Cellular Migration Ability Is Modulated by Extracellular Purines in Ovarian Carcinoma SKOV-3 Cells
Por:
Martínez-Ramírez A.S., Díaz-Muñoz M., Battastini A.M., Campos-Contreras A., Olvera A., Bergamin L., Glaser T., Jacintho Moritz C.E., Ulrich H., Vázquez-Cuevas F.G.
Publicada:
1 dic 2017
Resumen:
Extracellular nucleotides and nucleosides have emerged as important
elements regulating tissue homeostasis. Acting through specific
receptors, have the ability to control gene expression patterns to
direct cellular fate. We observed that SKOV-3 cells express the
ectonucleotidases: ectonucleotide pyrophosphatase 1 (ENPP1),
ecto-5-nucleotidase (NT5E), and liver alkaline phosphatase (ALPL).
Strikingly, in pulse and chase experiments supplemented with ATP, SKOV-3
cells exhibited low catabolic efficiency in the conversion of ADP into
AMP, but they were efficient in converting AMP into adenosine. Since
these cells release ATP, we proposed that the conversion of ADP into AMP
is a regulatory node associated with the migratory ability and the
mesenchymal characteristics shown by SKOV-3 cells under basal
conditions. The landscape of gene expression profiles of SKOV-3 cell
cultures treated with apyrase or adenosine demonstrated similarities
(e.g., decrease FGF16 transcript) and differences (e.g., the negative
regulation of Wnt 2, and 10B by adenosine). Thus, in SKOV-3 we analyzed
the migratory ability and the expression of epithelium to mesenchymal
transition (EMT) markers in response to apyrase. Apyrase-treatment
favored the epithelial-like phenotype, as revealed by the re-location of
E-cadherin to the cell to cell junctions. Pharmacological approaches
strongly suggested that the effect of Apyrase involved the accumulation
of extracellular adenosine; this notion was strengthened when the
incubation of the SKOV-3 cell with ,-methylene ADP (CD73 inhibitor) or
adenosine deaminase was sufficient to abolish the effect of apyrase on
cell migration. Overall, adenosine signaling is a fine tune mechanism in
the control of cell phenotype in cancer. J. Cell. Biochem. 118:
4468-4478, 2017. (c) 2017 Wiley Periodicals, Inc.
Filiaciones:
Martínez-Ramírez A.S.:
Departamento de Neurobiología Celular y Molecular, Instituto de Neurobiología, Universidad Nacional Autónoma de México, Boulevard Juriquilla 3001, Juriquilla Querétaro, Querétaro CP 76230, Mexico
Díaz-Muñoz M.:
Departamento de Neurobiología Celular y Molecular, Instituto de Neurobiología, Universidad Nacional Autónoma de México, Boulevard Juriquilla 3001, Juriquilla Querétaro, Querétaro CP 76230, Mexico
Battastini A.M.:
Departamento de Bioquímica, Instituto de Ciências Básicas e da Saúde, UFRGS, Porto Alegre, RS, Brazil
Campos-Contreras A.:
Departamento de Neurobiología Celular y Molecular, Instituto de Neurobiología, Universidad Nacional Autónoma de México, Boulevard Juriquilla 3001, Juriquilla Querétaro, Querétaro CP 76230, Mexico
Olvera A.:
Departamento de Neurobiología Celular y Molecular, Instituto de Neurobiología, Universidad Nacional Autónoma de México, Boulevard Juriquilla 3001, Juriquilla Querétaro, Querétaro CP 76230, Mexico
Bergamin L.:
Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, Av. Prof. Lineu Prestes 748Sao Paulo 05508-900, Brazil
Glaser T.:
Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, Av. Prof. Lineu Prestes 748Sao Paulo 05508-900, Brazil
Jacintho Moritz C.E.:
Departamento de Bioquímica, Instituto de Ciências Básicas e da Saúde, UFRGS, Porto Alegre, RS, Brazil
Ulrich H.:
Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, Av. Prof. Lineu Prestes 748Sao Paulo 05508-900, Brazil
Vázquez-Cuevas F.G.:
Departamento de Neurobiología Celular y Molecular, Instituto de Neurobiología, Universidad Nacional Autónoma de México, Boulevard Juriquilla 3001, Juriquilla Querétaro, Querétaro CP 76230, Mexico
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