Altered expression and changing distribution of the nerve growth associated protein GAP-43 during ocular HSV-1 infection in the rabbit

References

• Alexander K A, Cimler B M, Meiri K E, Stonn D R. Regulation of calmodulin binding to P-57. J Biol Chem 1987; 262: 6108–6113
   PubMedGoogle Scholar
• Andreassen T J, Luetje C W, Heideman W, Storm D R. Purification of a novel calmodulin binding protein from bovine cerebral cortex membranes. Biochemistry 1983; 22: 4615–4618
   Google Scholar
• Benowitz L I, Perrone-Bizzozero N I, Finklestein S P, Bird E D. Localization of the growth-associated phosphoprotein GAP-43 (B-50, Fl) in the human cerebral cortex. J. Neurosci 1989; 9: 990–995
   Google Scholar
• Beyer C F, Tepper D J, Hill J M. Cryogenic induced ocular HSV-1 reactivation is enhanced by an inhibitor of the lipoxygenase pathway. Curr Eye Res 1989; 8: 1287–1292
   PubMed Web of Science ®Google Scholar
• Beyer C F, Hill J M, Reidi J J, Beuerman R W. Corneal nerve disruption reactivates virus in rabbits latently infected with HSV-1. Invest Ophthal Vis Sci 1990; 31: 925–932
   PubMed Web of Science ®Google Scholar
• Bloom D C, Devi-Rao G B, Hill J M, Stevens J G, Wagner E K. Molecular analysis of herpes simplex virus type-1 during epinephrine-induced reactivation of latently infected rabbits. J. Virol 1994; 68: 1283–1292
   Google Scholar
• Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72: 248–254
   PubMed Web of Science ®Google Scholar
• Burnette W N. Western blotting: electrophoretic transfer of proteins from sodiumdodecyl sulfate polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal Biochem 1981; 112: 195–203
   PubMed Web of Science ®Google Scholar
• Chao H M, McEwen B S. Glucocorticoids and the expression of mRNAs for neurotrophins, their receptors and GAP-43 in the rat hippocampus. Mol Brain Res 1994; 26: 271–276
   PubMedGoogle Scholar
• Coggins P J, Zwiers H. B-50 (GAP-43): Biochemical and functional neurochemistry of a neuron specific phosphoprotein. J. Neurochem 1991; 56: 1095–1106
   Google Scholar
• Coggins P J, McLean K, Nagy A, Zwiers H. ADP-ribosylation of the neuronal phosphoprotein B-50/GAP-43. J. Neurochem 1993; 60: 368–371
   Google Scholar
• Costello B, Meymandi A, Freeman J A. Factors influencing GAP-43 gene expression in PC12 pheochromocytoma cells. J. Neurosci 1990; 10: 1398–1406
   PubMed Web of Science ®Google Scholar
• Dorster K S, Lozano A M, Aguayo A J, Willard M B. Expression of the adult rat growth associated protein GAP-43 in adult rat ganglion cells following axon injury. Neuron 1991; 6: 635–647
   Google Scholar
• Erzurumlu R S, Jhavery S, Moya K L, Benowitz L I. Peripheral nerve regeneration induces elevated expression of GAP-43 in the brain stem trigeminal complex of adult hamsters. Brain Res 1989; 498: 135–139
   PubMed Web of Science ®Google Scholar
• Fawl R L, Roizman B. The molecular basis of herpes simplex virus pathogenicity. Semin Virol 1994; 5: 261–271
   Web of Science ®Google Scholar
• Federoff H J, Grabczyk E, Fishman M C. Dual regulation of GAP-43 gene expression and by nerve growth factor and glucocorticoids. J. Biol Chem 1988; 263: 19290–19295
   PubMedGoogle Scholar
• Fishman M C, Valenzuela D. GAP-43 and neuronal remodeling. Prog Brain Res 1991; 89: 89–95
   Google Scholar
