The loss of neuron-specific proteins during the course of Wallerian degeneration of optic and sciatic nerve

Soifer, David; Iqbal, Khalid; H, Czosnek; Martini, Joerg; Sturman, JA; Hm, Wisniewski

doi:10.1523/jneurosci.01-05-00461.1981

Cited by 34 publications

(6 citation statements)

References 13 publications

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“…The biological consequence of the binding of intermediate filament subunits to the 66-kD protein might be to organize them into a cytoskeletal framework. In this regard, it is interesting that Soifer et al (29) observed the disappearance of a 65-kD polypeptide, with an isoelectric point similar to that determined for the 66-kD protein, coincident with the disappearance of the three neurofilament triplet proteins, from both optic and sciatic nerves undergoing Wallerian degeneration. Further studies on the appearance of this protein during development and various disease states may give us further clues as to its importance in both Wallerian degeneration and cytoskeletal dissolution, as well as in growth and cytoskeletal organization.…”

Section: Discussionmentioning

confidence: 64%

alpha-Internexin, a 66-kD intermediate filament-binding protein from mammalian central nervous tissues.

Pachter¹,

Liem²

1985

The Journal of Cell Biology

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In this paper we describe a 66-kD protein that co-purifies with intermediate filaments from rat optic nerve and spinal cord but can be separated further by ion-exchange chromatography. This protein is distinct from the 68-kD neurofilament subunit protein as judged by isoelectric focusing, immunoblotting, peptide mapping, and tests of polymerization competence. This protein is avidly recognized by the monoclonal anti-intermediate filament antigen antibody, previously demonstrated to recognize a common antigenic determinant in all five known classes of intermediate filaments. Also, when isolated this protein binds to various intermediate filament subunit proteins, which suggests an in vivo interaction with the intermediate filament cytoskeleton, and it appears to be axonally transported in the rat optic nerve. Because of this ability to bind to intermediate filaments in situ and in vitro we have named this protein a-internexin. A possible functional role for the protein in organizing filament assembly and distribution is discussed.It is generally acknowledged today that the cytoskeleton of most eukaryotic cells is comprised of three filamentous systems. Two of these, microtubules and microfilaments, are composed of subunit proteins that are phylogenetically highly conserved. In contrast, the third constituent, the intermediate filament, is composed of at least five classes of polypeptides which vary in their biochemical constitution and immunologic specificity and are uniquely displayed in distinct tissue types. These five classes of intermediate filament are vimentin filaments, found primarily in cells of mesenchymal origin; desmin filaments, prevalent in all three types of muscle cells--skeletal, smooth, and cardiac; keratin filaments in cells of epithelial origin; glial filaments, expressed in fibrous astroglia, and Bergmann glia and neurofilaments, present in many, though not all. differentiated neurons of vertebrates and invertebrates (16).Despite their biochemical heterogeneity, the five distinct intermediate filament types demonstrate similar ultrastructures (16) and contain a region with a similar amino acid sequence, which defines a common c~-helical domain (7). All intermediate filament types are also highly insoluble in isotonic buffers in the physiological pH range, which has led to the supposition that they are present in the cytoplasm only in the polymeric state (16). In contrast to tubulin, intermediate filament proteins have been shown to associate with the cytoskeletal framework as nascent polypeptides (5). Organizing centers, similar to microtubule organizing centers, which could assemble the elements of a cytoplasmic array of intermediate filament subunit proteins into polymers, have not been demonstrated in association with any type of intermediate filament network. However, the recent demonstrations that microinjection of antibodies to intermediate filament subunit proteins can effect the collapse of intermediate filament networks (4, 12) suggest that the physiology of the intermediat...

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Section: Discussionmentioning

confidence: 64%

alpha-Internexin, a 66-kD intermediate filament-binding protein from mammalian central nervous tissues.

