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PubMed1982

Axonal transport of muscarinic cholinergic receptors in rat vagus nerve: high and low affinity agonist receptors move in opposite directions and differ in nucleotide sensitivity.

The presence and transport of muscarinic cholinergic binding sites have been detected in the rat vagus nerve. These binding sites accumulate both proximal and distal to ligatures in a time-dependent manner. The results of double ligature and colchicine experiments are compatible with the notion that the anterogradely transported binding sites move by fast transport. Most of the sites accumulating proximal to ligatures bind the agonist carbachol with high affinity, while most of the sites accumulating distally bind carbachol with a low affinity. Also, the receptors transported in the anterograde direction are affected by a guanine nucleotide analogue (GppNHp), while those transported in the retrograde direction are less, or not, affected. The bulk of the sites along the unligated nerve trunk bind carbachol with a low affinity and are less sensitive to GppNHp modulation than the anterogradely transported sites. These results suggest that some receptors in the vagus may undergo axonal transport in association with regulatory proteins and that receptor molecules undergo changes in their binding and regulatory properties during their life cycle. These data also support the notion that the high and low affinity agonist form of the muscarinic receptor represent different modulated forms of a single receptor molecule.

Animals↗
PubMed1989

Axonal transport of horseradish peroxidase in the experimental tethered spinal cord.

There has been experimental evidence of the tethered cord syndrome being a gray matter disease resulting from excessive tensile force in the lumbosacral cord. Clinical findings also support this concept. This study was designed to elucidate the possibility of the involvement of the long tract in tethered cord. Long tract continuity was evaluated utilizing the retrograde axonal transport of horseradish peroxidase in fasciculus gracilis. There were no significant differences between the normal and experimental tethered cord in the number of labeled dorsal root ganglion cells of the lumbosacral cord. From this we conclude that involvement of the long sensory tract during steady state of severe cord traction at best is minimal. This study supports the hypothesis that tethered cord syndrome primarily is a gray matter disorder.

Animals↗
PubMed1985

Inhibition of the retrograde axonal transport of dopamine-beta-hydroxylase antibodies by the calcium ionophore A23187.

High levels of calcium, as well as calcium ionophores, have been reported to inhibit the anterograde transport of proteins. The effect of the calcium ionophore, A23187, on the retrograde axonal transport of proteins was therefore investigated. The uptake of antibodies to dopamine-beta-hydroxylase (anti-D beta H) by sympathetic nerve terminals in the iris and their subsequent accumulation in the superior cervical ganglion was inhibited by up to 65% by A23187 (6 nmol, i.o.). At this dose, catecholamine fluorescence in the iris was reduced, indicating a high rate of exocytosis, but tyrosine hydroxylase levels and the capacity of the treated irides to take up noradrenaline were unaffected. Higher amounts of A23187 (28 nmol, i.o.) did not cause a greater degree of inhibition of retrograde transport. However, this dose was toxic to the neurons, as shown by a 68% decrease in the ability of the nerve terminals in the iris to take up [3H]noradrenaline. This loss of function occurred gradually over a 12-h period. On the other hand, tyrosine hydroxylase levels were unaffected by 28 nmol A23187. The toxicity of A23187 may be a consequence of a build up in intracellular calcium, but such toxicity did not lead to any apparent loss of nerve terminals within a 3-day period.

Animals↗
PubMed1982

Abnormalities of axonal transport: are they a cause of peripheral nerve disease?

Applications of pulse-labeling techniques to the study of axonal transport have provided new insights into certain types of peripheral nerve disease. In normal neurons, many of the newly synthesized proteins that are rapidly transported to distal parts of the cell eventually undergo a process of "turnaround," after which they are carried back to the cell bodies for degradation. This turnaround is selectively impaired in rat nerves early in the course of streptozotocin-induced diabetes and of experimental neuropathies induced by exposure to acrylamide, zinc pyridinethione, or p-bromophenylacetylurea. In the neuropathy of p-bromo-phenylacetylurea, depression of turnaround precedes the clinical signs of neurologic dysfunction, is later proportional to the severity of the disability, and may account for the characteristic accumulation of debris in preterminal axons.

Acrylamides↗
PubMed2002

Calcium/calmodulin-dependent protein kinase IIbeta isoform is expressed in motor neurons during axon outgrowth and is part of slow axonal transport.

