1.
Biochem Biophys Res Commun
; 446(4): 857-62, 2014 Apr 18.
Artigo
em Inglês
| MEDLINE
| ID: mdl-24632200
RESUMO
Arginine-rich cell-penetrating peptides (CPPs) are promising carriers for the intracellular delivery of various bioactive molecules. However, many ambiguities remain about the molecular interplays on cell surfaces that ultimately lead to endocytic uptake of CPPs. By treatment of cells with octaarginine (R8), enhanced clustering of syndecan-4 on plasma membranes and binding of protein kinase Cα (PKCα) to the cytoplasmic domain of syndecan-4 were observed; these events potentially lead to the macropinocytic uptake of R8. The cytoplasmic V domain of syndecan-4 made a significant contribution to the cellular uptake of R8, whereas the cytoplasmic C1 and C2 domains were not involved in the process.
Assuntos
Membrana Celular/metabolismo , Peptídeos Penetradores de Células/metabolismo , Oligopeptídeos/metabolismo , Proteína Quinase C-alfa/metabolismo , Sindecana-4/metabolismo , Peptídeos Penetradores de Células/análise , Endocitose , Ativação Enzimática , Células HeLa , Humanos , Oligopeptídeos/análise , Pinocitose , Ligação Proteica , Proteína Quinase C-alfa/análise , Estrutura Terciária de Proteína , Sindecana-4/análise
2.
Angew Chem Int Ed Engl
; 51(30): 7464-7, 2012 Jul 23.
Artigo
em Inglês
| MEDLINE
| ID: mdl-22711581