[Histochemical data on the evolution of protocephalic neurosecretions in pterygot, insects during axonal transport].
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Axonal transport of actin in rabbit retinal ganglion cells.
We labeled proteins in the cell bodies of rabbit retinal ganglion cells with [35S]methionine and subsequently observed the appearance of radioactive actin in tissues containing the axons and synaptic terminals of these neurons, i.e., the optic nerve (ON), optic tract (OT), lateral geniculate nucleus (LGN) and the superior colliculus (SC). The temporal sequence of appearance of labeled actin (which was identified by its specific binding to DNase I, its electrophoretic mobility, and its peptide map) in these tissues indicated that actin is an axonally transported protein with a maximum transport velocity of 3.4--4.3 mm/d. The kinetics of labeling actin were similar to the kinetics of labeling two proteins (M1 and M2) which resemble myosin; these myosin-like proteins were previously found to be included in the groups of proteins (groups III and IV) transported with the third and fourth most rapid maximum velocities. The similarity in transport between actin and myosin-like proteins supports the idea that a number of proteins in the third and fourth transport groups may be functionally related by virtue of their involvement in a force-generating mechanism and suggests the possibility that these proteins may be axonally transported as a preformed force-generating unit.
Actins↗
Radioautographic study of the axonal transport of proteins into the sensory nerve endings of avian mechanoreceptors.
The axonal transport of proteins to the nerve endings of Herbst and Grandry sensory receptors has been investigated by electron-microscope radioautography. Soon after the injection of [3H]leucine into the trigeminal ganglia of young ducks, labeled proteins are conveyed along the suborbital sensory nerves to the sensory nerve endings at rates of at least 200-280 mm/day. Most of these rapidly transported proteins accumulate in areas containing vesicles of various kinds and along the axolemmal region. Later, the bulk of labeled proteins migrate along the axons at rates of about 15 mm/day and are distributed mainly to the mitochondria. A small portion of labeled material is transferred to the adjoining modified Schwann and specialized Grandry receptor cells. It is concluded that the transport of proteins from sensory ganglia to sensory nerve endings of mechanoreceptors is conveyed at fast and intermediate rates and is mainly used for the renewal of vesicles, axolemmal constituents and mitochondria.
Animals↗
Developmental stages of cortical Lewy bodies and their relation to axonal transport blockage in brains of patients with dementia with Lewy bodies.
We investigated 10 dementia with Lewy bodies (DLB) brains showing various degrees of Lewy pathology using alpha-synuclein-immunohistochemistry, and morphologically divided cortical Lewy bodies (LB) into six developmental stages. Further, we demonstrated the ultrastructure of each stage of cortical LB using alpha-synuclein-immunoelectron microscopy. In the initial stage, alpha-synuclein accumulated in part of the neuronal cytoplasm without filamentous components, then formed LB and LB-related neurites composed of granulo-filamentous components. Finally, LB degraded to extracellular LB composed of loose filamentous components with involved astroglial processes. In addition, we immunohistochemically investigated the accumulation of axonal transported substances in cortical LB, and showed that APP, chromogranin-A, synphilin-1 and synaptophysin accumulated in cortical LB from stages 1, 2, 3 and 4, respectively. These findings suggest that chronic axonal transport blockage is implicated in the development of cortical LB in DLB brains.
Amyloid beta-Protein Precursor↗
Two rates of fast axonal transport of [3H]glycoprotein in an identified invertebrate neuron.
Recently, the kinetics of fast axonal transport of a single type of organelle, the serotonergic storage vesicle, was described in an identified axon of Aplysia using a pulsing technique combined with intracellular injection of [3H]serotonin. Here we extended the single axon studies by analyzing the movement of pulses of [3H]glycoprotein, following injection into the giant Aplysia cell, R2, of the amino sugar [3H]N-acetylgalactosamine. This glycoprotein precursor has been shown to label several organelles in this neuron. [3H]Glycoprotein is found to move in the axon of R2 at 2 rates of fast transport, 174 and 105 mm per day at room temperature. We suggest that the 2 rates reflect movements of 2 different types of organelle.