Pachter¹,

Liem²

1985

The Journal of Cell Biology

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“…The great abundance of these proteins in the optic nerve suggests that they may be important structural proteins of axons or glia; some of them may be neurofilament proteins or nonneuronal intermediate filament proteins Schechter, 1983a, 1984). Like neurofilament proteins (Hoffman and Lasek, 1980;Dahl et al, 1981;Soifer et al, 1981), ON1 and ON2 were rapidly lost from the degenerating nerve. The time course of their reappearance would be consistent with an increase in neurofilaments accompanying the recovery in axonal diameter which is in progress by 12 weeks after nerve crush (Murray, 1982).…”

Section: Discus Stonmentioning

confidence: 99%

Changes in Protein Content of Goldfish Optic Nerve During Degeneration and Regeneration Following Nerve Crush

Perry

Burmeister

Grafstein

1985

Journal of Neurochemistry

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After the goldfish optic nerve was crushed, the total amount of protein in the nerve decreased by about 45% within 1 week as the axons degenerated, began to recover between 2 and 5 weeks as axonal regeneration occurred, and had returned to nearly normal by 12 weeks. Corresponding changes in the relative amounts of some individual proteins were investigated by separating the proteins by two-dimensional gel electrophoresis and performing a quantitative analysis of the Coomassie Brilliant Blue staining patterns of the gels. In addition, labelling patterns showing incorporation of [3H]proline into individual proteins were examined to differentiate between locally synthesized proteins (presumably produced mainly by the glial cells) and axonal proteins carried by fast or slow axonal transport. Some prominent nerve proteins, ON1 and ON2 (50-55 kD, pI approximately 6), decreased to almost undetectable levels and then reappeared with a time course corresponding to the changes in total protein content of the nerve. Similar changes were seen in a protein we have designated NF (approximately 130 kD, pI approximately 5.2). These three proteins, which were labelled in association with slow axonal transport, may be neurofilament constituents. Large decreases following optic nerve crush were also seen in the relative amounts of alpha- and beta-tubulin, which suggests that they are localized mainly in the optic axons rather than the glial cells. Another group of proteins, W2, W3, and W4 (35-45 kD, pI 6.5-7.0), which showed a somewhat slower time course of disappearance and were intensely labelled in the local synthesis pattern, may be associated with myelin. A small number of proteins increased in relative amount following nerve crush. These included some, P1 and P2 (35-40 kD, pIs 6.1-6.2) and NT (approximately 50 kD, pI approximately 5.5), that appeared to be synthesized by the glial cells. Increases were also seen in one axonal protein, B (approximately 45 kD, pI approximately 4.5), that is carried by fast axonal transport, as well as in two axonal proteins, HA1 and HA2 (approximately 60 and 65 kD respectively, pIs 4.5-5.0), that are carried mainly by slow axonal transport. Other proteins, including actin, that showed no net changes in relative amount (but presumably changed in absolute amount in direct proportion to the changes in total protein content of the nerve), are apparently distributed in both the neuronal and nonneuronal compartments of the nerve.

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“…This possibility seemed all the more compelling in view of the recent report (Drgtger et al 1983) that neurofilament protein contains an immunologically-recognised ct-MSH-like portion. This protein has been shown to break down in the early stages of the degenerative process (Bignami et al 1981 ;Soifer et al 1981). We therefore investigated the possible presence of an ~-MSHlike principle in the degenerating nerves during the period of 150 kD neurofilament protein breakdown and ct-MSH sensitivity.…”

Section: Introductionmentioning

confidence: 99%

Evidence that the neurotrophic actions of α-MSH may derive from its ability to mimick the actions of a peptide formed in degenerating nerve stumps

Edwards¹,

Zee²,

Verhaagen³

et al. 1984

Journal of the Neurological Sciences

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SUMMARYThe ability of ~-MSH to facilitate the recovery of sensorimotor nerve function following crush lesion is restricted to a critical period following such a lesion. This period coincided with the initiation of sprouting and the disappearance of the 150 kD neurofilament protein from the degenerating distal stump of the nerve.Degenerating nerve contains a factor that is active in a bioassay system for MSH. This factor could not be detected in control nerves.The hypothesis is forwarded that a neurotrophic factor known to be present in degenerating nerve stumps is an ~-MSH-like peptide formed by the breakdown of the 150 kD neurofilament protein.

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The loss of neuron-specific proteins during the course of Wallerian degeneration of optic and sciatic nerve

Cited by 34 publications

References 13 publications

alpha-Internexin, a 66-kD intermediate filament-binding protein from mammalian central nervous tissues.

alpha-Internexin, a 66-kD intermediate filament-binding protein from mammalian central nervous tissues.

Changes in Protein Content of Goldfish Optic Nerve During Degeneration and Regeneration Following Nerve Crush

Evidence that the neurotrophic actions of α-MSH may derive from its ability to mimick the actions of a peptide formed in degenerating nerve stumps

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