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PubMed1996

Actin-based motility of isolated axoplasmic organelles.

We previously showed that axoplasmic organelles from the squid giant axon move toward the barbed ends of actin filaments and that KI-washed organelles separated from soluble proteins by sucrose density fractionation retain a 235-kDa putative myosin. Here, we examine the myosin-like activities of KI-washed organelles after sucrose density fractionation to address the question whether the myosin on these organelles is functional. By electron microscopy KI-washed organelles bound to actin filaments in the absence of ATP but not in its presence. Analysis of organelle-dependent ATPase activity over time and with varying amounts of organelles revealed a basal activity of 350 (range: 315-384) nmoles Pi/mg/min and an actin-activated activity of 774 (range: 560-988) nmoles/mg/min, a higher specific activity than for the other fractions. By video microscopy washed organelles moved in only one direction on actin filaments with a net velocity of 1.11 +/- .03 microns/s and an instantaneous velocity of 1.63 +/- 0.29 microns/s. By immunogold electronmicroscopy, 7% of KI-washed organelles were decorated with an anti-myosin antibody as compared to 0.5% with non-immune serum. Thus, some axoplasmic organelles have a tightly associated myosin-like activity.

Actins↗
PubMed2001

Demonstration of a rhodopsin-retinochrome system in the stalk eye of a marine gastropod, Onchidium, by immunohistochemistry.

The stalk eye of Onchidium sp. (Gastropoda, Mollusca) is the principal photoreceptor in a multiple photoreceptive system that consists of the stalk and dorsal eyes, dermal photoreceptor cells, and photosensitive neurons. To examine the localization of photopigments, the stalk eyes were immunostained with specific antibodies to rhodopsin, retinochrome, and retinal-binding protein (RALBP), which had been generated against squid retinal proteins. The retina of the stalk eye was divided into villous, pigmented, somatic, and neural layers. It was comprised mainly of two types of visual and pigmented supportive cells. The type 1 visual (VC1) cell was characterized by well-developed microvilli on its apical protrusion and photic vesicles in the cytoplasm. The photic vesicles were specifically blackened by prolonged osmification. The type 2 visual (VC2) cell had less numerous, shorter microvilli on its concave apical surface and lacked photic vesicles. The anti-squid rhodopsin antiserum was localized specifically to the villous layer that corresponded to the VC1 microvilli. With the anti-retinochrome peptide antibody, the somatic layer showed specific but patchy, positive staining that corresponded to the cytoplasm of the VC1 cells. Because the photic vesicles are known to contain retinochrome, these results indicate that this retinochrome is localized in the VC1 cytoplasm. Anti-RALBP antibody stained the supranuclear cytoplasm to the distal cytoplasm of VC1 cells. This is the first demonstration of the localization of RALBP in the Gastropoda Onchidium stalk eye. In squid retina that were immunostained as positive controls, the anti-rhodopsin antibody stained rhabdomeric microvilli, the anti-retinochrome antibody stained the inner segment and the basal region of the outer segment, and the anti-RALBP antibody stained the outer and inner segments, respectively. These results suggest that the rhodopsin-retinochrome system that has been established in cephalopod eyes is present in the Onchidium stalk eye.

Animals↗
PubMed2001

Embryonic and paralarval development of the central nervous system of the loliginid squid Sepioteuthis lessoniana.

The embryonic development of the central nervous system (CNS) in the oval squid Sepioteuthis lessoniana is described. It has three distinct phases: (1) The ganglionic accumulation phase: Ganglionic cell clusters develop by ingression, migration, and accumulation of neuroblasts. (2) The lobe differentiation phase: Ganglia differentiate into lobes. The phase is identified by the beginning of an axogenesis. During this phase, neuropils are first formed in the suboesophageal mass, then in the basal lobe system, and finally in the inferior frontal lobes and the superior frontal-vertical lobe systems. (3) The neuropil increment phase: After the shape of the lobes reached its typical form, neuropil growth occurs, specifically in the vertical lobe. The paralarval central nervous system (CNS) is characterized by neuronal gigantism of the giant fibers and some suboesophageal commissures and connectives. The neuropil formation in the CNS of S. lessoniana occurs somewhat earlier than in Octopus vulgaris, although the principal developmental plan is quite conservative among the other coleoids investigated. Some phylogenetic aspects are discussed based on the similarities in the morphologic organization of their brains.

Animals↗
PubMed2007

Evidence for multiple signaling pathways in single squid olfactory receptor neurons.