Acetylgalactosamine↗
Sunday Driver links axonal transport to damage signaling.
Neurons transmit long-range biochemical signals between cell bodies and distant axonal sites or termini. To test the hypothesis that signaling molecules are hitchhikers on axonal vesicles, we focused on the c-Jun NH2-terminal kinase (JNK) scaffolding protein Sunday Driver (syd), which has been proposed to link the molecular motor protein kinesin-1 to axonal vesicles. We found that syd and JNK3 are present on vesicular structures in axons, are transported in both the anterograde and retrograde axonal transport pathways, and interact with kinesin-I and the dynactin complex. Nerve injury induces local activation of JNK, primarily within axons, and activated JNK and syd are then transported primarily retrogradely. In axons, syd and activated JNK colocalize with p150Glued, a subunit of the dynactin complex, and with dynein. Finally, we found that injury induces an enhanced interaction between syd and dynactin. Thus, a mobile axonal JNK-syd complex may generate a transport-dependent axonal damage surveillance system.
Adaptor Proteins, Signal Transducing↗
Essential fatty acid treatment--effects on nerve conduction, polyol pathway and axonal transport in streptozotocin diabetic rats.
This study was designed to examine the effect of dietary supplementation with essential fatty acids (evening primrose oil--5% weight:weight added to the diet) on acute neurophysiological and neurochemical defects in streptozotocin-diabetic rats. Diabetic rats, which were not given evening primrose oil, showed highly significant elevations of nerve sorbitol and fructose combined with a depletion of nerve myo-inositol. In those animals there was also a 40% reduction (p less than 0.02) in the accumulation of axonally transported substance P-like immunoreactivity proximal to a 12 h sciatic nerve ligature together with reduced motor nerve conduction velocity (13% [p less than 0.001] and 20% [p less than 0.001] in two separate experiments). Treatment of other diabetic rats with evening primrose oil prevented completely the development of the motor nerve conduction velocity deficit without affecting sorbitol, fructose or myo-inositol levels or the deficit in axonal transport of substance P. In a second experiment, treatment of diabetic rats with evening primrose oil was associated with significant attenuation of the conduction velocity deficit, but not complete prevention.
Animals↗
Remodeling and sorting process of ethanolamine and choline glycerophospholipids during their axonal transport in the rabbit optic pathway.
The existence of a mechanism by which the ester- and ether-linked aliphatic chains of the major phospholipids are retailored during their axonal transport and sorted to specific membrane systems along the optic nerve and tract was investigated. A mixture of [1-14C]hexadecanol and [3H]arachidonic acid was injected into the vitreous body of albino rabbits. At 24 h and 8 days later, the distribution (as measured by the 3H/14C ratio) and the positioning (as monitored by hydrolytic procedures) of radioactivity in the various phospholipid classes of retina, purified axons, and myelin of the optic nerve and tract were determined. At the two intervals after labeling, the 3H/14C ratios of each diradyl type of phosphatidylethanolamine and phosphatidylcholine were (a) substantially unchanged all along the axons within the optic nerve and tract and (b) markedly modified in comparison with those found in the retina and axons for molecular species selectively restricted to myelin sheath. Evidence is thus available that intraxonally moving ethanolamine and choline glycerophospholipids, among others, are added to axonal membranes most likely without extensive modifications. In contrast, they are transferred into myelin after retailoring. Through these two processes, the sorting and targeting of newly synthesized phospholipids to their correct membrane domains, such as axoplasmic organelles, axolemma, or periaxonal myelin, could be controlled.
Animals↗
Toxic neurofilamentous axonopathies and fast anterograde axonal transport. IV. In vitro analysis of transport following acrylamide and 2,5-hexanedione.
