Proteins of fast axonal transport in the regenerating hypoglossal nerve of the rat

Redshaw, J.D.; Bisby, Mark A.

doi:10.1139/y84-231

Cited by 33 publications

(10 citation statements)

References 9 publications

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“…Our results indicate that the fluorescence signal strength, on average, was higher in the puncta of the aged rat. In adult animals, GAP-43 is transiently upregulated in neurons subjected to axonal damage (Redshaw and Bisby, 1984;TetzlafT et al, 1991;Chong et al, 1992;Lindd et al, 1992;Booth and Brown, 1993;Mehta et al, 1993;Li et al, 1993;Piehl et al, 1993b). A normalization of the GAP-43 expression usually occurs a few weeks following lesioning, even if a functional regeneration is not achieved.…”

Section: Increased Levels Of Gap-43 In Aged Motoneurons Supplying Incmentioning

confidence: 99%

“…In the sciatic nerve, aFGF levels decline proximal to a transection (Eckenstein et al, 1991;Piehl et al, 1993b1, and aFGF may be released from severed axons to promote regeneration (see also Cordeiro et al, 1989). After lesioningof motoneuron axons, GAP-43 expression increases in the parent cell bodies, both in the medulla oblongata and in the spinal cord (Redshaw and Bisby, 1984;Tetzlaff et al, 1991;Chong et al, 1992;Lindd et al, 1992;Piehl et al, 1993b). Recently, it was shown that in rat motoneurons subjected to chronic axotomy the mRNAs encoding for a-CGRP, aFGF, and GAP-43 return to normal levels after 5 months (Piehl et al, 1993b).…”

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confidence: 99%

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Increase in α‐CGRP and GAP‐43 in aged motoneurons: A study of peptides, growth factors, and ChAT mRNA in the lumbar spinal cord of senescent rats with symptoms of hindlimb incapacities

Johnson

Mossberg

Arvidsson

et al. 1995

J of Comparative Neurology

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Sprague-Dawley rats develop progressive motor dysfunctions during the third year of life. We use this as a model to examine possible neuronal mechanism(s) that may cause motor impairments occuring during aging. In this study we have used indirect immunofluorescence histochemistry (IF) and in situ hybridization histochemistry (ISH) to study quantitatively and qualitatively the staining pattern and mRNA expression of calcitonin gene-related peptide (alpha-CGRP), growth-associated protein 43 (GAP-43), and acidic fibroblast growth factor (aFGF) in spinal lumbar motoneurons of young adult (2-3 months) and aged (30 months) Sprague-Dawley rats. In addition, mRNAs encoding choline acetyltransferase (ChAT), beta-CGRP, and cholecystokinin (CCK) were analyzed. All aged rats used in this study disclosed symptoms of hindlimb incapacity, ranging from mild weight-bearing insufficiency to paralysis of the hind limbs. The symptoms were confined to the musculature of the hindlimb and hip regions. Only a small number (approximately 15%) of the large motoneurons that innervate the hindlimb muscles were lost in those aged rats that had clinical symptoms of hindlimb motor incapacities. The remaining motoneurons expressed ChAT mRNA at levels similar to those of young adult rats. The vast majority of these motoneurons showed increased mRNA levels for alpha-CGRP and GAP-43. Aged motoneurons contained more CGRP like immunoreactivity (LI), but the number of immunoreactive neurons was smaller than in adult rats. GAP-43-LI could be detected in motoneurons in aged, but not in adult, rats. GAP-43-LI was always colocalized with CGRP-LI in aged motoneurons. Studies of individual aged rats revealed that the increase of GAP-43 mRNA-positive cell bodies occurred in cases with the most severe clinical symptoms, whereas the increase in alpha-CGRP was even evident in rats with mild symptoms. No alterations in content of aFGF-LI or aFGF mRNA could be detected in the aged rat, and the content of CCK and beta-CGRP mRNAs was also normal. The usefulness of this rat model for studies of neuromuscular aging and possible functional roles for GAP-43 and CGRP in plastic and regenerative processes during aging are discussed.

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Section: Increased Levels Of Gap-43 In Aged Motoneurons Supplying Incmentioning

confidence: 99%

mentioning

confidence: 99%

Increase in α‐CGRP and GAP‐43 in aged motoneurons: A study of peptides, growth factors, and ChAT mRNA in the lumbar spinal cord of senescent rats with symptoms of hindlimb incapacities

Johnson

Mossberg

Arvidsson

et al. 1995

J of Comparative Neurology

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“…Extrinsic neurons, which are capable of regeneration, respond to axonal lesions with a variety of biochemical and morphological changes, commonly referred to as cell-body response or axonal reaction (for review, see Lieberman 197 1, 1974;Grafstein and McQuarrie, 1978;Kreutzberg, 1982;Barron, 1983aBarron, ,b, 1989Grafstein 1983Grafstein ,1986Tetzlaff et al, 1986). In regenerating extrinsic neurons and regenerating neurons of lower vertebrates, this cell-body response includes dramatic changes in cytoskeletal protein synthesis (Hall et al, 1978;Burrell et al, 1979;Hall, 1982;Quesada et al, 1986;Tesser et al, 1986;Greenberg and Lasek, 1988;Oblinger and Lasek, 1988;Tetzlaff et al, 1988) and cytoskeletal mRNA expression (Neumann et al, 1983;Hoffman et al, 1987;Wong and Oblinger, 1987;Goldstein et al, 1988;Hoffman and Cleveland, 1988;Hoffman, 1989;Miller et al, 1989;Oblinger et al, 1989;Muma et al, 1990;Verge et al, 1990b), as well as the expression of growth-associated proteins such as GAP-43 (Skene and Willard, 198 1;Redshaw and Bisby, 1984a;Bisby, 1988;Hoffman, 1989;Van der Zee et al, 1989;Verge et al, 1990a; for review, see Benowitz and Routtenberg, 1987;Skene, 1989). In contrast, most studies on intrinsic neurons of the mammalian CNS did not find an increased expression of GAP-43 after axotomy.…”

