. "M\u00E1\u0161a, Martin" . "Mare\u0161, Michael" . "Horn, Martin" . . "Complex modulation of peptidolytic activity of cathepsin D by sphingolipids"@en . "[C611D6C0D23C]" . . "P(IAA400550705), S, Z(AV0Z40550506)" . . "Complex modulation of peptidolytic activity of cathepsin D by sphingolipids"@en . . . "Complex modulation of peptidolytic activity of cathepsin D by sphingolipids" . . "000298521700012" . . "12" . "sphingolipid; phospholipid; inhibition; activation; cathepsin D; enzyme regulation"@en . . "\u017Debrakovsk\u00E1, Iva" . "1388-1981" . . . . "10.1016/j.bbalip.2011.09.005" . "NL - Nizozemsko" . "191400" . "5"^^ . . . . "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." . . "V\u00E1vrov\u00E1, K." . . . "Srp, Jaroslav" . . "6"^^ . "Biochimica Et Biophysica Acta-Molecular and Cell Biology of Lipids" . "RIV/61388963:_____/11:00366668!RIV12-AV0-61388963" . "Complex modulation of peptidolytic activity of cathepsin D by sphingolipids" . "1811" . . "RIV/61388963:_____/11:00366668" . . "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."@en . . "8"^^ . . . . .