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Complex modulation of peptidolytic activity of cathepsin D by sphingolipids
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SYSNO ASEP 0366668 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Complex modulation of peptidolytic activity of cathepsin D by sphingolipids Author(s) Žebrakovská, Iva (UOCHB-X) ORCID, RID
Máša, Martin (UOCHB-X)
Srp, Jaroslav (UOCHB-X) RID, ORCID
Horn, Martin (UOCHB-X) RID, ORCID
Vávrová, K. (CZ)
Mareš, Michael (UOCHB-X) RID, ORCIDNumber of authors 6 Source Title Biochimica Et Biophysica Acta-Molecular and Cell Biology of Lipids. - : Elsevier - ISSN 1388-1981
Roč. 1811, č. 12 (2011), s. 1097-1104Number of pages 8 s. Language eng - English Country NL - Netherlands Keywords sphingolipid ; phospholipid ; inhibition ; activation ; cathepsin D ; enzyme regulation Subject RIV CE - Biochemistry R&D Projects IAA400550705 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) CEZ AV0Z40550506 - UOCHB-X (2005-2011) UT WOS 000298521700012 DOI 10.1016/j.bbalip.2011.09.005 Annotation Cathepsin D is an aspartic peptidase involved in cellular processes including proliferation and apoptosis. We describe a complex pattern of modulation of the peptidolytic activity of cathepsin D by sphingolipids. A panel of sphingolipid derivatives was screened in a FRET-based assay; these molecules demonstrated negative or positive modulation of cathepsin D peptidolytic activity, depending on the sphingolipid structure. Certain sphingosines and ceramides inhibited cathepsin D, and structural requirements for this inhibitory effect were evaluated. In contrast, monoester phosphosphingolipids, especially ceramide-1-phosphate, were identified as activators of cathepsin D peptidolytic activity Thus, sphingolipids and phosphosphingolipids, known to be antagonistic in their cell-signaling functions, displayed opposite modulation of cathepsin D. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Year of Publishing 2012
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