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Titel: Regulation of ADAM10 activity through microdomain-dependent intracellular calcium changes
VerfasserIn: Gharzia, Federico Guillermo
Aljohmani, Ahmad
Beck, Andreas
Philipp, Andreas
Yildiz, Daniela
Sprache: Englisch
Titel: Cell Communication and Signaling
Bandnummer: 22
Heft: 1
Verlag/Plattform: BMC
Erscheinungsjahr: 2024
Freie Schlagwörter: Calcium
Proteolysis
Metalloproteinases
Exosomes
Transient receptor potential channels
Junction and adhesion molecules
DDC-Sachgruppe: 610 Medizin, Gesundheit
Dokumenttyp: Journalartikel / Zeitschriftenartikel
Abstract: A disintegrin and metalloproteinases (ADAMs) are transmembrane proteases that cleave other proteins close to the surface in a process called shedding. The prominent member ADAM10 has been linked to several pathologies such as Alzheimer’s disease, bacterial infection, cancer development and metastasis. Although the regulation of the ADAM10 activity by calcium influx and calmodulin inhibition has been reported, the spatiotemporal regulation of Ca2+-dependent ADAM10 activation and the required source of Ca2+ ions have not been thoroughly studied. In the present study, we observed the rapid Ca2+-dependent activation of ADAM10 in A549 lung carcinoma cells upon stimulation with ionomycin. The calmodulin-inhibitors trifluoperazine and ophiobolin A mediated delayed activation of ADAM10, which apparently did not depend on intracellular Ca2+ in the case of trifluoperazine. Furthermore, the surface translocation and release of ADAM10 in extracellular vesicles exhibited different kinetics and were only partially linked to catalytic activation. Finally, ADAM10 activation was observed after the entry of Ca2+ through certain channels, such as canonical members of transient receptor potential (TRP) channels. Therefore, the opening of particular channels for Ca2+ entry points and subsequent Ca2+ flux as well as the temporal aspects of the consequent increase in Ca2+ levels, must be considered for future therapeutic options involving the increasing or decreasing ADAM10 activity.
DOI der Erstveröffentlichung: 10.1186/s12964-024-01891-5
URL der Erstveröffentlichung: https://biosignaling.biomedcentral.com/articles/10.1186/s12964-024-01891-5
Link zu diesem Datensatz: urn:nbn:de:bsz:291--ds-443691
hdl:20.500.11880/39641
http://dx.doi.org/10.22028/D291-44369
ISSN: 1478-811X
Datum des Eintrags: 13-Feb-2025
Bezeichnung des in Beziehung stehenden Objekts: Supplementary Information
In Beziehung stehendes Objekt: https://static-content.springer.com/esm/art%3A10.1186%2Fs12964-024-01891-5/MediaObjects/12964_2024_1891_MOESM1_ESM.jpg
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Fakultät: M - Medizinische Fakultät
Fachrichtung: M - Experimentelle und Klinische Pharmakologie und Toxikologie
Professur: M - Jun.-Prof. Dr. Daniela Yildiz
Sammlung:SciDok - Der Wissenschaftsserver der Universität des Saarlandes

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