Molecular interplays involved in the cellular uptake of octaarginine on cell surfaces and the importance of syndecan-4 cytoplasmic V domain for the activation of protein kinase Cα.
Biochem Biophys Res Commun
; 446(4): 857-62, 2014 Apr 18.
Article
en En
| MEDLINE
| ID: mdl-24632200
ABSTRACT
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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Oligopéptidos
/
Membrana Celular
/
Proteína Quinasa C-alfa
/
Sindecano-4
/
Péptidos de Penetración Celular
Límite:
Humans
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
2014
Tipo del documento:
Article