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PubMed1981

Influence of descending bulbospinal monoamine neurons on axonal transport of acetylcholine and cholinergic enzymes.

The influence of descending bulbospinal monoamine (MA) neurons on the intra-axonal transport of acetylcholine (ACh) and related enzymes (cholineacetyltransferase, CAT, and ACh-esterase, AChE) in rat sciatic nerve was studied in crush experiments following intracisternal injections of specific neurotoxins. The injection of 6-hydroxydopamine (6-OH-DA) and 5,6-dihydroxytryptamine (5,6-diOH-TA) (50 micrograms X 2) caused a degeneration of catecholamine (CA) and 5-hydroxytryptamine (5-HT) nerve terminals, respectively, and a combination of the two neurotoxins caused a loss of virtually all MA terminals in the lumbar spinal cord. The results of the neurotoxin injections were controlled by the Falck-Hillarp fluorescence method. The effect of neurotoxin treatment on the enzyme activities in the sciatic nerve was very small. The ACh levels of uncrushed nerves and in nerves proximal to a crush performed 12 hours before dissection decreased following either 6-OH-DA or 5,6-diOH-TA. However, the combination treatment with both 6-OH-DA and 5,6-diOH-TA had no influence on ACh accumulation and transport, as compared to the control group. In a previous study we have shown that mid-thoracic spinal cord transection increased AChE-transport while ACh-transport was decreased. The results of this study indicate that the bulbospinal MA neurons may be involved (perhaps indirectly) i the regulation of ACh levels and transport in motor neurons, but less important for the modulation of the cholinergic enzymes.

Acetylcholine↗
PubMed1982

Composition and subcellular distribution of glycoproteins and glycosaminoglycans undergoing axonal transport in garfish olfactory nerves.

The study examined the subcellular distribution of [3H]glucosamine-labeled glycoconjugates undergoing axonal transport in 100,000 x g soluble and two membranous subfractions of the garfish olfactory nerve. Analysis was made of intact glycoconjugates and of glycopeptides and glycosaminoglycans derived from these molecules by limit protease digestion. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed labeling of a variety of high-molecular-weight molecules with a lower molecular weight distribution in the soluble fraction than in the membranous fractions. Following protease digestion, nearly two-thirds of transported radioactivity in glycopeptides was recovered in the plasma membrane-enriched subfraction, with the remainder equally divided between soluble and higher density membrane fraction. Comparison of the distribution of glycopeptide radioactivity and chemically assayed hexosamine revealed transport labeling of a large variety of different-sized neutral and acidic glycopeptides in all subfractions. Transport labeling of most glycoprotein carbohydrate chains was in proportion of their hexosamine content. Transported glycosaminoglycan label was most heavily concentrated in the plasma membrane fraction, whereas hexosamine was most concentrated in the higher density membrane fraction. The labeling pattern suggested both transported and nontransported pools of these molecules. The specific glycosaminoglycans chondroitin sulfate and heparan sulfate were recovered in all subfractions, whereas hyaluronic acid was confined to the soluble fraction.

Animals↗
PubMed1990

Premature onset of fast axonal transport in bromophenylacetylurea neuropathy: an electrophoretic analysis of proteins exported into motor nerve.

To test whether abnormal processing of proteins for fast axonal transport is involved in the neuropathy induced by BPAU (p-bromophenylacetylurea) we examined transport onset. [35S]Methionine was injected into the lumbar ventral horn of rats 2 weeks after BPAU, 400 mg/kg (i.p.) or vehicle. At intervals of 30-90 min consecutive 3-mm segments of the L4 and L5 ventral roots were digested for polyacrylamide gel electrophoresis and fluorography. Fast transported proteins were identified by comparison with samples from mid-thigh sciatic nerve ligated for 16 h after radiolabeling. A prominent 26 kDa band represented the earliest exported protein. It was usually absent at 30 min, but it entered the roots by 45 min. This band was consistently displaced further in BPAU nerve (n = 11) than in controls (n = 11). The mean difference was 5 +/- 0.6 mm (P less than 0.001). However, there was no difference in the apparent velocity of transport. These results imply premature onset of transport in BPAU neuropathy.

Animals↗
PubMed1993

Differential axonal transport of individual Na,K-ATPase catalytic (alpha) subunit isoforms in rat sciatic nerve.