Recent investigations into the mechanisms of neurotoxicity of acrylamide and gamma-diketones have demonstrated reductions in the delivery of radiolabelled proteins to the distal axon. To differentiate a toxicant-induced compromise in the capacity of the fast anterograde axonal transport system from a neuron cell body processing effect, selective exposure of either the L5 dorsal root ganglion or sciatic nerve to 0.7 mM acrylamide (ACR) or 4 mM 2,5-hexanedione (2,5-HD) was performed during in vitro transport. Nerve exposure to ACR decreased the quantity of transport by 32%, 2,5-HD reduced the quantity by 44%. Ganglion exposure produced no significant changes. We conclude that both toxicants penetrate the nerve barriers and act directly and/or indirectly on the axonal transport mechanisms to cause the reductions in transport.
Acrylamide↗
Contribution of axonal transport to the renewal of myelin phospholipids in peripheral nerves. II. Biochemical study.
The classes of radioactive phospholipids appearing in the ciliary ganglion (CG) and especially in the myelin sheath of the intraorbital part of the oculomotor nerve (OMN) were determined after the intracerebral injection of [2-3H]glycerol and [methyl-14C]choline to chickens. Analysis of the radioactive compounds in water-soluble fractions and chloroform-methanol extracts was performed by thin-layer chromatography (TLC). The water-soluble content of the OMN and CG was much poorer in [2-3H]glycerol and metabolites than in [methyl-14C]choline and derivatives. All classes of glycerophospholipids were found to be axonally transported along the OMN and into the CG, but choline-phosphoglycerides (CPG) were largely predominant. In myelin fractions from the OMN, the specific radioactivity (SRA) of CPG labeled with [2-3H]glycerol reached a maximum earlier (40 h) than the SRA of CPG labeled with [methyl-14C]choline. A 25-fold enhancement of the [14C]SRA of sphingomyelin (SM) was observed between 12 h and 7 days. These results indicate that: (1) axonally transported phospholipids labeled with [2-3H]glycerol consist mainly of CPG; (2) small amounts of CPG are translocated from the axon to myelin; and (3) the progressive enrichment of myelin in [14C]CPG and, to a greater extent, SM draws attention to the importance of the base recycling for local synthesis of myelin phospholipids. Thus the axonal supply of Schwann cells with choline and the transfer of axonal phospholipids to myelin would probably contribute to the metabolic interdependence existing between neuron and glia.
Animals↗
Three subpopulations of fast axonally transported retinal ganglion cell proteins are differentially trafficked in the rat optic pathway.
Post-Golgi trafficking of the major fast axonally transported (FT) proteins was investigated in the rat optic pathway. Following intra-ocular injection of 35S-methionine, radiolabeled FT proteins in the optic tract (OT) and superior colliculus (SC) were analyzed by two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) and fluorography. Twenty FT proteins, including a known plasma membrane protein (SNAP-25) and synaptic vesicle protein (synaptobrevin-2), displayed consistent 2D-PAGE migration behavior and were chosen for densitometric quantitative analysis. Results showed that at least three subpopulations of the 20 FT proteins could be differentiated based on their trafficking behavior to axons (OT) vs. terminals (SC). To assess whether Golgi-independent processes (e.g., delayed somal release and/or retrograde transport) could account for the differential compartmentation behavior between the three FT classes, we assessed whether radiolabeled FT proteins became redistributed in the optic pathway following a nerve transection blockade. The results showed that radiolabelled FT proteins did not show a quantitative change in their axon vs. terminal compartmentation in response to disconnection from cell bodies or targets. Thus, the three classes of fast axonally transported proteins were likely trafficked to distinct destinations in the optic pathway by Golgi sorting mechanisms.
Animals↗
Retrograde axonal transport of horseradish peroxidase for determining motor projection patterns to the developing limb in Xenopus.
Horseradish peroxidase (HRP) injected into developing limb buds of Xenopus laevis tadpoles is carried by retrograde axonal transport to the somata of motoneurones in the ventral horn. Small injection of 10% HRP were found to remain well localised to specified sites in the limb bud. Two types of labelled cells were found: diffusely labelled and granular labelled. Diffusely labelled cells result from axonal damage in the presence of HRP. Granular labelled cells result only from uptake of HRP from the region of the axon endings. No gradular uptake was found from axon shafts. It is concluded that the distribution of granular labelled cells accurately reflects the region of the ventral horn projecting to the site of injection in the limb.
