Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/57717
Title: Expression of Tyrosine Hydroxylase is Negatively Regulated Via Prion Protein
Authors: Mello da Luz, Marcio Henrique [UNIFESP]
Glezer, Isaias [UNIFESP]
Xavier, Andre Machado [UNIFESP]
Paiva da Silva, Marcelo Alberti [UNIFESP]
Monteiro, Jessica [UNIFESP]
Pino, Volejnik [UNIFESP]
Zamith, Thiago Panaro [UNIFESP]
Vieira, Taynara Fernanda [UNIFESP]
Antonio, Bruno Brito [UNIFESP]
Moreira Antunes, Hanna Karen [UNIFESP]
Martins, Vilma Regina
Lee, Kil Sun [UNIFESP]
Keywords: Cellular prion protein
Dopamine metabolism
Tyrosine hydroxylase
Gene expression
Issue Date: 2016
Publisher: Springer/Plenum Publishers
Citation: Neurochemical Research. New York, v. 41, n. 7, p. 1691-1699, 2016.
Abstract: Cellular prion protein (PrPC) is a glycoprotein of the plasma membrane that plays pleiotropic functions by interacting with multiple signaling complexes at the cell surface. Recently, a number of studies have reported the involvement of PrPC in dopamine metabolism and signaling, including its interactions with tyrosine hydroxylase (TH) and dopamine receptors. However, the outcomes reported by independent studies are still debatable. Therefore in this study, we investigated the effects of PrPC on the TH expression during the differentiation of N2a cells with dibutyryl-cAMP, a well-known cAMP analog that activates TH transcription. Upon differentiation, TH was induced with concomitant reduction of PrPC at protein level, but not at mRNA level. shRNA-mediated PrPC reduction increased the basal level of TH at both mRNA and protein levels without dibutyryl-cAMP treatment. This phenotype was reversed by re-expression of PrPC. PrPC knockdown also potentiated the effect of dibutyryl-cAMP on TH expression. Our findings suggest that PrPC has suppressive effects on TH expression. As a consequence, altered PrPC functions may affect the regulation of dopamine metabolism and related neurological disorders.
URI: https://repositorio.unifesp.br/handle/11600/57717
ISSN: 0364-3190
Other Identifiers: http://dx.doi.org/10.1007/s11064-016-1885-1
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