| Online-Ressource |
Verfasst von: | Häussermann, Sabine [VerfasserIn]  |
| Kittstein, Walter [VerfasserIn]  |
| Rincke, Gabriele [VerfasserIn]  |
| Johannes, Franz-Josef [VerfasserIn]  |
| Marks, Friedrich [VerfasserIn]  |
| Gschwendt, Michael [VerfasserIn]  |
Titel: | Proteolytic cleavage of protein kinase Cμ upon induction of apoptosis in U937 cells |
Titelzusatz: | Identification of the cleavage site and characterization of the fragment |
Verf.angabe: | Sabine Häussermann, Walter Kittstein, Gabriele Rincke, Franz-Josef Johannes, Friedrich Marks, Michael Gschwendt |
E-Jahr: | 1999 |
Jahr: | 30 November 1999 |
Umfang: | 5 S. |
Fussnoten: | Gesehen am 22.04.2021 |
Titel Quelle: | Enthalten in: Vereinigung der Europäischen Biochemischen GesellschaftenFEBS letters |
Ort Quelle: | Chichester : Wiley, 1968 |
Jahr Quelle: | 1999 |
Band/Heft Quelle: | 462(1999), 3, Seite 442-446 |
ISSN Quelle: | 1873-3468 |
Abstract: | Treatment of U937 cells with various apoptosis-inducing agents, such as TNFα and β-D-arabinofuranosylcytosine (ara-C) alone or in combination with the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA), bryostatin 1 or cycloheximide, causes proteolytic cleavage of protein kinase Cμ (PKCμ) between the regulatory and catalytic domain, generating a 62 kDa catalytic fragment of the kinase. The formation of this fragment is effectively suppressed by the caspase-3 inhibitor Z-DEVD-FMK. In accordance with these in vivo data, treatment of recombinant PKCμ with caspase-3 in vitro results also in the generation of a 62 kDa fragment (p62). Treatment of several aspartic acid to alanine mutants of PKCμ with caspase-3 resulted in an unexpected finding. PKCμ is not cleaved at one of the typical cleavage sites containing the motif DXXD but at the atypical site CQND378/S379. The respective fragment (amino acids 379-912) was expressed in bacteria as a GST fusion protein (GST-p62) and partially purified. In contrast to the intact kinase, the fragment does not respond to the activating cofactors TPA and phosphatidylserine and is thus unable to phosphorylate substrates effectively. |
DOI: | doi:10.1016/S0014-5793(99)01577-X |
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/S0014-5793(99)01577-X |
| Volltext: https://www.sciencedirect.com/science/article/pii/S001457939901577X |
| DOI: https://doi.org/10.1016/S0014-5793(99)01577-X |
Datenträger: | Online-Ressource |
Sprache: | eng |
Sach-SW: | Apoptosis |
| Caspase-3 |
| Caspase-3 inhibitor |
| Cleavage site |
| Protein kinase Cμ |
| Proteolytic fragment |
K10plus-PPN: | 1755734301 |
Verknüpfungen: | → Zeitschrift |
Proteolytic cleavage of protein kinase Cμ upon induction of apoptosis in U937 cells / Häussermann, Sabine [VerfasserIn]; 30 November 1999 (Online-Ressource)