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Posttranslational proteolytic processing of Leda-1/Pianp involves cleavage by MMPs, ADAM10/17 and gamma-secretase

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...

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Hauptverfasser: Biswas, Siladitta (VerfasserIn) , Adrian, Monica (VerfasserIn) , Winkler, Manuel (VerfasserIn) , Géraud, Cyrill (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 2 September 2016
In: Biochemical and biophysical research communications
Year: 2016, Jahrgang: 477, Heft: 4, Pages: 661-666
ISSN:1090-2104
DOI:10.1016/j.bbrc.2016.06.116
Online-Zugang:Verlag, Volltext: https://doi.org/10.1016/j.bbrc.2016.06.116
Verlag, Volltext: http://www.sciencedirect.com/science/article/pii/S0006291X16310348
Volltext
Verfasserangaben:Siladitta Biswas, Monica Adrian, Jochen Weber, Konstantin Evdokimov, Manuel Winkler, Cyrill Géraud
Beschreibung
Zusammenfassung: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.
Beschreibung:Gesehen am 31.07.2019
Available online 24 June 2016
Beschreibung:Online Resource
ISSN:1090-2104
DOI:10.1016/j.bbrc.2016.06.116

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