Status: Bibliographieeintrag
Standort: ---
Exemplare:
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| Online-Ressource |
Verfasst von: | Biswas, Siladitta [VerfasserIn]  |
| Adrian, Monica [VerfasserIn]  |
| Winkler, Manuel [VerfasserIn]  |
| Géraud, Cyrill [VerfasserIn]  |
Titel: | Posttranslational proteolytic processing of Leda-1/Pianp involves cleavage by MMPs, ADAM10/17 and gamma-secretase |
Verf.angabe: | Siladitta Biswas, Monica Adrian, Jochen Weber, Konstantin Evdokimov, Manuel Winkler, Cyrill Géraud |
E-Jahr: | 2016 |
Jahr: | 2 September 2016 |
Umfang: | 6 S. |
Fussnoten: | Gesehen am 31.07.2019 ; Available online 24 June 2016 |
Titel Quelle: | Enthalten in: Biochemical and biophysical research communications |
Ort Quelle: | [Amsterdam] : Elsevier B.V., 1959 |
Jahr Quelle: | 2016 |
Band/Heft Quelle: | 477(2016), 4, Seite 661-666 |
ISSN Quelle: | 1090-2104 |
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. |
DOI: | doi:10.1016/j.bbrc.2016.06.116 |
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 |
| Volltext: http://www.sciencedirect.com/science/article/pii/S0006291X16310348 |
| DOI: https://doi.org/10.1016/j.bbrc.2016.06.116 |
Datenträger: | Online-Ressource |
Sprache: | eng |
Sach-SW: | ADAM |
| Gamma secretase |
| Immune regulation |
| Nervous system |
| Proteolysis |
K10plus-PPN: | 1670340112 |
Verknüpfungen: | → Zeitschrift |
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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