Alteration of tyrosine hydroxylase activity in PC12 cells infected with herpes simplex virus type 1 Journal Article


Authors: Rubenstein, R.; Price, R. W.; Joh, T.
Article Title: Alteration of tyrosine hydroxylase activity in PC12 cells infected with herpes simplex virus type 1
Abstract: During infection with herpes simplex virus type 1 (HSV-1) the activity of tyrosine hydroxylase (TH) in PC 12 pheochromocytoma cells was initially depressed reaching a nadir at 6 hours post-inoculation, but recovered rapidly with a return to baseline activity by 8 to 9 hours post-inoculation. Subsequently, TH activity again fell with a second more variable rise in activity occurring at 24 hours post-inoculation. Studies with metabolic inhibitors and 2 temperature-sensitive viral mutants indicated that these alterations of TH activity were dissociated from morphological cytopathology and likely required expression of "late" viral gene products. Immunotitration using anti-TH antibody suggested that early depression of TH activity resulted principally from loss of enzyme protein rather than simple enzyme inactivation, and that reconstitution of activity at 9 hours was related to augmented enzyme synthesis. These observations illustrate the complexity of perturbed cellular metabolism during HSV-1 infection and suggest involvement of two unexpected processes: alteration of a specialized cell function as a result of viral genes expressed late in the replicative cycle, and augmented synthesis of a cell-coded gene product during the course of infection. © 1985 Springer-Verlag.
Keywords: nonhuman; cells, cultured; in vitro study; time factors; gene expression regulation; cell culture; tyrosine 3 monooxygenase; simplexvirus; dactinomycin; virus infection; ultraviolet rays; pheochromocytoma; herpes simplex virus 1; cycloheximide; immunologic techniques; temperature sensitive mutant; tyrosine 3-monooxygenase; human; priority journal; support, non-u.s. gov't; support, u.s. gov't, p.h.s.
Journal Title: Archives of Virology
Volume: 83
Issue: 1-2
ISSN: 0304-8608
Publisher: Springer  
Date Published: 1985-03-01
Start Page: 65
End Page: 82
Language: English
DOI: 10.1007/bf01310965
PUBMED: 2857560
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 26 October 2021 -- Source: Scopus
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  1. Richard W. Price
    58 Price