The knocking down of the oncoprotein Golgi phosphoprotein 3 in T98G cells of glioblastoma multiforme disrupts cell migration by affecting focal adhesion dynamics in a focal adhesion kinase-dependent manner
Author
dc.contributor.author
Arriagada, Cecilia
Author
dc.contributor.author
Luchsinger, Charlotte
Author
dc.contributor.author
González, Alexis E.
Author
dc.contributor.author
Schwenke, Tomás
Author
dc.contributor.author
Arriagada, Gloria
Author
dc.contributor.author
Folch, Hugo
Author
dc.contributor.author
Ehrenfeld, Pamela
Author
dc.contributor.author
Burgos, Patricia V.
Author
dc.contributor.author
Mardones, Gonzalo A.
Admission date
dc.date.accessioned
2019-10-15T12:25:24Z
Available date
dc.date.available
2019-10-15T12:25:24Z
Publication date
dc.date.issued
2019
Cita de ítem
dc.identifier.citation
PLoS ONE, Volumen 14, Issue 2, 2019,
Identifier
dc.identifier.issn
19326203
Identifier
dc.identifier.other
10.1371/journal.pone.0212321
Identifier
dc.identifier.uri
https://repositorio.uchile.cl/handle/2250/171677
Abstract
dc.description.abstract
Golgi phosphoprotein 3 (GOLPH3) is a conserved protein of the Golgi apparatus that in humans has been implicated in tumorigenesis. However, the precise function of GOLPH3 in malignant transformation is still unknown. Nevertheless, clinicopathological data shows that in more than a dozen kinds of cancer, including gliomas, GOLPH3 could be found overexpressed, which correlates with poor prognosis. Experimental data shows that overexpression of GOLPH3 leads to transformation of primary cells and to tumor growth enhancement. Conversely, the knocking down of GOLPH3 in GOLPH3-overexpressing tumor cells reduces tumorigenic features, such as cell proliferation and cell migration and invasion. The cumulative evidence indicate that GOLPH3 i
Biochemistry, Genetics and Molecular Biology (all)
Keywords
dc.subject
Agricultural and Biological Sciences (all)
Título
dc.title
The knocking down of the oncoprotein Golgi phosphoprotein 3 in T98G cells of glioblastoma multiforme disrupts cell migration by affecting focal adhesion dynamics in a focal adhesion kinase-dependent manner