Previously, we identified calcium/calmodulin-dependent protein kinase IIbeta (CaMKIIbeta) mRNA in spinal motor neurons with 372 bp inserted in what corresponds to the "association" domain of the protein. This was interesting because known additions and deletions to CaMKIIbeta mRNA are usually less than 100 bp in size and found in the "variable" region. Changes in the association domain of CaMKIIbeta could influence substrate specificity, activity or intracellular targeting. We show that three variations of this insert are found in CNS neurons or sciatic motor neurons of Sprague-Dawley rats. We used PCR and nucleic acid sequencing to identify inserts of 114, 243, or 372 bases. We also show that addition of the 372 bases is associated with outgrowth of the axon (the standard CaMKIIbeta downregulates when axon outgrowth occurs). Radiolabeling, immunoblots, and 2D PAGE identified this larger CaMKIIbeta as part of the group of soluble proteins moving at the slowest rate of axonal transport (SCa) in sciatic motor neurons (similar1 mm/day). This group is composed mainly of structural proteins (e.g., tubulin) used to assemble the cytoskeleton of regrowing axons.

Amino Acid Sequence↗
PubMed1990

Proteins of slow axonal transport in sciatic motoneurones of rats with streptozotocin-induced diabetes or galactosaemia.

This study examined the distribution of axonally transported tubulin and a 68 kDa polypeptide in the sciatic nerve 34 days after injection of labelled methionine into the ventral horn of the spinal cord of control rats, rats with streptozotocin-induced diabetes mellitus and rats fed a diet containing 40% galactose. The proteins were separated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) of pellets produced by treatment of nerve extracts with Triton X-100 followed by differential ultra-centrifugation. The most marked effect of both diabetes and galactosaemia was to reduce the amount of activity present in tubulin transported at a rate of 1.4 to 2.1 mm/day. The distribution of activity in the 68 kDa polypeptide band was not markedly affected by either of the experimental conditions. These findings, taken together with those of other studies, indicate that the polyol pathway may contribute to the development of some defects of nerve function in diabetic rats, but is uninvolved in others.

Animals↗
PubMed1981

Rate of anterograde axonal transport of [125I]wheat germ agglutinin from retina to optic tectum in the chick.

We have investigated the rate of anterograde axonal transport of affinity-purified [125I]wheat germ agglutinin (WGA) in chick retinal ganglion cells. By 2 lines of evidence, we found the rate to be 22-44 mm/day. This rate is slower than that reported for many other endogenously synthesized proteins or for horseradish peroxidase, the only other exogenously supplied protein studied as an anterograde transported marker. This difference in rate of transport of [125I]WGA may reflect a novel pathway important in membrane recycling.

Animals↗
PubMed1979

Axonal transport of vasoactive intestinal peptide in sciatic nerve.

Dense plexuses of neurones containing immunoreactive vasoactive intestinal peptide (VIP) have been found in discrete areas of the central nervous system and in peripheral organs, including the gastrointestinal tract, pancreas and urogenital system. In many of these locations VIP is concentrated in nerve endings, where it can be released by high K+ concentrations in a Ca2+-dependent manner. VIP release may also be provoked by electrical stimulation of nerves, for example the vagus. VIP thus shows some of the features of neurotransmitter or neuromodulator substances. The presence of immunoreactive VIP in the fine terminal varicosities as well as in the cell bodies of neurones suggests that it might be transported from the perikaryon, where it is presumably formed, to the nerve endings, through the axonal transport system. Such transport would be in keeping with a role for the peptide as a neurohumor or neurohormone. We report here that VIP accumulates in constricted rat sciatic nerves in a manner suggesting fast, anterograde axonal flow.

Animals↗
PubMed2001

Nerve growth factor modulates the activation status and fast axonal transport of ERK 1/2 in adult nociceptive neurones.

Mature dorsal root ganglion cells respond to neurotrophins, and the intracellular signalling pathways activated by neurotrophins have been characterized in vitro. We have now used immunocytochemistry and Western blots to examine the expression and activation of extracellular signal-regulated protein kinase-1/2 (ERK) in rat dorsal root ganglion cells in vivo, using antisera to total (tERK) and phosphorylated (pERK) forms. This has revealed a number of novel findings. tERK immunoreactivity is present in most dorsal root ganglion cells but is expressed most strongly in small (nociceptive) cells and, surprisingly, is absent in a population of large cells that expressed trkB or trkC but mainly lack p75(NTR) immunoreactivity. In contrast pERK is prominent in a few trkA cells and in satellite glial cells, and is further increased by NGF treatment. tERK and pERK both undergo fast anterograde and retrograde axonal transport, indicated by accumulation at a sciatic nerve ligature, and NGF reduces the level of retrograde pERK transport.