Three isoforms of the Na,K-ATPase catalytic (alpha) subunit are present in neurons, demonstrated by in situ hybridization of neurons and Western blot of nerve. We used Western blot with antibodies specific for alpha 1, alpha 2 and alpha 3 peptides to measure the accumulation of individual peptides at a ligature on the sciatic nerve. alpha 1 peptide accumulated with kinetics suggesting rapid axonal transport of that isoform within nerve. alpha 2 and alpha 3 peptides did not accumulate at the ligature. These studies provide insight into the dynamics of axonal Na,K-ATPase isoforms.

Animals↗
PubMed1981

Biological importance of the retrograde axonal transport of nerve growth factor in sensory neurons.

Nerve growth factor is retrogradely transported in sympathetic and sensory neurons throughout life. Although this transport is known to be biologically significant in sympathetic neurons, such a function was not yet known in sensory ganglia. By using the neuropeptide substance P as a biochemical marker, we show that sensory ganglia from newborn and adult rats respond in nerve growth factor and that its retrograde axonal transport is biologically relevant, as indicated by an increase in substance P and in general protein content.

Animals↗
PubMed1997

Alteration in neurofilament axonal transport in the sciatic nerve of the diisopropyl phosphorofluoridate (DFP)-treated hen.

Diisopropyl phosphorofluoridate (DFP) is an organophosphorus ester that produces organophosphorus ester-induced delayed neurotoxicity (OPIDN) in hens 7-14 days after a single s.c. dose of 1.7 mg/kg. In this study, hens were treated with a single dose of DFP (1.7 mg/kg, s.c.) 24 hr after [35S]methionine injection into the sacrolumbar region of their spinal cord, and killed 3, 7, 14, or 27 days post-DFP treatment. The rates of transport of labeled high (NF-H), medium (NF-M), and low (NF-L) molecular weight neurofilaments, and tubulin were faster in DFP-treated birds than in controls after 3 days. Subsequently, the rate of transport of these proteins started falling, so that the peaks of labeled proteins in control and DFP-treated hens were overlapping after 7 days. At 14 days, the peaks of NF-H, NF-M, and NF-L in treated hens were distinctly behind the corresponding peaks in control hens. This was again followed by an increase in transport of NF-H and NF-L, but not of NF-M, so that the labeled NF-H and NF-L showed the same pattern in control and treated hens after 27 days. The transient decrease in NF-H and NF-L axonal transport rate, and recovery correlated in a temporal manner with the previously reported increase of Ca2+/calmodulin-dependent protein kinase-mediated phosphorylation of neurofilament proteins and inhibition of calpain activity in the sciatic nerve in OPIDN. Proteinase inhibition has been reported recently to result in enhanced phosphorylation of neurofilaments in some cells. The present study suggests that the enhanced phosphorylation of neurofilaments by DFP-increased Ca2+/calmodulin-dependent protein kinase activity may be contributing toward alteration in NF axonal transport and the development of OPIDN.

Animals↗
PubMed1979

Axonal transport and metabolism of [3H]fucose- and [35S]-sulfate-labeled macromolecules in the rat visual system.

The axonal transport of labeled macromolecules in retinal ganglion cells of rats was investigated from 1 to 20 days following intraocular injection of [3H]fucose and [35S]sulfate. Maximal incorporation of [3H]fucose into acid insoluble material in the retina was at 8 h, followed by a biphasic decline. Transported [3H]fucose (98% as glycoprotein) was in the optic nerve at 1 h, the optic tract and lateral geniculate body by 2 h, and the superior colliculus by 3 h after injection, indicating a rate of transport of approximately 200 mm/day. Radioactivity continued to accumulate in the superior colliculus for at least 8 h and began to decline rapidly by 24 h. Between 3 and 6 days levels rose again in both optic tract and superior colliculus before starting a gradual decline, indicating that a wave of rapidly transported material was delayed in leaving the retina. When proteins in the superior colliculus were fractionated by gel electrophoresis, the composition of the two fucosylated protein transport phases could be partially resolved. Radioactivity in individual gel peaks represented primarily in the first phase decayed with an average half-life of one day, althouth that in one prominent protein of molecular weight 280,000 turned over with a half-life of the order of 12 h. Radioactive peaks primarily in the second phase decayed with an average half-life of more than a week. Incorporation of [35S]sulfate into acid insoluble material in the retina was maximal at 1-2 h, after which there was a rapid loss of label. The appearance of [35S]sulfate in the optic tract, lateral geniculate body and superior colliculus preceded by a short time that of the [3H]fucose; indicating a shorter retinal processing time for this label. The total transported [35S]sulfate in the superior colliculus peaked by 4-8 h and had fallen by 65% at one day; no prominent second wave of transport was observed as was the case for [3H]fucose. Acid insoluble [35S]sulfate in the superior colliculus was equally divided between glycopeptides and glycosaminoglycans at all times examined, indicating that these macromolecules are transported at the same rate. [35S]Sulfate incorporated into various proteins fractionated by gel electrophoresis had heterogeneous turnover rates, the average being around 12 h. Radioactivity in one group of proteins, of molecular weight around 90,000, decayed with a half-life of only a few hours.