At least two different G-protein-mediated transduction cascades, the adenylate cyclase and phospholipase C (PLC) pathway, process chemosensory stimuli for various species. In squid olfactory receptor neurons (ORNs), physiological studies indicate that both pathways may be present; however, confirmation of the transduction molecules at the protein level is absent. Here we provide evidence that the G-proteins involved in both adenylate cyclase and PLC pathways are present in squid ORNs (Lolliguncula brevis). We used immunoblotting to show that Galpha(olf), Galpha(q), and a downstream effector, enzyme PLC140, are present in the squid olfactory epithelium (OE). To localize these proteins to one or more of the five morphological cell types described for squid OE, paraformaldehyde-fixed olfactory organs were cryosectioned (10 microm), double-labeled for Galpha(olf), Galpha(q), or PLC140, and imaged. Analysis of serial sections from entire olfactory organs for epithelial area and patterns of immunofluorescence revealed a region of highest immunoreactivity at the anterior half of the organ. At the cellular level, type 1 cells could not be distinguished morphologically and were not included in the analysis. The three labeling patterns observed in type 2 cells were Galpha(q) alone, PLC140 alone, and colocalization of Galpha(q) and PLC140. Subsets of cell types 3, 4, and 5 showed colocalization of Galpha(olf) with Galpha(q) but not with PLC140. These data suggest that the PLC pathway predominates in type 2 cells; however, coexpression of Galpha(olf) with Galpha(q) in cell types 3, 4, and 5 suggests that both pathways may participate in olfactory transduction in non-type 2 squid ORNs.

Adenylyl Cyclases↗
PubMed1986

Distribution of immunoreactive somatostatin (ISRIF) in the nervous system of the squid, Loligo pealei.

Somatostatin (SRIF) is a neuropeptide with a widespread distribution in the mammalian CNS. In the present study we have examined the distribution of immunoreactive-like SRIF (ISRIF)-containing elements in the nervous system of the cephalopod mollusk Loligo pealei, or the Woods Hole squid. ISRIF was localized by light immunocytochemistry in sections of the squid-optic lobe, circumesophageal ganglia-and in stellate ganglion. In the optic lobe, ISRIF neurons were found in the internal granule cell layer and medulla and immunoreactive fibers were seen throughout the lobe and in the optic tract but were absent from the optic nerve, i.e., the projection between the retina and optic lobe. In the supraesophageal complex, ISRIF neurons were found in all lobes, but primarily in the vertical, subvertical, and frontal. In the subesophageal ganglion, ISRIF neurons were seen mainly following unilateral pallial nerve lesions; these neurons were primarily small-to-medium sized. ISRIF fibers were seen in many of the nerves exiting from the brain and in nerves extending between the sub- and supra-esophageal ganglia. In the stellate ganglion, ISRIF was present in many neurons as well as in a plexus of fibers within the ganglion; the peptide was absent from the second-order fibers and the giant axon. The data suggest that a molecule immunologically similar to vertebrate SRIF may be a major transmitter/modulator in this invertebrate. These results provide a foundation for further studies to evaluate the role of this molecule.

Animals↗
PubMed1995

Expression of neurofilament proteins during development of the nervous system in the squid Loligo pealei.

The squid nervous system includes various brain ganglia, optic lobes (the visual center), and the stellate ganglia, the system of giant motor fibers responsible for rapid jet-propelled escape behavior. The large caliber of giant fibers is due, in part, to the accumulation of squid-specific neurofilaments (NFs) made up of a heavily phosphorylated NF 220 protein together with NF 70 and NF 60 subunits. Using antibodies prepared against known peptide sequences in these proteins, together with a mammalian-derived antibody that specifically recognizes phosphorylated squid NF 220, we studied the localization of NFs in adult tissues and during neural development. Immunoblot and immunohistochemical analyses showed that NFs were present in adult neural tissues, primarily in selected fibers, with giant axons showing the most robust expression. After the first neurons differentiated at stage 22, immunoblots showed NF 60- and NF 70-immunoreactive proteins at all stages. The NF 220 subunit, however, was not detected in immunoblots at any developmental stage. Phosphorylated NF 220 immunoreactivity, although absent in immunoblots, was first seen in selected fibers of the stellate ganglia at stage 25, increasing thereafter in all giant fibers until hatching (stage 30). The stellate ganglion is the first neural tissue to acquire a mature neurofilament complement (i.e., phosphorylated NF 220), shortly before the onset of jet-propelled escape behavior. The temporal pattern of expression of the NFs during development resembled that seen in vertebrates; i.e., the smaller NFs appeared before the larger subunit in most neural tissues. In the squid, the expression pattern seems to depend upon the post-transcriptional regulation of a single gene rather than upon transcriptional regulation of three independent genes as in vertebrates.