Aging↗
PubMed2006

Axonal transport of microtubules: the long and short of it.

Recent studies on cultured neurons have demonstrated that microtubules are transported down the axon in the form of short polymers. The transport of these microtubules is bidirectional, intermittent, asynchronous, and occurs at the fast rate of known motors. The majority of the microtubule mass in the axon exists in the form of longer immobile microtubules. We have proposed a model called 'cut and run', in which the longer microtubules are mobilized by enzymes that sever them into shorter mobile polymers. In this view, the molecular motors that transport microtubules are not selective for short microtubules but rather impinge upon microtubules irrespective of their length. In the case of the longer microtubules, these motor-driven forces do not transport the microtubules in a rapid and concerted fashion but presumably affect them nonetheless. Here, we discuss the mechanisms by which the short microtubules are transported and suggest possibilities for how analogous mechanisms may align and organize the longer microtubules and functionally integrate them with each other and with the actin cytoskeleton.

Animals↗
PubMed1989

Quantification of axonally transported material using cytofluorimetric scanning.

This paper describes in detail a cytofluorimetric scanning technique used for studying amounts of material axonally transported in antero- and retrograde direction in peripheral nerves. Operating procedures, preparation of tissues and instrumental set-up are described. The basis for quantification of material in a nerve section treated for immunofluorescence is discussed. The reliability of the method has been tested by comparing results with biochemical data. There are several advantages of the technique. (1) Many different substances can be studied in one single nerve segment, thus reducing biological variation and costs. (2) Both morphological data and quantitative figures can be obtained; following scanning the section can be photographed. (3) The method can also be used on studies in the central nervous system and on tissue cultures, since it is possible to scan on single axons or bundles of fibres.

Animals↗
PubMed1983

Fine structure and axonal transport labeling of intraepithelial sensory nerve endings in anterior hard palate of the rat.

The fine structure of intraepithelial free nerve endings, Merkel receptors, and special (possibly chemosensory) corpuscular receptors has been examined in anterior hard palate of the rat. Samples were taken from the two anterior large rugae as well as from the more rostral incisive papilla. Most nerve endings were concentrated in regions in which the epithelium and connective tissue interdigitated extensively. The nerve endings contained relatively pale cytoplasm, a variety of vesicles, and numerous mitochondria. Distinctions could be made among different endings depending on their intraepithelial location, or on the degree of specialization of the neighboring epithelial cells. Simple (free) nerve endings entered the epithelium between epithelial papillae; upon entering, their basal lamina became associated with the epithelial basal lamina in various ways, and their Schwann cell sheath also entered the epithelium for a short length. Free nerve endings were found at various sites among the regular epithelial cells in the basal layers, the stratum granulosum, and stratum spinosum, and next to the stratum corneum border; they did not form specialized junctions with the epithelial cells. Intraepithelial nerve endings at all levels could be labeled by axonal transport from the trigeminal ganglion. Some nerve endings in anterior hard palate were associated with specialized epithelial cells, either in Merkel complexes or in apparent chemosensory corpuscles; both were labeled by axonal transport from the trigeminal ganglion. The specialized epithelial cells in the corpuscular receptors formed possible efferent and afferent synapses with the nerve endings. The nerve endings in the Merkel complexes formed junctions with the specialized Merkel epithelial cells. Both the Merkel complexes and corpuscular receptors were found in their respective characteristic epithelial papillae, which were surrounded by a dense plexus of subepithelial terminal axons and nerve endings.

Animals↗
PubMed1978

Thalamic afferents to the limbic cortex in the cat studied with the method of retrograde axonal transport of horseradish peroxidase.

Thalamic afferents to the limbic cortex in the cat were studied with the method of retrograde axonal transport of horseradish peroxidase. The anterior limbic region receives fibers largely from the anteromedial nucleus and partly from the anterodorsal and anteroventral nuclei. There appears to be a dorsoventral organization of cortical projections of the anteromedial nucleus to the anterior limbic region. The cingular area has its main input from the anteroventral and anteromedial nuclei. The lower bank and fundus of the splenial sulcus receive fibers from the anteroventral nucleus, particularly its parvocellular part. The retrosplenial area receives projections from the naterodorsal, anteroventral and anteromedial nuclei. The agranular retrosplenial area (area 30) recieves hardly any fibers from the anterior thalamic nuclei. The postsubicular and presubicular areas receive cortical afferents from the anterodorsal, anteroventral (both magnocellular and parvocellular parts) and anteromedial nuclei. In addition, the limbic cortex receives many fibers from the dorsal lateral, medial pulvinar and lateral pulvinar nuclei, and few fibers from the intralaminar and midline nuclei.