Aging↗
Ca2+-activated protease activity in frog sciatic nerve: characterization and effect on rapidly transported axonal proteins.
Protease activity was studied in the frog sciatic nerve. The activity was measured as the release of TCA-soluble radioactivity from either 3H-labelled proteins transported by rapid axonal transport (AXT) or 3H-labelled ganglionic proteins. In nerve homogenates containing transported substrates, protease activity exhibited two peaks, one around pH 5 and one around pH 8. Ca2+ at 100 microM or higher concentrations only stimulated the latter, which was inhibited by 1 mM parachloromercuric benzoate, a sulphydryl reagent, but unaffected by ATP (1 mM). The proteolytic activity was recovered in the 10(5) g supernatant of the homogenate. In desheathed nerves containing 3H-labelled transported proteins, the protease activity could be activated by exposing the nerve to a Ca2+-ionophore, X-537 A, or to an elevated Ca2+-concentration (50 mM). These conditions were also shown to increase the influx and efflux of 45Ca2+ in the nerves. The results indicate the presence within axons of a Ca2+-activated soluble protease, which degrades rapidly transported proteins. The finding that the protease degraded ganglionic soluble proteins to about the same extent suggests a broad substrate specificity. The present system should be useful for further characterization of protease activity during various physiological conditions.
Adenosine Triphosphate↗
Inflammation of the rat paw enhances axonal transport of opioid receptors in the sciatic nerve and increases their density in the inflamed tissue.
The effect of inflammation, induced by unilateral intraplantar injection of Freund's adjuvant, on opioid receptors transported in the sciatic nerve and on opioid receptors present in the paw of the rat was studied by means of in vitro receptor autoradiography using [125I]beta-endorphin (human) as ligand. In the absence of inflammation, human beta-endorphin binding sites accumulated proximally and distally to a ligature placed on the sciatic nerve in a time-dependent manner, indicating bidirectional axonal transport. Some human beta-endorphin binding was also visible in non-inflamed paw tissue. Inflammation of the paw tissue massively increased human beta-endorphin binding on both sides of the sciatic nerve ligature and in the ipsilateral paw tissue. In inflamed paw tissue, beta-endorphin binding accumulated in the cutaneous nerve fibers as well as in the immune cells infiltrating the surrounding tissue. In the sciatic nerve and paw tissue, beta-endorphin binding was displaced by (D-Ala2, N-methyl-Phe4, Gly-ol5)enkephalin and (D-Pen2, D-Pen5)enkephalin, selective mu- and delta-opioid receptor agonists, respectively, and by the universal opioid antagonist naloxone, but not by U-50,488H, a k-selective receptor agonist. Taken together, these data provide neuroanatomical evidence for local inflammation-induced enhanced axonal transport of opioid receptors in rat sciatic nerve and accumulation in paw tissue.
3,4-Dichloro-N-methyl-N-(2-(1-pyrrolidinyl)-cycloh↗
Retrograde axonal transport of beta-adrenoreceptors in rat brain: effect of reserpine.
Retrograde axonal transport of beta-adrenoreceptors was assessed by measuring the accumulation of binding sites for the beta-receptor ligand [125I]iodocyanopindolol [( 125I]ICP) distal to a unilateral 6-hydroxydopamine (6-OHDA) lesion placed in the ascending noradrenergic axons of the locus coeruleus. Accumulation of binding sites was linear over a 3 day period and was blocked by intracerebroventricular 6-OHDA given 1 day prior to sacrifice. A single dose of reserpine (5 mg/kg, i.p.) caused a long lasting (6-8 week) biphasic depletion of frontal cortex norepinephrine (NE) associated with increased frontal cortex binding of another beta-receptor ligand, [3H]dihydroalprenolol [( 3H]DHA), at 7-14 days, and again at 28 days post-reserpine. Unlike the changes in cortical beta-receptors, retrograde transport of [125I]ICP in presynaptic noradrenergic neurons was decreased or blocked completely at 7-14 days and at 6 weeks, and was increased to 470% and 240% of control at 21 days and 8 weeks after reserpine. Anterograde transport of [3H]DHA binding sites was measured by accumulation proximal to a 6-OHDA lesion in this pathway. This transport varied in a pattern similar to that seen for retrograde transport of [125I]ICP binding sites. These data and others suggest that presynaptic beta-receptors are regulated independently of frontal cortex beta-receptors, which appear to be located primarily on postsynaptic cells. On the other hand, the regulation of both anterograde and retrograde transport appears to be interrelated since both types of transport were altered in a similar way in the face of long-term NE depletion by reserpine.
