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PubMed2006

Confocal microscopy of the light organ crypts in juvenile Euprymna scolopes reveals their morphological complexity and dynamic function in symbiosis.

In the hours to days following hatching, the Hawaiian bobtail squid, Euprymna scolopes, obtains its light-emitting symbiont, Vibrio fischeri, from the surrounding environment and propagates the bacteria in the epithelial crypts of a specialized light organ. Three-dimensional analyses using confocal microscopy revealed that each of the three crypts on either side of the juvenile light organ is composed of four morphological regions. Progressing from the lateral pore to the medial blind end of each crypt, the regions consist of 1) a duct, 2) an antechamber, 3) a bottleneck, and 4) a deep region. Only the deep region houses a persistent bacterial population, whereas the duct, antechamber, and bottleneck serve as conduits through which the bacteria enter during initial colonization and exit during diel venting, a behavior in which approximately 90% of the symbionts are expelled each dawn. Our data suggest that, like the duct, the antechamber and bottleneck may function to promote and maintain the specificity of the symbiosis. Pronounced structural and functional differences among the deep regions of the three crypts, along with previously reported characterizations of embryogenesis, suggest a continued developmental progression in the first few days after hatching. Taken together, the results of this study reveal a high degree of complexity in the morphology of the crypts, as well as in the extent to which the three crypts and their constituent regions differ in function during the early stages of the symbiosis.

Aliivibrio fischeri↗
PubMed1977

An ultrastructural and cytochemical analysis of oogenesis in the squid, Loligo pealei.

Oogenesis has been investigated utilizing both light and electron microscopical techniques in the squid, Loligo pealei. This complex process has been divided into five stages according to the structure of the follicle. Because of the highly coordinated differentiation of the follicle cells (and follicular syncytium) and the oocyte, their development is described in concert. Specific attention is given to the contribution of the follicular syncytium to vitellogenesis and the formation of the extracellular egg envelope or chorion. Our observations indicate heterosynthetic yolk production and the synthesis of the secondary envelope by the follicular syncytium.

Animals↗
PubMed2002

Trafficking of axonal K+ channels: potential role of Hsc70.

Voltage-gated potassium ion channels in axons underlie the repolarization phase of the membrane action potential and help to set the resting potential. In addition to being present in the axolemma, they are also found in axoplasm in small vesicles, 30-50 nm in diameter, which may serve as a reserve pool of K+ channel protein (Clay and Kuzirian [2000] J Neurobiol 45:172-184). We have developed a novel technique for extracting these vesicles from axoplasm, which relies on the ability of Texas red to bind to them, thereby reducing their buoyancy so that they are amenable to pelleting by ultracentrifugation (Clay and Kuzirian [2000] J Neurobiol 45:172-184). The mechanism underlying this process may be binding of Texas red to Hsc70, which is primarily a cytosolic protein. However, a small portion of it is located on the surface of vesicles. Kinesin is also on the vesicle surface. This protein is membrane bound in our in vitro vesicle preparation when solutions that do not contain MgATP are added to extruded axoplasm. The addition of MgATP to the solution appears to release a significant amount of kinesin from the vesicles, possibly by the Hsc70-MgATP catalysis mechanism recently proposed by Tsai et al.

Animals↗
PubMed2001

Local synthesis of nuclear-encoded mitochondrial proteins in the presynaptic nerve terminal.

One of the central tenets in neuroscience has been that the protein constituents of distal compartments of the neuron (e.g., the axon and nerve terminal) are synthesized in the nerve cell body and are subsequently transported to their ultimate sites of function. In contrast to this postulate, we have established previously that a heterogeneous population of mRNAs and biologically active polyribosomes exist in the giant axon and presynaptic nerve terminals of the photoreceptor neurons in squid. We report that these mRNA populations contain mRNAs for nuclear-encoded mitochondrial proteins to include: cytochrome oxidase subunit 17, propionyl-CoA carboxylase (EC 6.4.1.3), dihydrolipoamide dehydrogenase (EC 1.8.1.4), and coenzyme Q subunit 7. The mRNA for heat shock protein 70, a chaperone protein known to be involved in the import of proteins into mitochondria, has also been identified. Electrophoretic gel analysis of newly synthesized proteins in the synaptosomal fraction isolated from the squid optic lobe revealed that the large presynaptic terminals of the photoreceptor neuron contain a cytoplasmic protein synthetic system. Importantly, a significant amount of the cycloheximide resistant proteins locally synthesized in the terminal becomes associated with mitochondria. PCR analysis of RNA from synaptosomal polysomes establishes that COX17 and CoQ7 mRNAs are being actively translated. Taken together, these findings indicate that proteins required for the maintenance of mitochondrial function are synthesized locally in the presynaptic nerve terminal, and call attention to the intimacy of the relationship between the terminal and its energy generating system. J. Neurosci. Res. 64:447-453, 2001. Published 2001 Wiley-Liss, Inc.

