Characterization of Mg-independent and Mg-dependent Ecto-ATPase activities in luminal a breast cancer MCF-7 cells

Breast cancer remains the most prevalent malignancy among women, characterized by molecular heterogeneity and complex tumor microenvironment interactions. Purinergic signaling, particularly through extracellular adenosine triphosphate (ATP) hydrolysis, plays a significant role in regulating cancer p...

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Published in:Biochemical and biophysical research communications Vol. 777; p. 152256
Main Authors: Lacerda-Abreu, Marco Antonio, Silva, Enderson, Mendonça, Bruna dos Santos, de Moraes, Gabriela Nestal, Meyer-Fernandes, José Roberto
Format: Journal Article
Language:English
Published: United States Elsevier Inc 01.09.2025
Subjects:
Adenosine Triphosphatases - metabolism
Adenosine Triphosphate - metabolism
Adhesion
Breast cancer
Breast Neoplasms - enzymology
Breast Neoplasms - metabolism
Breast Neoplasms - pathology
Cell migration
Ecto-ATPase
Extracellular ATP hydrolysis
Female
Humans
Hydrolysis
Kinetics
Magnesium - metabolism
MCF-7 Cells
MCF-7 cells
Mg2+-dependent ATPase activity
Purinergic signaling
Substrate Specificity
Tumor microenvironment
PR
APCP
ALP
MCF-7
MCF10-A
NTP
ADP
FBS
Pi
cDNA
Mg2+-dependent ATPase activity
NDP
RT-qPCR
PBS
ENTPDase
Tumor microenvironment
AMP
MCF-7 cells
EGF
Breast cancer
Adhesion
ER
ECM
Extracellular ATP hydrolysis
NMP
Ecto-ATPase
DIDS
ARL67156
HER2
ATP
Cell migration
PCR
Purinergic signaling
Mg(2+)-dependent ATPase activity
ISSN:0006-291X, 1090-2104, 1090-2104
Online Access:Get full text
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Summary:Breast cancer remains the most prevalent malignancy among women, characterized by molecular heterogeneity and complex tumor microenvironment interactions. Purinergic signaling, particularly through extracellular adenosine triphosphate (ATP) hydrolysis, plays a significant role in regulating cancer progression. Ectonucleotidases and ectophosphatases modulate ATP and inorganic phosphate (Pi) metabolism, thereby influencing tumor-associated processes such as migration and adhesion. In this study, we biochemically characterized ecto-ATPase activity in luminal breast cancer cells (MCF-7) and compared it to non-tumorigenic breast epithelial cells (MCF10-A). We identified distinct Mg2+-dependent and independent ecto-ATPase activities, with MCF-7 cells exhibiting a significant Mg2+-dependent increase in ATP hydrolysis. Kinetic analyses revealed that Mg2+-independent activity presents higher substrate affinity, whereas the Mg2+-dependent enzyme displays greater catalytic capacity. Substrate specificity assays demonstrated preferential hydrolysis of ATP and ADP, highlighting the potential role of ecto-ATPase in extracellular nucleotide homeostasis. Pharmacological inhibition with ARL67156 reduced Mg2+-dependent ecto-ATPase activity, leading to a significant decrease in cell migration and adhesion, indicating a functional role in breast cancer progression. These findings underscore the relevance of ecto-ATPase in luminal breast cancer and its potential as a therapeutic target. Future investigations should explore its interplay with purinergic signaling and oncogenic pathways to develop novel strategies for targeted breast cancer treatment. •Magnesium-dependent and magnesium-independent ecto-ATPase activities were identified in luminal A MCF-7 breast cancer cells.•Higher ecto-ATPase activity is found in breast cancer compared to non-tumoral breast cells.•Ecto-ATPase activity is associated with cell adhesion and migration in MCF-7 cells.
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ISSN:0006-291X
1090-2104
1090-2104
DOI:10.1016/j.bbrc.2025.152256