Status: Bibliographieeintrag
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| Verfasst von: | Biswas, Siladitta [VerfasserIn]  |
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| | Adrian, Monica [VerfasserIn] |
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| | Winkler, Manuel [VerfasserIn] |
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| | Géraud, Cyrill [VerfasserIn] |
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| Titel: | Posttranslational proteolytic processing of Leda-1/Pianp involves cleavage by MMPs, ADAM10/17 and gamma-secretase |
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| Verf.angabe: | Siladitta Biswas, Monica Adrian, Jochen Weber, Konstantin Evdokimov, Manuel Winkler, Cyrill Géraud |
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| E-Jahr: | 2016 |
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| Jahr: | 2 September 2016 |
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| Umfang: | 6 S. |
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| Fussnoten: | Gesehen am 31.07.2019 ; Available online 24 June 2016 |
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| Titel Quelle: | Enthalten in: Biochemical and biophysical research communications |
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| Ort Quelle: | [Amsterdam] : Elsevier B.V., 1959 |
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| Jahr Quelle: | 2016 |
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| Band/Heft Quelle: | 477(2016), 4, Seite 661-666 |
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| ISSN Quelle: | 1090-2104 |
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| Abstract: | Leda-1/Pianp is a type I transmembrane protein expressed by CNS cells, murine melanoma cell line B16F10 and rat liver sinusoidal endothelial cells. The early steps of posttranslational modifications of Leda-1/Pianp have been described to include glycosylation and processing by proprotein convertases. Here, we comprehensively characterized the subsequent steps of proteolytic processing of Leda-1/Pianp. For this purpose specific protease inhibitors and cell lines deficient in PS1, PS2, PS1/PS2 and ADAM10/17 were deployed. Leda-1/Pianp was cleaved at numerous cleavage sites within the N-terminal extracellular domain. The sheddases involved included MMPs and ADAM10/17. Ectodomain shedding yielded C-terminal fragments (CTF) of ∼15 kDa. The CTF was further processed by the γ (gamma)-secretase complex to generate the intracellular domain (ICD) of ∼10 kDa. Although PS1 was the dominant intramembrane protease, PS2 was also able to cleave Leda-1/Pianp in the absence of PS1. Thus, Leda-1/Pianp is constitutively processed by proprotein convertases, sheddases including MMPs and ADAM10/17 and intramembrane protease γ-secretase. |
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| DOI: | doi:10.1016/j.bbrc.2016.06.116 |
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| URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext: https://doi.org/10.1016/j.bbrc.2016.06.116 |
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| | Volltext: http://www.sciencedirect.com/science/article/pii/S0006291X16310348 |
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| | DOI: https://doi.org/10.1016/j.bbrc.2016.06.116 |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| Sach-SW: | ADAM |
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| | Gamma secretase |
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| | Immune regulation |
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| | Nervous system |
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| | Proteolysis |
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| K10plus-PPN: | 1670340112 |
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| Verknüpfungen: | → Zeitschrift |
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Posttranslational proteolytic processing of Leda-1/Pianp involves cleavage by MMPs, ADAM10/17 and gamma-secretase / Biswas, Siladitta [VerfasserIn]; 2 September 2016 (Online-Ressource)
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