Animals↗
PubMed1990

Characterization of the distinctive neurofilament subunits of the soma and axon initial segments in the squid stellate ganglion.

The stellate ganglion, which gives rise to the giant axons of the squid, was dissected into two parts, one containing primarily cell bodies and the other axon initial segments. A neurofilament protein-enriched extract of each was prepared and compared biochemically and immunochemically with an axoplasmic neurofilament preparation and with the glial sheath that surrounds the axons. Both parts of the ganglion lacked the 220 kDa subunit of axoplasmic neurofilaments (NFs). However, they did contain a protein of about 190 kDa that reacted with the Pruss anti-intermediate filament antibody (aIFA; Pruss et al.: Cell 27:419-428, 1981), but not with a phosphorylation-dependent NF antibody (Cohen et al.: J Neurosci 7: 2056-2074, 1987). Dephosphorylation of the axoplasmic NF220 yielded a product that comigrated on two-dimensional (2D) gel electrophoresis with the 190 kDa ganglion protein, suggesting that the latter represented the incompletely phosphorylated precursor of NF220. The major low molecular weight aIFA-reactive species in the ganglion preparations was a polypeptide of about 65 kDa. A relatively small quantity of that polypeptide was also found in axoplasm and it comigrated in 2D gels with an aIFA-reactive polypeptide from the glial sheath. These results indicate that the site of modification of the 190 kDa NF precursor to the 220 kDa axonal form is probably at the point where the axon initial segments leave the ganglion, which is several mm distal to its site of synthesis in the cell body. Furthermore, the filament network of the axoplasm and possibly the cell bodies includes a glial-like intermediate filament protein in addition to the NF protein subunits.

Animals↗
PubMed1991

Active polysomes in the axoplasm of the squid giant axon.

Axons and axon terminals are widely believed to lack the capacity to synthesize proteins, relying instead on the delivery of proteins made in the perikaryon. In agreement with this view, axoplasmic proteins synthesized by the isolated giant axon of the squid are believed to derive entirely from periaxonal glial cells. However, squid axoplasm is known to contain the requisite components of an extra-mitochondrial protein synthetic system, including protein factors, tRNAs, rRNAs, and a heterogeneous family of mRNAs. Hence, the giant axon could, in principle, maintain an endogenous protein synthetic capacity. Here, we report that the squid giant axon also contains active polysomes and mRNA, which hybridizes to a riboprobe encoding murine neurofilament protein. Taken together, these findings provide direct evidence that proteins (including the putative neuron-specific neurofilament protein) are also synthesized de novo in the axonal compartment.

Animals↗
PubMed1995

Glia-to-axon communication: enrichment of glial proteins transferred to the squid giant axon.

The transfer of newly synthesized proteins from the glial sheath into the axon is a well-documented process for the squid giant axon. In this study, we used a novel approach to separate the transferred glial proteins (TGPs) from the endogenous axoplasmic proteins of the squid giant axon. Axoplasm, containing radiolabelled TGPs, was extruded as a cylinder and immersed in an intracellular buffer. After 1-30 min, the TGPs were enriched in the intracellular buffer, because they were eluted from the axoplasm into the intracellular buffer much faster than the endogenous axoplasmic proteins. Most of the TGPs enriched in the intracellular buffer did not pellet when centrifuged at 24,000 g for 20 min and were susceptible to protease digestion without the addition of Triton X-100. Additionally, transmission electron microscopic autoradiography of intact axons, containing radiolabelled TGPs, suggested that most TGPs were not associated with vesicular organelles within the axon. We conclude that most of the TGPs are not contained within vesicles in the axoplasm of the squid giant axon, as would be expected if the mechanism of glia-to-axon transfer were conventional exocytosis-endocytosis or microphagocytosis.

Animals↗
PubMed2003

Effects of barrier-induced nuclear spin magnetization inhomogeneities on diffusion-attenuated MR signal.

