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Molecular Interactions Modulating Neuronal Survival and Growth

Published online by Cambridge University Press:  18 September 2015

R.J. Riopelle ,
K.E. Dow ,
V.M.K. Verge  and
P.M. Richardson
R.J. Riopelle*
Affiliation:
Department of Medicine, Queen's University, Kingston
K.E. Dow
Affiliation:
Department of Pediatrics, Queen's University, Kingston
V.M.K. Verge
Affiliation:
Department of Surgery, McGill University, Montreal
P.M. Richardson
Affiliation:
Department of Surgery, McGill University, Montreal
*
Apps Medical Research Centre, Kingston General Hospital, Kingston, Ontario, Canada K7L 2V7
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Abstract:

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The extracellular environment of the neuron provides a heterogeneous milieu of survival and growth modulating molecular species subserving regulatory signals that operate in development, meditate activity-dependent enduring changes in synaptic connectivity, and promote or inhibit survival and axonal regeneration following insult. Parallel distributed processing networks in neurons, activated by these molecular species, can likely be recruited selectively to serve specific needs of the organism.

Type
Research Article
Information
Canadian Journal of Neurological Sciences , Volume 18 , Issue S3 , August 1991 , pp. 398 - 402
Copyright
Copyright © Canadian Neurological Sciences Federation 1991

