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Ectonucleotidase activity driven by acid ectophosphatase in luminal A MCF-7 breast cancer cells.
Lacerda-Abreu, Marco Antonio; Mendonça, Bruna Dos Santos; Nestal de Moraes, Gabriela; Meyer-Fernandes, José Roberto.
Affiliation
  • Lacerda-Abreu MA; Instituto de Bioquímica Médica Leopoldo De Meis, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil.
  • Mendonça BDS; Instituto de Bioquímica Médica Leopoldo De Meis, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil.
  • Nestal de Moraes G; Instituto de Bioquímica Médica Leopoldo De Meis, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil.
  • Meyer-Fernandes JR; Instituto de Bioquímica Médica Leopoldo De Meis, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil.
Cell Biol Int ; 48(11): 1637-1648, 2024 Nov.
Article in En | MEDLINE | ID: mdl-39285521
ABSTRACT
Ectophosphatases catalyse the hydrolysis of phosphorylated molecules, such as phospho-amino acids, in the extracellular environment. Nevertheless, the hydrolysis of nucleotides in the extracellular environment is typically catalysed by ectonucleotidases. Studies have shown that acid ectophosphatase, or transmembrane-prostatic acid phosphatase (TM-PAP), a membrane-bound splice variant of prostatic acid phosphatase, has ecto-5'-nucleotidase activity. Furthermore, it was demonstrated that ectophosphatase cannot hydrolyse ATP, ADP, or AMP in triple-negative breast cancer cells. In contrast to previous findings in MDA-MB-231 cells, the ectophosphatase studied in the present work displayed a remarkable capacity to hydrolyse AMP in luminal A breast cancer cells (MCF-7). We showed that AMP dose-dependently inhibited p-nitrophenylphosphate (p-NPP) hydrolysis. The p-NPP and AMP hydrolysis showed similar biochemical behaviours, such as increased hydrolysis under acidic conditions and comparable inhibition by NiCl2, ammonium molybdate, and sodium orthovanadate. In addition, this ectophosphatase with ectonucleotidase activity was essential for the release of adenosine and inorganic phosphate from phosphorylated molecules available in the extracellular microenvironment. This is the first study to show that prostatic acid phosphatase on the membrane surface of breast cancer cells (MCF-7) is correlated with cell adhesion and migration.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Acid Phosphatase / Breast Neoplasms Limits: Female / Humans Language: En Journal: Cell Biol Int Year: 2024 Document type: Article Affiliation country: Brazil Country of publication: United kingdom

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Acid Phosphatase / Breast Neoplasms Limits: Female / Humans Language: En Journal: Cell Biol Int Year: 2024 Document type: Article Affiliation country: Brazil Country of publication: United kingdom