The spatial distribution of the transverse nuclear spin magnetization, appearing in a single compartment with impermeable boundaries in a Stejskal-Tanner gradient pulse MR experiment, is analyzed in detail. At short diffusion times the presence of diffusion-restrictive barriers (membranes) reduces effective diffusivity near the membranes and leads to an inhomogeneous spin magnetization distribution (the edge-enhancement effect). In this case, the signal reveals a quasi-two-compartment behavior and can be empirically modeled remarkably well by a biexponential function. The current results provide a framework for interpreting experimental MR data on various phenomena, including water diffusion in giant axons, metabolite diffusion in the brain, and hyperpolarized gas diffusion in lung airways.

Animals↗
PubMed1994

Water diffusion in the giant axon of the squid: implications for diffusion-weighted MRI of the nervous system.

To clarify the result that marked diffusional anisotropy had been found in nomyelinated nerve, and in completion of an evaluation of the role of all longitudinal axonal structures, we report NMR measurements of water diffusion in the giant axon of the squid, where diffusional anisotropy is determined by the neurofilamentary structure. The diffusion coefficients of water parallel and perpendicular to the long axis of the squid giant axon at 20 degrees C are (1.61 +/- 0.06) x 10(-5) cm2 s-1 and (1.33 +/- 0.09) x 10(-5) cm2 s-1, respectively, which yield an anisotropic diffusion ratio of 1.2 +/- 0.1. Water diffusion in the squid giant axon is therefore quite rapid and nearly isotropic, thus eliminating the possibility of a significant role for the longitudinally oriented neurofilaments in producing diffusional anisotropy within the axoplasm. In conjunction with our work on garfish nerves therefore, only membranes, either as numerous axonal membranes or as myelin (if present), remain to fulfill the role of the primary determinant of anisotropic water diffusion in nerve and in white matter.

Animals↗
PubMedDate not supplied

Ionic channels: II. Voltage- and agonist-gated and agonist-modified channel properties and structure.

This article reviews the different forms of ionic channels: voltage-gated, agonist-gated, and agonist- and second messenger-modified channels. The recent advances in our knowledge of the amino acid sequence of the sodium channel and the nicotinic acetylcholine receptor and the relationship of the primary structure to the channels' quarternary structure and function are discussed.

Animals↗
PubMed2004

Topographic regulation of phosphorylation in giant neurons of the squid, Loligo pealei: role of phosphatases.

In previous studies of phosphorylation in squid stellate ganglion neurons, we demonstrated that a specific multimeric phosphorylation complex characterized each cellular compartment. Although the endogenous protein profile of cell body extracts (giant fiber lobe, GFL), as determined by Coomassie staining, was similar to that of axoplasm from the giant axon, in this study we show that the protein phosphorylation profiles are qualitatively different. Whereas many axoplasm proteins were phosphorylated, including most cytoskeletal proteins, virtually all phosphorylation in perikarya was confined to low molecular weight compounds (<6 kDa). Because phosphorylation of exogenous substrates, histone and casein, was equally active in extracts from both compartments, failure to detect endogenous protein phosphorylation in cell bodies was attributed to the presence of more active phosphatases. To further explore the role of phosphatases in these neurons, we studied phosphorylation in the presence of serine/threonine and protein tyrosine phosphatase (PTP) inhibitors. We found that phosphorylation of axonal cytoskeletal proteins was modulated by okadaic acid-sensitive ser/thr phosphatases, whereas cell body phosphorylation was more sensitive to an inhibitor of protein tyrosine phosphatases, such as vanadate. Inhibition of PTPs by vanadate stimulated endogenous phosphorylation of GFL proteins, including cytoskeletal proteins. Protein tyrosine kinase activity was equally stimulated by vanadate in cell body and axonal whole homogenates and Triton X-100 free soluble extracts, but only the Triton X soluble fraction (membrane bound proteins) of the GFL exhibited significant activation in the presence of vanadate, suggesting higher PTP activities in this fraction than in the axon. The data are consistent with the hypothesis that neuronal protein phosphorylation in axons and cell bodies is modulated by different phosphatases associated with compartment-specific multimeric complexes.

Animals↗
PubMed2004

Short-range axonal/dendritic transport by myosin-V: A model for vesicle delivery to the synapse.