Animals↗
PubMed1983

Distribution of proteins migrating with fast axonal transport. Their relationship to smooth endoplasmic reticulum.

The cross-sectional distribution of 3H-labeled proteins moving with the front and plateau of fast axonal transport was analyzed by quantitative electron microscopic autoradiography in sciatic nerves of rats following injection of a 1:1 mixture of [3H]proline and [3H]lysine into lumbar ventral horns. While in the front the transported proteins were uniformly distributed within the axons excluding the axolemma, which was not labeled, in the plateau 90% of 3H-labeled proteins were uniformly distributed and 10% were exclusively located at a 80-nm annulus with its outer edge at the axolemma. Ultrastructural morphometry showed that the density of smooth endoplasmic reticulum (SER) in a 160 nm wide subaxolemmal annulus was approximately twice that in the remaining axon, where it was uniform. These findings: (a) are consistent with the concept that membranous materials are released from the fast transport, move laterally and are inserted into the axolemma; (b) indicate that a portion of SER, largely located at the periphery of the axon, is not involved in fast transport.

Animals↗
PubMed1990

Retrograde axonal transport of neurotensin in the dopaminergic nigrostriatal pathway in the rat.

Although the existence of receptor transport has been clearly demonstrated in peripheral nerves, there is no clear cut evidence in the brain of such a process for neuropeptide receptors. Because of the localization of neurotensin receptors on dopaminergic terminals, the dopaminergic nigrostriatal pathway appears to be the system of choice for studying the axonal transport of neuropeptide receptors in the brain. When labelled neurotensin was injected into the rat striatum, a delayed accumulation of radioactivity in the ipsilateral substantia nigra was observed about 2 h after injection. An essential requirement to clearly observe this phenomenon was the pretreatment of animals with kelatorphan in order to prevent the labelled neurotensin degradation. The appearance of this labelling was prevented by injection of an excess of unlabelled neurotensin or of neurotensin 8-13, an active neurotensin fragment, but not by neurotensin 1-8, which had no affinity for neurotensin receptors. This process was saturable, microtubule-dependent and occurred only in mesostriatal and nigrostriatal dopaminergic neurons as identified after 6-hydroxydopamine lesion and by autoradiography. These results demonstrate that neurotensin was retrogradely transported by a process involving neurotensin receptors. The retrograde transport of receptor-bound neuropeptide may represent an important dynamic process which conveys information molecules from the synapse towards the cell body.

Animals↗
PubMed1976

Selective uptake and retrograde axonal transport of dopamine-beta-hydroxylase antibodies in peripheral adrenergic neurons.

In the present experiments the uptake and retrograde axonal transport of antibodies to dopamine beta-hydroxylase (DBH) in adrenergic neurons was studied. When partially purified labelled antibodies to DBH were injected unilaterally into the vicinity of the adrenergic nerve terminals in the iris, radioactive substances accumulated preferentially in the superior cervical ganglia of the injected. By SDS (sodium dodecyl sulfate) gel electrophoresis and immunoprecipitation it could be shown that the accumulated radioactivity in the superior cervical ganglion represented antibodies to DBH. This retrograde accumulation was greatly reduced by colchicine, axotomy or destruction of the adrenergic nerve terminals by 6-hydroxydopamine. The rate of retrograde transport was the same as that of nerve growth factor (NGF) and tetanus toxin in sympathetic neurons. The retrograde transport of antibodies was confined to sympathetic neurons and could not be detect in either sensory or motor neurons.

Animals↗
PubMed2000

Human amyloid-beta1-42 applied in vivo inhibits the fast axonal transport of proteins in the sciatic nerve of rat.

Human amyloid-beta1-42 has been suggested to be a pathogenetic factor in Alzheimer's disease. The precise mechanism by which this peptide causes the degeneration of neurons in the affected brain is not yet fully understood. By using immunohistochemistry we explored the inhibitory effects of human amyloid-beta1-42 applied in vivo on the fast axonal transport of acetylcholinesterase, the amyloid precursor protein, the vesicular acetylcholine transporter and synaptophysin in the sciatic nerve of rat. Our findings provide evidence for the in vivo neurotoxic effect of human amyloid-beta peptide.