References

REFERENCES

1.Caroni, P, Schwab, ME. Two membrane protein fractions from rat central myelin with inhibitory properties for neurite growth and fibroblast spreading. J Cell Biol 1988; 106: 1281–1288.CrossRefGoogle ScholarPubMed
2.Barde, Y-A. Trophic factors and neuronal survival. Neuron 1989; 2: 1525–1534.CrossRefGoogle ScholarPubMed
3.Lipton, SA, Kater, SB. Neurotransmitter regulation of neuronal out–growth, plasticity and survival. TINS 1989; 12: 265–270.Google Scholar
4.Ayer-LeLievre, C, Olson, L, Ebendal, T, et al. Expression of the beta-nerve growth factor gene in hippocampal neurons. Science 1988; 240: 1339–1341.CrossRefGoogle ScholarPubMed
5.Dow, KE, Mirski, SEL, Roder, JC, et al. Neuronal proteoglycans: Biosynthesis and functional interaction with neurons in vitro. J Neurosci 1988; 8: 3278–289.CrossRefGoogle ScholarPubMed
6.Riopelle, RJ, Dow, KE. Functional interactions of neuronal heparin sulphate proteoglycans with laminin. Brain Res 1990; 52: 92–100.CrossRefGoogle Scholar
7.Tomaselli, KJ, Reichardt, LEIntegrine, cadherins, and cell adhesion molecules of the immunoglobulin superfamily: Neuronal receptors that regulate axon growth and guidance. The Assembly In: Landmesser, Lynn T. ed. The Assembly of the Nervous System. Alan R Liss Ine, 1989: 81–108.Google Scholar
8.Martin, GR, Timpl, R. Laminin and other basement membrane com-ponents. Ann Rev Cell Biol 1987; 3: 57–85.CrossRefGoogle Scholar
9.Nybroe, O, Moran, N, Bock, E. Equilibrium binding analysis of neu-ral cell adhesion molecule binding to heparin. J Neurochem 1989; 52: 1947–1949.CrossRefGoogle Scholar
10.Cole, GJ, Akeson, R. Identification of a heparin binding domain of the neural cell adhesion molecule N-CAM using synthetic peptides. Neuron 1989; 2: 1157–1165.CrossRefGoogle ScholarPubMed
11.Jessell, T. Adhesion molecules and the hierarchy of neural develop-ment. Neuron 1988; 1: 3–13.CrossRefGoogle Scholar
12.Matsunaga, M, Hatta, K, Nagafuchi, A, et al. Guidance of optic nerve fibers by N-cadherin adhesion molecules. Nature 1988; 334: 62–64.CrossRefGoogle ScholarPubMed
13.Hoffman, S, Crossin, KL, Edelman, GM. Molecular forms, binding functions, and developmental expression patterns of cytotactin and cytotactin-binding proteoglycan, an interactive pair of extracellular matrix molecules. J Cell Biol 1988; 106: 519–532.CrossRefGoogle ScholarPubMed
14.Pittman, RN. Release of plasminogen activator and a calcium-dependent metalloprotease from cultured sympathetic and sensory neurons. Dev Biol 1985; 110: 91–101.CrossRefGoogle Scholar
15.Pittman, RN, Williams, AG. Neurite penetration into collagen gels requires Ca++-dependent metalloproteinase activity. Dev Neurosci 1989; 11: 41–51.CrossRefGoogle Scholar
16.Monard, D. Cell derived proteases and protease inhibitors as regula-tors of neurite outgrowth. TINS 1988; 11: 541–544.Google ScholarPubMed
17.Riopelle, RJ, Dow, KE. Neurite formation on laminin: effects of a galactosyltransferase on primary sensory neurons. Brain Research 1991; 541: 265–272.CrossRefGoogle ScholarPubMed
18.Begovac, PC, Shur, BD. Cell surface galacotsyltransferase mediates the initiation of neurite outgrowth from PC 12 cells on laminin. J Cell Biol 1990; 110: 461–470.CrossRefGoogle Scholar
19.Schwab, ME, Otten, U, Agid, Y, et al. Nerve growth factor (NGF) in the rate CNS: absence of specific retrograde axonal transport and tyrosine hydroxylase induction in locus coeruleus and substantia nigra. Brain Res 1979; 168: 473–483.CrossRefGoogle Scholar
20.Richardson, PM, Riopelle, RJ. Uptake of nerve growth factor along peripheral and spinal axons of primary sensory neurons. J Neurosci 1984; 4: 1683–1689.CrossRefGoogle ScholarPubMed
21.Large, T, Weskamp, G, Helder, JC, et al. Structure and developmen-tal expression of the Nerve Growth Factor receptor in the chicken central nervous system. Neuron 1989; 2: 1123–1134.CrossRefGoogle Scholar
22.Bar Sagi, D, Feramisco, JR. Microinjection of the ras oncogene pro-tein into PC 12 cells induces morphological differentiation. Cell 1985; 42: 841–843.CrossRefGoogle Scholar
23.Hagag, N, Halegoua, S, Viola, M. Inhibition of growth factor-induced differentiation of PC 12 cells by microinjection of antibody to ras p21. Nature 1986; 319: 680–682.CrossRefGoogle Scholar
24.Borasio, GD, John, J, Wittinghofer, A, et al. ras p21 protein promotes survival and fiber outgrowth of cultured embryonic neurons. Neuron 1989; 2: 1087–1096.CrossRefGoogle ScholarPubMed
25.Richardson, PM, Verge Issa, VMK, Riopelle, RJ. Distribution of neu-ronal receptors for nerve growth factor in the rat. J Neurosci 1985; 6: 2312–2321.CrossRefGoogle Scholar
26.Hagg, T, Manfhorpe, M, Vahlsing, HL, et al. Delayed treatment with nerve growth factor reverses the apparent loss of cholinergic neurons after acute brain damage. Exp Neuol 1988; 101: 303–312.CrossRefGoogle ScholarPubMed
27.Vantini, G, Schiavo, N, DiMartino, A, et al. Evidence for a physio-logical role of Nerve Growth Factor in the central nervous system of neonatal rats. Neurons 1989; 3: 267–273.CrossRefGoogle Scholar
28.Verge, VMK, Richardson, PM, Benoit, R, et al. Histochemical char-acterization of sensory neurons with high-affinity receptors for nerve growth factor. J Neurocytol 1990; 18: 583–591.CrossRefGoogle Scholar
29.Verge, VMK, Riopelle, RJ, Richardson, PM. Nerve Growth Factor receptors on normal injured sensory neurons. J Neurosci 1989; 9: 914–922.CrossRefGoogle ScholarPubMed
30.Diamond, J, Coughlin, M, Macintrye, L, et al. Evidence that endoge-neous ? nerve growth factor is responsible for the collateral sprouting, but not the regeneration, of nociceptive axons in adult rats. Proc Natl Acad Sci USÅ 1987; 84: 6596–6600.CrossRefGoogle Scholar
31.Heumann, R, Korsching, S, Bandtlow, C, et al. Changes of nerve growth factor synthesis in nonneuronal cells in response to sciatic nerve transection. J Cell Biol 1987; 104: 1623–1631.CrossRefGoogle ScholarPubMed
32.Nelson, RB, Linden, DJ, Hyman, C, et al. The two major phospho-proteins in growth cones are probably identical to two protein kinase C substrates correlated with persistence of long-term potentation. J Neurosci 1989; 9: 381–389.CrossRefGoogle Scholar
33.Halpain, S, Girault, J-A, Greengard, P. Activation of NMDA recep-tors induces dephosphorylation of the cytoskeletal protein MAP2. Neuron 1990; 5: 237–246.CrossRefGoogle Scholar
34.Desmond, NL, Levy, WB. Synaptic correlates of associative poten-tation/depression an ultrastructural study in the hippocampus. Brain Res 1983; 265: 21–30.CrossRefGoogle ScholarPubMed
35.Chang, F-L, Greenough, WT. Transient and enduring morphological correlates of synaptic activity and efficacy change in the rat hip-pocampal slice. Brain Res 1984; 309: 35–46.CrossRefGoogle Scholar
36.Linden, DJ, Wong, KL, Sheu, F-S, et al. NMDA receptor blockade prevents the increase in protein kinase C substrate (protein Fl) phosphorylation produced by long-term potentiation. Brain Res 1988; 458: 142–146.CrossRefGoogle Scholar
37.Coughlin, C, Elam, JS. Enhanced axonal transport of glycosamino-glycans in regenerating goldfish optic nerve. Brain Res 1989; 493: 326–330.CrossRefGoogle Scholar
38.Dow, KE, Levine, R, Sole, M, et al. Proteoglycan transport in regen-erating goldfish retinotectal projection. Soc for Neuroscience Abstracts 1990; 16: 170.Google Scholar
39.Grafstein, B. The retina as a regenerating organ. In: Adler, R, Farber, D, eds. The Retina: A Model for Cell Biology Studies, Part II. Toronto: Academic Press Inc., 1986: 275–335.CrossRefGoogle Scholar
40.Larrivee, DC, Grafstein, B. Relationship between phosphorylation synthesis of goldfish optic nerve proteins during regeneration. J Neurosci 1989; 9: 574–581.CrossRefGoogle ScholarPubMed
41.Bray, D, Hollenbeck, PJ. Growth cone motility and guidance. Ann Rev Cell Biol 1988; 4: 43–61.CrossRefGoogle ScholarPubMed
42.Bray, D, Vasiliev, J. Networks from mutants. Nature 1989. 338: 203–204.CrossRefGoogle ScholarPubMed
43.Hohn, A, Leibrock, J. et al. Identification and characterization of a novel member of the nerve growth factor/brain-derived neurotrophic factor family. Nature 1990. 344: 339–341.CrossRefGoogle ScholarPubMed