Protein kinase C-dependent inhibition of the lysosomal degradation of endocytosed proteins in rat hepatocytes

Autor:	Raúl A. Marinelli, Elena J. Ochoa, Emilio A. Rodríguez Garay, Maria C. Larocca
Rok vydání:	2002
Předmět:	Proteolysis Endocytic cycle Biology chemistry.chemical_compound medicine Animals Staurosporine Umbelliferones Enzyme Inhibitors Phosphorylation Rats Wistar MARCKS Myristoylated Alanine-Rich C Kinase Substrate Cells Cultured Horseradish Peroxidase Protein Kinase C Protein kinase C Mannose 6-phosphate receptor medicine.diagnostic_test Activator (genetics) Intracellular Signaling Peptides and Proteins Membrane Proteins Proteins Cell Biology Phosphoproteins Endocytosis Rats Cell biology Kinetics Protein Transport Biochemistry chemistry Hepatocytes Phorbol Tetradecanoylphorbol Acetate Lysosomes Glucosidases medicine.drug
Zdroj:	Cellular Signalling. 14:641-647
ISSN:	0898-6568
DOI:	10.1016/s0898-6568(02)00003-7
Popis:	We studied the role of protein kinase C (PKC) in the lysosomal processing of endocytosed proteins in isolated rat hepatocytes. We used [14C]sucrose-labeled horseradish peroxidase ([14C]S-HRP) to simultaneously evaluate endocytosis and lysosomal proteolysis. The PKC activator phorbol 12-myristate 13-acetate (PMA) inhibited the lysosomal degradation of [14C]S-HRP (1 microM PMA: 40% inhibition, P
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76528b99933b6d78fb1d9a552f504b6d https://doi.org/10.1016/s0898-6568(02)00003-7 Zobrazit plný text záznamu Full Text from ScienceDirect