Myosin-V is a versatile motor involved in short-range axonal/dendritic transport of vesicles in the actin-rich cortex and synaptic regions of nerve cells. It binds to several different kinds of neuronal vesicles by its globular tail domain but the mechanism by which it is recruited to these vesicles is not known. In this study, we used an in vitro motility assay derived from axoplasm of the squid giant axon to study the effects of the globular tail domain on the transport of neuronal vesicles. We found that the globular tail fragment of myosin-V inhibited actin-based vesicle transport by displacing native myosin-V and binding to vesicles. The globular tail domain pulled down kinesin, a known binding partner of myosin-V, in affinity isolation experiments. These data confirmed earlier evidence that kinesin and myosin-V interact to form a hetero-motor complex. The formation of a kinesin/myosin-V hetero-motor complex on vesicles is thought to facilitate the coordination of long-range movement on microtubules and short-range movement on actin filaments. The direct interaction of motors from both filament systems may represent the mechanism by which the transition of vesicles from microtubules to actin filaments is regulated. These results are the first demonstration that the recombinant tail of myosin-V inhibits vesicle transport in an in vitro motility assay. Future experiments are designed to determine the functional significance of the interaction between myosin-V and kinesin and to identify other proteins that bind to the globular tail domain of myosin-V.

Actin Cytoskeleton↗
PubMed1975

Effects of thiamine antagonists on nerve conduction. II. Voltage clamp experiments with antimetabolites.

Thiamine antimetabolites were externally applied to voltage clamped squid giant axons to investigate the possible role of thiamine in nerve conduction. Phenylthiazinothiamine, in concentrations as low as 250 muM, reduced peak early current and steady-state current, with the depression of the former being two to five times greater than that of the latter. Peak transient and steady-state conductances were about equally depressed by thiamine tert-butyl disulfide (2 mM) and L-586944-00P07 (5-10 mM). None of the antimetabolites produced an appreciable change in the kinetics of Na+ activation, K+ activation, or Na+ inactivation. Thiamine itself, applied externally up to 30 mM, had no appreciable effect on either the magnitude or time course of the ionic currents. Although these data are consistent with the hypothesis that thiamine may be involved in nerve conduction, they probably reflect a nonspecific stabilizing interaction of this class of compound with the axon membrane. Taken in this light, the hypothesis that thiamine plays a direct role in Na+ channel permeability changes must be reevaluated.

Animals↗
PubMed1976

A long-lasting birefringence change recorded from a tetanically stimulated squid giant axon.

A long-lasting birefringence change (the delayed response) was found to be produced in a tetanically stimulated squid giant axon. The change was independent of the concurrent membrane potential change, summated on repetitive stimulation, and always had a sign representing a decrease in resting birefringence. The axons was placed between a polarizer and an analyzer with their polarizing axes crossed, making an angle of 45 degrees with the longitudinal direction of the axon. The light beam that passed through the axon and the other optical elements was received by a photodiode. The change in light intensity evoked by repetitive stimulation was composed of brief initial responses, which took place in response to individual stimuli, and a delayed response, which developed gradually and lasted for several hundred msec. It was necessary to differentiate the effect of birefringence change from that of turbidity change. Formulas were derived on the assumption that the optical properties of the axon could be represented by a model of a uniaxial crystal that was not only birefringent but also dichroic, its extinction coefficients and the angle of retardation being changed independently on excitation. Calculations with them yielded the resting retardation, which agreed well with those obtained by the Senarmont's method, and the change in birefringence, which agreed well with the other calculated value derived from experiments using a quarter-wave plate. The results of the calculation confirmed the existence of the long-lasting birefringence change in the tetanically stimulated axon.

Action Potentials↗
PubMed1977

The presence of transfer RNA in the axoplasm of the squid giant axon.

Previous work has revealed that 4S RNA is the primary species of RNA in the axoplasm from the giant axons of the squid and Myxicola. This study shows that axoplasmic 4S RNA from the squid giant axon has the functional properties of tRNA. Axoplasmic RNA was charged with amino acids by aminoacyl-tRNA synthetases prepared from squid brain. Tthe aminoacylation was prevented by incubating the RNA with RNase prior to running the reaction. The amino acid-RNA complex was labile at pH 9, which is characteristic of the acyl linkage between an amino acid and its tRNA. Aminoacyl-tRNA synthetase activity was also present in the axoplasm, primarily in the soluble fraction.

Amino Acyl-tRNA Synthetases↗