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confidence: 99%

Response of facial and rubrospinal neurons to axotomy: changes in mRNA expression for cytoskeletal proteins and GAP-43

et al. 1991

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Neurons confined within the mammalian CNS usually do not regenerate after axonal injury, while axonal regeneration is the rule in the PNS. It has been hypothesized that this may be related to differences in the microenvironment of the PNS versus CNS and to differences in the neuronal response to injury. In order to test the latter hypothesis, we compared changes in gene expression after axotomy in two populations of neurons: rat facial motoneurons and rat rubrospinal neurons. In situ hybridization with cDNA probes for the medium and light neurofilament protein revealed a reduced mRNA content in both facial and rubrospinal neurons at all times investigated (i.e., 1, 2, and 3 weeks after axotomy). On the other hand, mRNAs for actin and tubulin were increased in both neuronal populations during the first week after axotomy. While this increase was sustained in facial motoneurons for several weeks, total tubulin mRNA and actin mRNA were decreased in rubrospinal neurons at 2 and 3 weeks after axotomy, coincident with their atrophy. The developmentally regulated T alpha 1 tubulin mRNA, which was previously shown to be reexpressed in facial motoneurons after axotomy, was elevated severalfold in axotomized rubrospinal neurons, and increased levels persisted in some rubrospinal neurons as late as 7 weeks after axotomy. Similarly, the developmentally regulated GAP-43 mRNA increased in both axotomized facial and rubrospinal neurons, and increased levels were sustained in some axotomized rubrospinal neurons for at least 7 weeks. The response of rubrospinal neurons to axotomy in the cervical spinal cord is, in the first week, qualitatively similar to the response of facial motoneurons. However, by 2 weeks after axotomy there is a generalized reduction in mRNA levels for all three cytoskeletal proteins that is associated with neuronal atrophy. During this period, mRNA levels for the two specific markers of the growth state, T alpha 1 tubulin and GAP-43, remain elevated. Thus, axotomy of rubrospinal neurons appears to set in motion two independent events. First, an axotomy signal initiates a cell-body reaction similar to that of PNS neurons, including increased mRNA levels for T alpha 1 tubulin and GAP-43. Later, a generalized cellular atrophy and decrease in mRNA levels occur without reversing the specific responses of T alpha 1 and GAP-43 to axotomy. We conclude that the failure of rubrospinal neurons to regenerate is not due to a failure to initiate gene-expression changes characteristic of regenerating peripheral neurons.(ABSTRACT TRUNCATED AT 400 WORDS)

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“…We have recently found that the neuron-specific protein GAP-43 (also termed B-50, Fl, P57, or pp46) is present in axons and axonal growth cones but is not detectable in growing dendrites or dendritic growth cones of hippocampal neurons in culture (Goslin et al, 1988). Previous work has shown that the expression of GAP-43 is closely correlated with neurite growth, both during development and regeneration (Skene and Willard, 198 1 ac;Benowitz and Lewis, 1983;Redshaw and Bixby, 1984;Jacobson et al, 1986;Benowitz and Routtenberg, 1987;Skene, 1989). GAP-43 is a prominent protein component of growth cones, the motile tips of elongating neurites, comprising approximately 1 Yo of the total protein of growth cone membranes (Meiri et al, 1986(Meiri et al, , 1988Skene et al, 1986).…”

mentioning

confidence: 99%

Changes in the distribution of GAP-43 during the development of neuronal polarity

et al. 1990

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GAP-43, a neuron specific growth-associated protein, is selectively distributed to the axonal domain in developing neurons; it is absent from dendrites and their growth cones. Using immunofluorescence microscopy, we have further examined the distribution of GAP-43 during the development of hippocampal neurons in culture, in order to determine when this polarized distribution arises. Cultured hippocampal neurons initially extend several short processes which have the potential to become either axons or dendrites. At this stage, before the morphological expression of polarity, GAP-43 is concentrated in the growth cones of these processes but is distributed more or less equally among them. Polarity becomes established when one of these processes elongates to become the axon. At the earliest stage when the emerging axon can be identified, GAP-43 is preferentially concentrated in its growth cone. During the next few days, as the remaining processes take on dendritic properties, they lose their residual GAP-43 immunoreactivity. Throughout development, GAP-43 remains highly concentrated in the axonal growth cone, but the concentration of GAP-43 in the axon shaft increases, beginning near the growth cone and progressing proximally until GAP-43 is uniformly distributed along the entire axon. At all stages of development, GAP-43 is also concentrated in the region of the Golgi apparatus. These results suggest that the selective sorting of at least one membrane protein into the axon coincides with the morphological expression of polarity. These results also raise the possibility that GAP-43 may play an important role in the early phases of axonal outgrowth, by which the functional polarity of neurons is established.

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Proteins of fast axonal transport in the regenerating hypoglossal nerve of the rat

Cited by 33 publications

References 9 publications

Increase in α‐CGRP and GAP‐43 in aged motoneurons: A study of peptides, growth factors, and ChAT mRNA in the lumbar spinal cord of senescent rats with symptoms of hindlimb incapacities

Increase in α‐CGRP and GAP‐43 in aged motoneurons: A study of peptides, growth factors, and ChAT mRNA in the lumbar spinal cord of senescent rats with symptoms of hindlimb incapacities

Response of facial and rubrospinal neurons to axotomy: changes in mRNA expression for cytoskeletal proteins and GAP-43

Changes in the distribution of GAP-43 during the development of neuronal polarity

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