Animals↗
Retrograde axonal transport of endogenous proteins in sciatic nerve demonstrated by covalent labeling in vivo.
Extracellularly applied N-succinimidyl [2,3-3H]propionate was used in vivo to covalently label intra-axonal proteins in the rat sciatic nerve. This technique permitted a unique view of axonal transport of proteins independent of biosynthesis. The proteins detected in slow anterograde transport (1 to 2 millimeters per day) correspond to cytoskeletal proteins described in previous papers. The slowly retrogradely transported component (3 to 6 millimeters per day) was composed primarily of a single protein with a molecular weight of 68,000.
Animals↗
Selective effects of experimental glaucoma on axonal transport by retinal ganglion cells to the dorsal lateral geniculate nucleus.
Rapid-phase axonal transport to the dorsal lateral geniculate nucleus (dLGN) was determined autoradiographically in seven macaque monkey eyes with chronic intraocular pressure (IOP) elevation, in four eyes with an acute IOP elevation, and in three eyes with normal IOP. The monkeys with chronic IOP elevation showed a greater decrease in radioactive labeling of the magnocellular layers of the dLGN than the parvocellular layers by qualitative examination. Grain counts in selected specimens confirmed that transport to the magnocellular layers was less than to the parvocellular layers in monkeys with chronic IOP elevation. This selectivity was present in mildly damaged specimens and increased with greater ganglion cell loss. In monkeys with acute IOP elevation, qualitative evaluation suggested no consistent difference in transport among the dLGN layers; one animal in this group had less transport to the parvocellular than to the magnocellular layers by grain counts. Starting in early stages of the disease, chronic experimental glaucoma causes preferential damage to the ganglion cells that project to the magnocellular layers of the dLGN.
Animals↗
Progressive and selective changes in neurotrophic factor expression and substance p axonal transport induced by perinatal diabetes: protective action of antioxidant treatment.
Diabetes-induced embryo malformations and growth retardation are correlated with a variety of biochemical changes including oxidative stress. In this study, we show that the morphological alterations are correlated with progressive and selective changes of mRNA expression in specific neurotrophic factors. At embryological stage E-17, diabetes affected both embryo growth and NGF mRNA expression, which was reduced by as much as 90 and 56% in target tissues of sensory system such as tongue and intestine, respectively. The reduction in retina and heart was around 50%. Conversely, the mRNA expression of low-affinity neurotrophin receptor p75 was increased. At birth, BDNF mRNA expression was affected with a significant generalized reduction,while in vibrissae we observed a reduction of BDNF and p75 mRNAs and an increase of NGF. At postnatal day 14, pups from diabetic mothers showed reduced muscle levels of IGF-I, while we observed a partial impairment of substance P axonal transport at postnatal day 28. Treatment of diabetic mothers with silybin, a flavonoid with antioxidant properties, prevented most of the changes in neurotrophic factor expression and substance P axonal transport with no effects on hyperglycemia and embryo growth retardation. These results indicate that oxidative stress may influence neurotrophic factor synthesis in target territories during development. In addition, these data suggest that nervous system abnormalities observed in diabetic embryopathy may also derive by insufficient neurotrophic factor biosynthesis involving sequentially NGF in the embryo and BDNF and IGF-I in the early postnatal days. Insulin treatment of diabetic mothers normalized hyperglycemia and body growth, with consequent regular embryonic and postnatal development.
Animals↗