Animals↗
PubMed1987

Effects of storage time and thermal treatment on the nutritive value of squid (Illex argentinus).

The storage (-28 degrees C) of squids prior to thermal treatment (steaming at 100 degrees C and autoclaving at 115 degrees C) was found to exert no significant influence on the available lysine and tryptophan contents of the flesh stored for no longer than 9-10 months. During a longer period of storage the contents of the studied amino acids decreased by 22.2% on an average. The -SH groups content and weight losses after thermal treatment were increasing with the time of frozen storage. The colour of squid flesh, as measured with a and b indicators (LAB system), changed most in the autoclaved samples, the colour changing towards yellow-red.

Animals↗
PubMed1989

Evidence that glutamate mediates axon-to-Schwann cell signaling in the squid.

High-frequency stimulation (100 Hz) of isolated giant axons of the small squid Alloteuthis subulata and the large squid Loligo forbesi caused the periaxonal Schwann cell resting potential (Em = -40 mV) to hyperpolarize up to 11 mV in direct proportion to train duration and action potential amplitude. In both species, the Schwann cell also hyperpolarized up to 17 mV with the application of L-glutamate (10(-9) to 10(-6) M), in a dose-dependent manner. By contrast, in the presence of 10(-8) M d-tubocurarine (d-TC) to block the cholinergic component of the Schwann cell response, Schwann cells depolarized 8-9 mV during electrical stimulation of the axon or application of L-glutamate. In the presence of 10(-5) M 2-amino-4-phosphonobutyrate (2-APB), the hyperpolarization to glutamate and to axon stimulation was blocked, whereas the cholinergic (carbachol-induced) hyperpolarization was unaffected. In experiments with Alloteuthis, L-aspartate (10(-7) M) also caused a Schwann cell hyperpolarization, but this was not blocked by 2-APB. In tests with glutamate receptor agonists and antagonists, quisqualate (10(-5) M) produced a hyperpolarization blocked by 10(-4) M L-glutamic acid diethylester (GDEE), which also blocked the response to axonal stimulation. Kainic acid (10(-4) M) also caused a hyperpolarization, but n-methyl-D-aspartate (NMDA; 10(-4) M), ibotenate (10(-5) M), alpha-amino-3-hydroxy-5-methyl-isoxazole proprionate (AMPA; (10(-4) M), and isethionate (10(-5) M) had no effect.(ABSTRACT TRUNCATED AT 250 WORDS)

Action Potentials↗
PubMed1990

Substance P modulation of the membrane potential of the Schwann cell of the squid giant nerve fibre.

Substance P produced a dose-dependent, long-lasting hyperpolarization of the membrane of the Schwann cells of the giant nerve fibre of the tropical squid. A survey of the effectiveness of a range of other naturally occurring tachykinin agonists suggested that the receptors present on the squid Schwann cell belong to the subtype SP-P or NK1, for which substance P is the preferred agonist. A survey of the effectiveness of a range of substance P fragments indicated that the direct hyperpolarizing effects of the substance P molecule were mediated by peptides with an intact amidated C-terminal. However, a second subset of receptors that can be activated by N-terminal fragments and analogues lacking an amidated C-terminal was also present in this preparation. The non-subtype-specific antagonist D-Arg1,D-Trp7,9,Leu11 substance P (spantide) was a potent blocker of the effects of substance P in this preparation. Activation of the substance P receptors did not interact with the effects induced by activation of either the nicotinic cholinergic receptors or octopaminergic receptors present in this preparation. However, it did potentiate the effects of activation of the receptors for vasoactive intestinal peptide (VIP), either in response to bath application of the peptide or due to their activation by the release of an endogenous VIP-like peptide after stimulation of the giant axon.

Animals↗
PubMed1994

Neurotransmitter-mediated signaling between axons and glial cells.

Neurotransmitter-mediated signaling is not restricted to the synaptic regions of the nervous system but also takes places along fiber tracts lacking vesicular means of releasing neuroactive substances. The first demonstration for dynamic signaling of this type came in the early 1970s from studies by Villegas and co-workers in squid axons and their satellite Schwann cells. In this invertebrate system, glutamate has been identified as the mediator of this signaling in being first released from the active axons thus setting off a series of cascades, leading to a cholinergic activation of the Schwann cell membrane. Recent evidence suggests that receptor-mediated signaling also exists between glial cells and axons in vertebrates. In the frog optic nerve, axonal activity facilitated the activity of glial ion channels. In the neonatal rat optic nerve, electrical activity of axons triggered oscillations in intracellular calcium in a subset of glial cells. These observations have been postulated to reflect receptor-mediated signaling, including a mechanism in which glutamate is released from axons via the reversal of a transporter and induces intracellular calcium spiking in glial cells via metabotropic glutamate receptors. The efficacy of "axon-to-glia" transmission may, like that in "neuron-to-neuron" transmission, be modulated by co-release of multiple neuroactive substances. One possibility is that adenosine, which is known to be released from fiber tracts, can modulate glutamate signaling in white matter by modulating the periaxonal glutamate concentration through an effect on the glial glutamate uptake system.