• Gato S, Yamada K, Inoue N, Nagahiro S, Ushio Y. Increased expression of the growth associated protein GAP-43/B-50 following cerebral hemitransection or striatal injury in the substantia nigra of adult rats. Brain Res 1994; 647: 333–339
   Google Scholar
• Gispen W H. Neuronal plasticity and function. Clin Neuropharmacol 1993; 16 (suppl. 1): S5–S11
   Google Scholar
• Goslin K, Banker G. Rapid changes in the distribution of GAP-43 correlate with the expression of neuronal polarity during normal development and under experimental conditions. J. Cell Biol 1990; 110: 1319–1331
   PubMed Web of Science ®Google Scholar
• Haruta Y, Rootman D S, Xie L, Kiritoshi A, Hill J M. Recurrent HSV corneal lesions induced by cyclophosphamide and dexamethasone. Invest Ophthal Vis Sci 1989; 30: 371–376
   PubMed Web of Science ®Google Scholar
• Henken D B, Goldstein M E, Zhang Q-I, Curtis R. Neuronal sprouting in mouse sensory ganglia infected with herpes simplex virus type 2 (HSV-2): induction of growth-associated protein (GAP-43) and ultrastructural evidence. J. Neuro Virol 1995; 1: 157–164
   Web of Science ®Google Scholar
• Hens J JH, DeWit D, Dekker L V, Boomsma F, Oestreicher A B, Margolis F, Gispen W H, De Graan P NE. Studies on the role of B-50 (GAP-43) in the mechanism of Ca2+-induced noradrenaline release: lack of involvement of protein kinase C after the Ca2+ trigger. J Neurochem 1993; 60: 1264–1273
   Google Scholar
• Hill J M, Helmy M F, Osborne P A, Johnson E M, jr, Gebhardt B M. Antibody to nerve growth factor induce HSV-1 ocular shedding in latently infected rabbits. Invest Ophthal Vis Sci 1992; 31 (suppl): 314
   Google Scholar
• Hoffman P N. Expression of GAP-43, a rapidly transported growth-associated protein, and class II beta tubulin, a slowly transported cytoskeletal protein are coordinated in regenerating neurons. J. Neurosci 1989; 9: 893–897
   PubMedGoogle Scholar
• Jacobson R D, Virag I, Skene J HP. A protein associated with axon growth, GAP-43, is widely distributed and developmentally regulated in rat CNS. J. Neurosic 1986; 6: 1843–1855
   PubMedGoogle Scholar
• Jolles J, Zwiers H, Van Dongen C J, Schotman P, Wirtz K WA, Gispen W H. Modulation of brain polyphosphoinositide metabolism by ACTH-sensitive protein phosphorylation. Nature 1980; 268: 623–625
   Google Scholar
• Kaufman H E, Rayfield M A. Viral conjunctivitis and keratitis. The Cornea., H E Kaufman, M B McDonald, B A Barron, S R Waltman. Churchill Livingstone, New York 1988; 299–331
   Google Scholar
• Kennedy P GE, Steiner I. A molecular and cellular model to explain the differences in reactivation from latency by herpes simplex and varicella-zoster viruses. Neuropathol Appl Neurobiol 1994; 20: 368–374
   Google Scholar
• Lamelli U K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685
   PubMed Web of Science ®Google Scholar
• Martin R E, Bazan N G. Growth-associated protein GAP-43 and nerve cell adhesion molecule in sensory nerves of cornea. Exp Eye Res 1992; 55: 307–314
   PubMed Web of Science ®Google Scholar
• Martin R E, Henken D B, Hill J M. Herpes simplex virus (HSV-1) infection increases nerve growth-associated protein (GAP-43/B-50) immunoreactivity in rabbit cornea and trigeminal ganglion (TG). Soc Neurosci Abst 1994; 20(2)1259
   Google Scholar
• Martin R E, Hill J M, Bazan N G. Viral latency and GAP-43: changing enrichment of a growth associated protein in wound healing and viral infection. Soc Neurosci Abst 1992; 18: 236