Afferent Pathways↗
PubMed1997

Increased solubility of high-molecular-mass neurofilament subunit by suppression of dephosphorylation: its relation to axonal transport.

To investigate the role of phosphorylation in the turnover and transport of neurofilament (NF) proteins in vivo, we studied their solubility properties and axonal transport in the rat sciatic nerve using phosphatase inhibitors to minimize dephosphorylation during preparation. About 20% of the 200-kDa subunit (NF-H) in the axon was soluble in the 1% Triton-containing buffer under the present conditions, whereas this amount was less and more variable in the absence of phosphatase inhibitors. The 68-kDa subunit (NF-L) was exclusively insoluble and not affected by the inhibitors. Such selective solubilization of NF-H by phosphorylation differed significantly from the in vitro phosphorylation with cyclic AMP-dependent protein kinase, which resulted in NF disassembly. The carboxy-terminal phosphorylation state of NF-H probed with the phosphorylation-sensitive antibodies was also not directly related to solubility. The solubility of NF-H did not differ along the nerve. In contrast, the solubility of L-[35S]methionine-labeled, transported NF-H was lowest at the peak of radioactivity. Higher solubility at the leading edge, regardless of its location along the nerve, indicates that NF-H solubility is positively correlated with the rate of NF transport.

Animals↗
PubMed1980

Association of an axonally transported polypeptide (H) with 100-A filaments. Use of immunoaffinity electron microscope grids.

Polypeptide H (mol wt 195,000) is axonally transported in rabbit retinal ganglion cells at a velocity of 0.7--1.1 mm/d, i.e., in the most slowly moving of the five transport groups described in these neurons. To identify the organelle with which H is associated, we purified H, prepared antibodies directed against it, and adsorbed the antibodies onto Formvar-coated electron microscope grids. When the resulting "immuno-affinity grids" were incubated with extracts of spinal cord and then examined in the electron microscope, they contained as many as 100 times more 100-A filaments than did grids coated similarly with nonimmune IgG. The ability of the anti-H IgG to specifically adsorb filaments to grids was completely blocked by incubating the IgG with polypeptide H. The 100-A filaments adsorbed to anti-H immunoaffinity grids could be specifically decorated by incubating them with anti-H IgG. These observations demonstrate that H antigens (and most likely H itself) are associated with 100-A neurofilaments. In addition, they suggest that the use of immunoaffinity grids may be a useful approach for determining the organelle associations of polypeptides.

Animals↗
PubMed2004

Cytoplasmic aggregates trap polyglutamine-containing proteins and block axonal transport in a Drosophila model of Huntington's disease.

Huntington's disease is an autosomal dominant neurodegenerative disorder caused by expansion of a polyglutamine tract in the huntingtin protein that results in intracellular aggregate formation and neurodegeneration. Pathways leading from polyglutamine tract expansion to disease pathogenesis remain obscure. To elucidate how polyglutamine expansion causes neuronal dysfunction, we generated Drosophila transgenic strains expressing human huntingtin cDNAs encoding pathogenic (Htt-Q128) or nonpathogenic proteins (Htt-Q0). Whereas expression of Htt-Q0 has no discernible effect on behavior, lifespan, or neuronal morphology, pan-neuronal expression of Htt-Q128 leads to progressive loss of motor coordination, decreased lifespan, and time-dependent formation of huntingtin aggregates specifically in the cytoplasm and neurites. Huntingtin aggregates sequester other expanded polyglutamine proteins in the cytoplasm and lead to disruption of axonal transport and accumulation of aggregates at synapses. In contrast, Drosophila expressing an expanded polyglutamine tract alone, or an expanded polyglutamine tract in the context of the spinocerebellar ataxia type 3 protein, display only nuclear aggregates and do not disrupt axonal trafficking. Our findings indicate that nonnuclear events induced by cytoplasmic huntingtin aggregation play a central role in the progressive neurodegeneration observed in Huntington's disease.

Animals↗
PubMed1987

Combined axonal transport tracing and immunocytochemistry for mapping pathways of peptide-containing nerves in the peripheral nervous system.

The various combinations of axonal transport tracing and immunocytochemistry used for mapping pathways of peptide-containing nerves, and in particular those of the peripheral nervous system, are reviewed. The advantages and disadvantages of these methods are discussed. The applications and results presented illustrate the future potential value of this approach.

Animals↗