of NFs for Bodian's silver stain is conserved during the evolution of nervous systems in a diverse spectrum of animals. Further, considerable variation in the molecular weight of NF subunits was found among the 6 vertebrates studied. This variation suggests that the molecular weight of NFs has not been conserved during evolution, a quality which appears to be unusual for a structural protein.

Animals↗
PubMed1983

Blockade of synaptic transmission in the squid giant synapse by a spider toxin (JSTX).

We studied the effect of spider toxin (JSTX)--specific blocker of glutamate receptor--on giant synapse of the squid stellate ganglion. JSTX irreversibly blocked the excitatory postsynaptic potential (EPSP) without affecting the presynaptic action potential or the antidromic action potential. L-glutamate depolarized the postsynaptic membrane and suppressed EPSP which may be due to desensitization. The action of glutamate was completely blocked in the presence of JSTX. The results suggest that glutamate is the transmitter at the giant synapse of squid.

Animals↗
PubMed1984

Glial polypeptides transferred into the squid giant axon.

The proteins synthesized by the glial sheath of an isolated segment of squid giant axon and by the cell bodies of the giant axon in the isolated stellate ganglion were labeled by incubation in the presence of [3H]leucine. The axoplasm, which contained labeled proteins transferred from the glial sheath, was separated from the sheath by mechanical extrusion. The labeled proteins in the axoplasm, the empty sheath and the stellate ganglion were analyzed and compared by one- and two-dimensional polyacrylamide gel electrophoresis. Over 80 glial polypeptides were found to be selectively transferred into the axoplasm and many of these were distinct from stellate ganglion polypeptides which presumably could be supplied to the axon via axonal transport. Three of the more highly labeled transferred glial polypeptides (TGPs) were actin, a fodrin-like polypeptide and a polypeptide we have named traversin. Our observations, considered in the context of other reports, suggest that the squid axon receives a large number of polypeptides from its surrounding glia either by phagocytozing glial cell process that project into it or via cytoplasmic channels between adaxonal glia and the axon. These TGPs may help the axon survive unfavorable conditions.

Animals↗
PubMed1984

Lithium transport across squid axon membrane.

This paper describes the pathways for lithium transport across the axonal membrane of squid. We were able to show that the membrane of this classical neuronal preparation possesses the lithium transport mechanisms previously identified in red blood cells. It is now possible to predict that the lithium treatment-induced changes in choline and lithium transport that have been observed in red blood cells of manic depressive patients also occur in nerve membrane.

Animals↗
PubMed1986

Mammalian optic nerve fibers display two pharmacologically distinct potassium channels.

A suction electrode recording technique was used to study action potential characteristics of rat optic nerve fibers. Two pharmacologically distinct potassium channels are described. One is sensitive to 4-aminopyridine (4-AP) and the other to tetraethylammonium (TEA). 4-AP application leads to a substantial broadening of the optic nerve action potential, but TEA does not. 4-AP application also elicits a TEA-sensitive post-spike positivity, i.e. an intracellular hyperpolarization. From these results we suggest that the 4-AP-sensitive channel, not the TEA-sensitive channel, is primarily responsible for action potential repolarization of mammalian optic nerve fibers.

4-Aminopyridine↗
PubMed1986

Serotonin metabolism and the nature of monoamine oxidase in squid central nervous system.

Monoamine oxidase activity, using type A and type B substrates and inhibitors, was investigated in the central brain and synaptosomes prepared from the optic lobe of squid. Although substantial MAO activity towards serotonin (5-HT), phenylethylamine and tyramine was present, the enzyme could not be differentiated into the two subtypes previously described in the vertebrate central nervous system. However, this enzyme is functional since 5-HT levels, as identified by immunocytochemical procedures, are low in the squid nervous system and show significant increases in pargyline treated squids.

Animals↗
PubMed1986

Sodium depletion in the periaxonal space of the squid axon treated with pyrethroids.

Pyrethroids are known to increase the steady-state sodium current during a step depolarization and to increase and prolong the tail sodium current associated with a step repolarization of the membrane. The pyrethroid-induced tail sodium current of squid axons developed as a function of the duration of the conditioning depolarizing pulse. However, with further lengthening the conditioning pulse duration, it decreased, further increased, or remained constant depending on the direction of sodium current during the depolarization, irrespective of the membrane potential per se. The depletion or accumulation of sodium in the periaxonal space during a 200-ms conditioning depolarizing pulse in the axon internally treated with pronase, pyrethroids, or both, was demonstrated by measurements of the changes in sodium reversal potential. Thus the observed changes in tail current amplitude as a function of the conditioning pulse duration are explicable in terms of changes in sodium concentration in the periaxonal space without assuming inactivation of the pyrethroid-modified channel.

Animals↗
PubMed1986

Chromatophore motoneurons in the brain of the squid, Lolliguncula brevis: an HRP study.

The location of the motoneuron somata controlling activity of the chromatophore muscles was studied in the squid Lolliguncula brevis. Retrograde transport of horseradish peroxidase from injection sites in the skin or in the mantle muscle established that the chromatophore motoneurons are situated in the subesophageal mass of the brain while at least some of the mantle muscle motoneurons are in the stellate ganglia. Motoneurons to chromatophores in the mantle have their somata in the posterior subesophageal mass, mainly in the chromatophore or fin lobes. Motoneurons to chromatophores in the head are located in the anterior pedal lobes and those to the chromatophores in the arms project mainly from the anterior chromatophore lobes. However, some neurons in the posterior chromatophore lobes project to the head or arm regions. A few cells in both the anterior and posterior chromatophore lobes project contralaterally. Somata in other lobes of the subesophageal mass are also labelled by injections in the skin or in the mantle muscle. Evidence presented here suggests that some of the neurons labelled outside the chromatophore lobes are chromatophore motoneurons.

Animals↗