   Google Scholar
• Meiri K F, Willard M, Johnson M I. Distribution and phosphorylation of the growth-associated protein GAP-43 in regenerating sympathetic neurons in culture. J Neurosci 1988; 8: 2571–2581
   Web of Science ®Google Scholar
• Neve R L, Finch E D, Bird E D, Benowitz L I. Growth associated protein is expressed selectively in associative regions of adult human brain. Proc Natl Acad Sci USA 1988; 85: 3638–3642
   PubMedGoogle Scholar
• Reinhard E, Skene P. Multiple elements may be used for regulation of the GAP-43 gene in different cell types. Perspect Dev Neurobiol 1982; 1: 29–37
   Google Scholar
• Rivera L, Beuerman R W, Hill J M. Corneal nerves contain intraaxonal HSV-1 after virus reactivation by epinephrine iontophoresis. Curr Eye Res 1988; 10: 1001–1008
   Google Scholar
• Roizman B, Sears A E. Herpes simplex viruses and their replication. Fundamental Virology, second edition., B N Fields, D M Knipe, R M Chanock, R S Hirsch, J L Melnick, T P Monath, B Roizman. Raven Press, New York 1991; 849–895
   Google Scholar
• Rózsa A J, Beuerman R W. Density and organization of free nerve endings in the corneal epithelium of the rabbit. Pain 1982; 14: 105–120
   PubMed Web of Science ®Google Scholar
• Rózsa A J, Guss R B, Beuerman R W. Neural remodeling following experimental surgery of the rabbit cornea. Invest Ophthal Vis Sci 1983; 24: 1033–1051
   PubMed Web of Science ®Google Scholar
• Schreyer D, Skene J HP. Fate of GAP-43 in ascending spinal axons of DRG neurons after peripheral nerve injury: delayed accumulation and correlation with regenerative potential. J. Neurosci 1991; 11: 3738–3751
   PubMed Web of Science ®Google Scholar
• Skene J HP, Willard M. Changes in axonally transported proteins during regeneration in toad retinal ganglion cells. J. Cell Biol 1981a; 89: 86–95
   PubMed Web of Science ®Google Scholar
• Skene J HP, Willard M. Axonally transported proteins associated with axon growth in rabbit central and peripheral nervous systems. J. Cell Biol 1981b; 89: 96–103
   PubMed Web of Science ®Google Scholar
• Stevens J G. Overview of herpesvirus latency. Virology 1994; 5: 191–196
   Google Scholar
• Stewart H JS, Cowen T, Curtis R, Wilkin G P, Mirsky R, Jessen K R. GAP-43 immunoreactivity is widespread in the autonomic neurons and sensory neurons of the rat. Neuroscience 1992; 47: 673–684
   Google Scholar
• Strittmatter S M, VaJenzuela D, Sudo Y, Linder M E, Fishman M C. An intracellular guanine nucleotide release protein for G0 GAP-43 stimulates isolated a-subunits by a novel mechanism. J. Biol Chem 1991; 266: 22465–22471
   PubMed Web of Science ®Google Scholar
• Stroop W G, Schaefer D C. Production of encephalitis restricted to the temporal lobes by experimental reactivation of herpes simplex virus. J. Infect Dis 1986; 28: 721–731
   Google Scholar
• Stroop W G, Schaefer D C. Severity of experimentally reactivated herpetic eye disease is related to the neurovirulence of the latent virus. Invest Ophthalmol Vis Sci 1987; 28: 229–237
   PubMed Web of Science ®Google Scholar
• Tetzlaff W, Zwiers H, Lederis K, Cassar L, Bisby M A. Axonal transport and localization of B-50/GAP-43-like immunoreactivity in the regenerating sciatic and facial nerves of the rat. J. Neurosci 1989; 94: 1303–1313
   Google Scholar