Animals↗
PubMed1995

Characterization of a voltage-dependent potassium channel in squid Schwann cells reconstituted in planar lipid bilayers.

An affinity column prepared with noxiustoxin (NTx), a K+ channel blocker from the venom of the Mexican scorpion Centruroides noxius, was used to purify a functional channel from a detergent extract of Schwann cell membrane of the giant axon of the squid Loligo vulgaris. The purified protein was reconstituted as a functional unit in a planar lipid bilayer and tested with a sequence of potentials to obtain information about single-channel amplitude and kinetics. The reconstituted channel showed delayed rectifier behavior with a slope conductance of 10 pS under 5:1 asymmetric KCl concentrations and a clear tendency to open under negative potentials. The zero-current potential was +36mV, which fitted well with the Nernst equation for the CIS/TRANS K(+)-concentration ratio of 5:1. The channel also showed a strong sensitivity to tetraethylammonium and its activity was inhibited by NTx, as expected from the purification procedure. The behavior of this protein in the presence of 0.5 mM ATP (cis side) was also tested, significantly increasing current fluctuations across the membrane. In order to compare the modulation of the Schwann cell K+ channel with that of the axonal K+ channel, a purified protein from the squid axon membrane was also tested in the presence of ATP. This 10-11 pS, delayed rectifier channel from the squid giant axon (Prestipino et al., FEBS Lett. 250:570-574, 1989) was also tested in the presence of ATP and showed a similar rise in activity.

Animals↗
PubMed1989

Identification of a kinesin-like microtubule-based motor protein in Dictyostelium discoideum.

Dictyostelium discoideum, a unicellular eukaryote amenable to both biochemical and genetic dissection, provides an attractive system for studying microtubule-based transport. In this work, we have identified microtubule-based motor activities in Dictyostelium cell extracts and have partially purified a protein that induces microtubule translocation along glass surfaces. This protein, which sediments at approximately 9S in sucrose density gradients and is composed of a 105 kd polypeptide, generates anterograde movement along microtubules that is insensitive to 5 mM NEM (N-ethyl-maleimide) but sensitive to 200 microM vanadate, and has similar nucleotide-dependent microtubule binding properties to those of kinesins purified from mammals, sea urchin and Drosophila. This kinesin-like molecule from Dictyostelium, however, is immunologically distinct from bovine and squid neuronal kinesins and supports microtubule movement on glass at four-fold greater velocities (2.0 versus 0.5 microns/sec). Furthermore, AMP-PNP (adenylyl imidodiphosphate), which promotes attachment of previously characterized kinesins to microtubules, decreases the affinity of the Dictyostelium kinesin homolog for microtubules. Thus, an AMP-PNP-induced rigor binding may not be a characteristic of kinesins from lower eukaryotes.

Adenosine Triphosphatases↗
PubMed1994

Specific interactions of Mss4 with members of the Rab GTPase subfamily.

Mss4 is a mammalian protein that was identified as a suppressor of a yeast secretory mutant harboring a mutation in the GTPase Sec4 and was found to stimulate GDP release from this protein. We have now performed a biochemical characterization of the Mss4 protein and examined the specificity of its association with mammalian GTPases. Mss4 is primarily a soluble protein with a widespread tissue distribution. Recombinant Mss4 binds GTPases present in tissue extracts, and by a gel overlay assay binds specifically Rab Rab10proteins. We further define the Mss4-GTPase interaction to a subset of Rabs belonging to the same subfamily branch which include Rab1, Rab3, Rab8, Rab10, Sec4 and Ypt1 but not Rab2, Rab4, Rab5, Rab6, Rab9 and Rab11. Accordingly, Mss4 co-precipitates from a brain extract with Rab3a but not Rab5. Mss4 only stimulates GDP release from, and the association of GTP gamma S with, this Rab subset. Recombinant Mss4 and Rab3a form a stable complex in solution that is dissociated with either GDP or GTP gamma S. Injection of Mss4 into the squid giant nerve terminal enhances neurotransmitter release. These results suggest that Mss4 behaves as a guanylnucleotide exchange factor (GEF) for a subset of Rabs to influence distinct vesicular transport steps along the secretory pathway.

Animals↗