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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Vydáno v:	Biochemical and biophysical research communications Ročník 777; s. 152256
Hlavní autoři:	Lacerda-Abreu, Marco Antonio, Silva, Enderson, Mendonça, Bruna dos Santos, de Moraes, Gabriela Nestal, Meyer-Fernandes, José Roberto
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States Elsevier Inc 01.09.2025
Témata:	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
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Abstract	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.
AbstractList	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.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. 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 Mg -dependent and independent ecto-ATPase activities, with MCF-7 cells exhibiting a significant Mg -dependent increase in ATP hydrolysis. Kinetic analyses revealed that Mg -independent activity presents higher substrate affinity, whereas the Mg -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 Mg -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. 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.
ArticleNumber	152256
Author	Mendonça, Bruna dos Santos Lacerda-Abreu, Marco Antonio Meyer-Fernandes, José Roberto de Moraes, Gabriela Nestal Silva, Enderson
Author_xml	– sequence: 1 givenname: Marco Antonio surname: Lacerda-Abreu fullname: Lacerda-Abreu, Marco Antonio email: marcoantoniolacerdaabreu@gmail.com organization: Instituto de Bioquímica Médica Leopoldo de Meis, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil – sequence: 2 givenname: Enderson orcidid: 0009-0004-9243-0768 surname: Silva fullname: Silva, Enderson organization: Instituto de Bioquímica Médica Leopoldo de Meis, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil – sequence: 3 givenname: Bruna dos Santos surname: Mendonça fullname: Mendonça, Bruna dos Santos organization: Instituto de Bioquímica Médica Leopoldo de Meis, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil – sequence: 4 givenname: Gabriela Nestal orcidid: 0000-0002-0385-3039 surname: de Moraes fullname: de Moraes, Gabriela Nestal organization: Instituto de Bioquímica Médica Leopoldo de Meis, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil – sequence: 5 givenname: José Roberto surname: Meyer-Fernandes fullname: Meyer-Fernandes, José Roberto email: meyer@bioqmed.ufrj.br organization: Instituto de Bioquímica Médica Leopoldo de Meis, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil
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Keywords	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
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SubjectTerms	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
Title	Characterization of Mg-independent and Mg-dependent Ecto-ATPase activities in luminal a breast cancer MCF-7 cells
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