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  1. Artikel: Fatty acid amide hydrolase drives adult mammary gland development by promoting luminal cell differentiation.

    Tundidor, Isabel / Seijo-Vila, Marta / Blasco-Benito, Sandra / Rubert-Hernández, María / Moreno-Bueno, Gema / Bindila, Laura / de la Rosa, Rubén Fernández / Guzmán, Manuel / Sánchez, Cristina / Pérez-Gómez, Eduardo

    Cell death discovery

    2024  Band 10, Heft 1, Seite(n) 12

    Abstract: Mammary gland development occurs primarily in adulthood, undergoing extensive expansion during puberty followed by cycles of functional specialization and regression with every round of pregnancy/lactation/involution. This process is ultimately driven by ...

    Abstract Mammary gland development occurs primarily in adulthood, undergoing extensive expansion during puberty followed by cycles of functional specialization and regression with every round of pregnancy/lactation/involution. This process is ultimately driven by the coordinated proliferation and differentiation of mammary epithelial cells. However, the endogenous molecular factors regulating these developmental dynamics are still poorly defined. Endocannabinoid signaling is known to determine cell fate-related events during the development of different organs in the central nervous system and the periphery. Here, we report that the endocannabinoid-degrading enzyme fatty acid amide hydrolase (FAAH) plays a pivotal role in adult mammary gland development. Specifically, it is required for luminal lineage specification in the mammary gland, and it promotes hormone-driven secretory differentiation of mammary epithelial cells by controlling the endogenous levels of anandamide and the subsequent activation of cannabinoid CB
    Sprache Englisch
    Erscheinungsdatum 2024-01-06
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ISSN 2058-7716
    ISSN 2058-7716
    DOI 10.1038/s41420-023-01788-1
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Identification of fatty acid amide hydrolase as a metastasis suppressor in breast cancer.

    Tundidor, Isabel / Seijo-Vila, Marta / Blasco-Benito, Sandra / Rubert-Hernández, María / Adámez, Sandra / Andradas, Clara / Manzano, Sara / Álvarez-López, Isabel / Sarasqueta, Cristina / Villa-Morales, María / González-Lois, Carmen / Ramírez-Medina, Esther / Almoguera, Belén / Sánchez-López, Antonio J / Bindila, Laura / Hamann, Sigrid / Arnold, Norbert / Röcken, Christoph / Heras-Murillo, Ignacio /
    Sancho, David / Moreno-Bueno, Gema / Caffarel, María M / Guzmán, Manuel / Sánchez, Cristina / Pérez-Gómez, Eduardo

    Nature communications

    2023  Band 14, Heft 1, Seite(n) 3130

    Abstract: Clinical management of breast cancer (BC) metastasis remains an unmet need as it accounts for 90% of BC-associated mortality. Although the luminal subtype, which represents >70% of BC cases, is generally associated with a favorable outcome, it is ... ...

    Abstract Clinical management of breast cancer (BC) metastasis remains an unmet need as it accounts for 90% of BC-associated mortality. Although the luminal subtype, which represents >70% of BC cases, is generally associated with a favorable outcome, it is susceptible to metastatic relapse as late as 15 years after treatment discontinuation. Seeking therapeutic approaches as well as screening tools to properly identify those patients with a higher risk of recurrence is therefore essential. Here, we report that the lipid-degrading enzyme fatty acid amide hydrolase (FAAH) is a predictor of long-term survival in patients with luminal BC, and that it blocks tumor progression and lung metastasis in cell and mouse models of BC. Together, our findings highlight the potential of FAAH as a biomarker with prognostic value in luminal BC and as a therapeutic target in metastatic disease.
    Mesh-Begriff(e) Animals ; Mice ; Amidohydrolases/genetics ; Biomarkers, Tumor ; Lung Neoplasms/pathology ; Neoplasm Recurrence, Local/pathology
    Chemische Substanzen Amidohydrolases (EC 3.5.-) ; Biomarkers, Tumor ; fatty-acid amide hydrolase (EC 3.5.1.-)
    Sprache Englisch
    Erscheinungsdatum 2023-05-30
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-38750-9
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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