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At least 1,495 records · Page 83Linked to original sources
PubMed2005

A mutation in the small heat-shock protein HSPB1 leading to distal hereditary motor neuronopathy disrupts neurofilament assembly and the axonal transport of specific cellular cargoes.

Distal hereditary motor neuronopathies (dHMNs) are a clinically and genetically heterogeneous group of disorders in which motor neurons selectively undergo age-dependant degeneration. Mutations in the small heat-shock protein HSPB1 (HSP27) are responsible for one form of dHMN. In this study, we have analysed the effect of expressing a form of mutant HSPB1 in primary neuronal cells in culture. Mutant (P182L) but not wild-type HSPB1 led to the formation of insoluble intracellular aggregates and to the sequestration in the cytoplasm of selective cellular components, including neurofilament middle chain subunit (NF-M) and p150 dynactin. These findings suggest a possible pathogenic mechanism for HSPB1 whereby the mutation may lead to preferential motor neuron loss by disrupting selective components essential for axonal structure and transport.

Axonal Transport↗
PubMed1984

Fast axonal transport of tyrosine sulfate-containing proteins: preferential routing of sulfoproteins toward nerve terminals.

The presence of a subset of fast-transported proteins containing sulfate while lacking carbohydrate residues [Stone et al. (1983). J. Neurochem. 41:1085-1089] was confirmed by two-dimensional gel electrophoretic analysis of individual fast-transported proteins double-labeled with 35SO4 and [3H]mannose. Analysis by high-pressure liquid chromatography revealed that the sulfate moieties of these "sulfoproteins" are linked to tyrosine residues. Separation of fast-transported 35SO4-labeled proteins delivered to local regions of axon from proteins en route toward terminal regions demonstrated, on the basis of acid lability of tyrosine-bound sulfate, that the sulfoproteins were localized preferentially in the wavefront of fast-transported proteins. Analysis of individual sulfoproteins confirmed differential transport in that sulfoproteins were present at threefold greater amount in the wavefront than in material off-loaded to local regions of the axon. By contrast, nonsulfated species of molecular weights similar to those of the sulfoproteins were detected in nearly equal amounts in both regions of the transport profile. Treatment of nerve segments containing total 35SO4-labeled fast-transported proteins with sodium carbonate led to solubilization of half the protein-bound sulfate. Exposure of the solubilized proteins to mild acid resulted in the release of approximately 80% of the 35SO4 associated with this fraction. Two-dimensional gel patterns displaying carbonate releasable or nonreleasable fractions are consistent with the most abundantly labeled sulfoproteins being transported within membrane-bound organelles. In terms of apparent destination and subcellular compartmentalization, the sulfoproteins meet critical requirements for consideration as secretable fast-transported proteins.

Animals↗
PubMed1983

Microtubule-neurofilament segregation produced by beta, beta'-iminodipropionitrile: evidence for the association of fast axonal transport with microtubules.

The subperineurial injection of beta,beta'-iminodipropionitrile (IDPN) into rat sciatic nerves resulted in focal disorganization of the axonal cytoskeleton characterized by segregation of neurofilaments and microtubules. Shortly after injection, microtubules clustered together to form a central channel, while neurofilaments became chaotically arrayed between the microtubule channel and axolemma. Electron microscopic autoradiography disclosed that rapidly transported organelles were preferentially associated with the microtubule-enriched central channels. These studies indicate that IDPN acts at the level of the axon to disrupt interactions between cytoskeletal elements and show that rapidly transported constituents are preferentially conveyed in association with microtubules. The model provides an opportunity to dissect the interactions of the cytoskeletal elements and other organelles.

Animals↗
PubMed2006

Axonal transport of mitochondria requires milton to recruit kinesin heavy chain and is light chain independent.

Mitochondria are distributed within cells to match local energy demands. We report that the microtubule-dependent transport of mitochondria depends on the ability of milton to act as an adaptor protein that can recruit the heavy chain of conventional kinesin-1 (kinesin heavy chain [KHC]) to mitochondria. Biochemical and genetic evidence demonstrate that kinesin recruitment and mitochondrial transport are independent of kinesin light chain (KLC); KLC antagonizes milton's association with KHC and is absent from milton-KHC complexes, and mitochondria are present in klc (-/-) photoreceptor axons. The recruitment of KHC to mitochondria is, in part, determined by the NH(2) terminus-splicing variant of milton. A direct interaction occurs between milton and miro, which is a mitochondrial Rho-like GTPase, and this interaction can influence the recruitment of milton to mitochondria. Thus, milton and miro are likely to form an essential protein complex that links KHC to mitochondria for light chain-independent, anterograde transport of mitochondria.

Animals↗
PubMed1983

Alpha-bungarotoxin binding sites on sensory neurones and their axonal transport in sensory afferents.

The autoradiographic localization of [125I]alpha-bungarotoxin binding sites on primary sensory fibres was investigated. Nicotinic alpha-bungarotoxin binding sites were localized to a small sub-population of large dorsal root ganglion cells in the rat, monkey, cat and human dorsal root ganglia. Ligation of the sciatic nerve or dorsal root in the rat resulted in an anterograde accumulation of binding sites proximal to the dorsal root ganglion, and a small retrograde accumulation. Unilateral dorsal root section in the rat produced a loss of toxin binding sites mainly within lamina III of the dorsal horn. These results suggest that nicotinic alpha-bungarotoxin binding sites manufactured in large dorsal root ganglion cell bodies are transported both centrally to the spinal cord and also peripherally.

Afferent Pathways↗
PubMed1995

Axonal transport of fluorescent carbocyanine dyes allows mapping of peripheral nerve territories in gingiva.

Sensory innervation of gingival tissue can cause neurogenic inflammation that depends on the extent of the branching area of the peripheral nerve fibers. We designed the present study to determine whether single trigeminal axons branch to both the buccal and palatal gingiva of maxillary molars of adult rats. Accumulation via retrograde transport of DiI (red) or DiA (green) fluorescent carbocyanine dyes in neurons of trigeminal ganglia was evaluated 7 days after applying one dye to the buccal sulcus and the other to the palatal sulcus. Both dyes were absorbed through the junctional epithelium, and the two sites each labeled similar numbers and sizes of neurons in the lateral zone of the maxillary division (44% from buccal and 46% from palatal gingiva). Double-labeled neurons had the same size (32.5 +/- 6.70 microns, mean circumference +/- S.D.) and location as single-labeled neurons, and they were 9% of the total. This study shows that exogenous dyes can diffuse into mucosa and thereby allow in vivo mapping of sensory nerve branching patterns to several intact tissues per animal. We found that 9% of the labeled cells extended to both the buccal and palatal gingiva. Thus, inflammation that spreads from one gingival region to the other could have a neurogenic mechanism involving trigeminal sensory neurons that extend their peripheral branches to innervate both buccal and palatal gingiva of adult rat molars.

Absorption↗