Alzheimer Disease↗
PubMed1996

Slow axonal transport of soluble actin with actin depolymerizing factor, cofilin, and profilin suggests actin moves in an unassembled form.

We examined the axonal transport of actin and its monomer binding proteins, actin depolymerizing factor, cofilin, and profilin, in the chicken sciatic nerve following injection of [35S]methionine into the lumbar spinal cord. At intervals up to 20 days after injection, nerves were cut into 1-cm segments and separated into Triton X-100-soluble and particulate fractions. Actin and its binding proteins were then isolated by affinity chromatography on DNase I-Sepharose and by one- and two-dimensional polyacrylamide gel electrophoresis. Fluorographic analysis showed that the specific activity of soluble actin was two to three times that of its particulate form and that soluble actin, cofilin, actin depolymerizing factor, and profilin were transported at similar rates in slow component b of axonal flow. Our data strongly support the view that the mobile form of actin in slow transport is soluble and that a substantial amount of this actin may travel as a complex with actin depolymerizing factor, cofilin, and profilin. Along labeled nerves the specific activity of the unphosphorylated form of actin depolymerizing factor, which binds actin, was not significantly different from that of its "inactive" phosphorylated form. This constancy in specific activity suggests that continuous inactivation and reactivation of actin depolymerizing factor occur during transport, which could contribute to the exchange of soluble actin with the filamentous actin pool.

Actin Depolymerizing Factors↗
PubMed1998

The corticoclaustral connections in the rat studied by means of the fluorescent retrograde axonal transport method.

The corticoclaustral connections in the rat were investigated by means of the method of the retrograde axonal transport of the fluorescent tracer (Fluoro-Gold; FG). The material consisted of 20 adult Wistar rats. The fluorescent tracer was injected into the anterior, middle or posterior parts of the claustrum. The retrogradely labeled neurons were detected in the layer VI of the neocortex. Injections of the tracer into the anterior part of the claustrum resulted in labeling of the neurons in the motor cortex. After administration of the tracer into the middle part of the insular claustrum, labeled neurons were present both in the motor and somatosensory cortices, while the injections of the tracer into its posterior part resulted in labeling of neurons in the visual cortex. Administration of the fluorescent tracer into the insular claustrum of the rat resulted in labeling of the cortical neurons of the corresponding areas of both hemispheres, however, the contralateral projections seem to be less numerous than the ipsilateral. Our results confirm the existence of reciprocal connections of the claustrum with the neocortex and suggest its role in integration and modification of information reaching the neocortex.

Animals↗
PubMed1984

Aluminum effect on slow axonal transport: a novel impairment of neurofilament transport.

Administration of aluminum (Al) produces accumulation of neurofilaments (NF), called neurofibrillary tangles (NFT), in neuronal cell bodies and proximal axonal segments. This study was undertaken to investigate whether these changes are associated with impairment of the slow axonal transport. Local administration of AlCl3 induced the formation of NFT in 90 to 100% of the rabbit hypoglossal neurons. [35S]Methionine was then administered to the hypoglossal nerve nuclei. The hypoglossal nerves were processed 18 or 28 days later for one- and two-dimensional SDS-polyacrylamide gel electrophoresis and fluorography. Labeled NF polypeptides and a polypeptide of 57 kilodaltons (Kd) were not detectable beyond the proximal 9-mm segment of the hypoglossal nerve in Al-treated rabbits 18 days after labeling, whereas they were present up to 27 mm from the medulla in controls. Tubulin and polypeptides migrating with slow component b were not significantly affected. In rabbits sacrificed 28 days after labeling, accumulation of NF subunits within the proximal 9 mm of hypoglossal nerve was less dramatic, and labeled NF were present up to 30 mm from the medulla whereas they were detectable up to 45 mm in controls. Morphological studies demonstrated the presence of enlarged axons filled with NF in the proximal 9 mm of the hypoglossal nerve. In nerve segments immediately distal, axons were markedly reduced in size and contained no NF but an apparently normal number of microtubules and other organelles. Transport of NF and of a 57-Kd polypeptide is markedly but reversibly slowed down or blocked within the proximal 9-mm segments of the hypoglossal nerve following Al administration to the hypoglossal nucleus. It is suggested that NF transport is maintained distally, resulting in lack of NF in axonal segments immediately distal to the block. Local Al intoxication provides a novel model of impairment of NF transport.

Aluminum↗