SearchPublisher and Institutes
You are here: Home :: Area NEM :: Life sciences :: Biochemistry
Nataa Kopitar-Jerala, Boris Turk
Cleavage of the myristoylated alanine-rich C kinase substrate (MARCKS) by cysteine cathepsins in cells and tissues of stefin B-deficient mice
Keywords: cathepsin, inhibitor, MARCKS, progressive myoclonus epilepsy
The myristoylated alanine-rich C kinase substrate (MARCKS) is a substrate of protein kinase C (PKC). Besides the regulation on the level of gene transcription, MARCKS concentrations within the cell are regulated also by proteolytic cleavages by the cysteine proteinases: cathepsins and calpains. Stefin B (cystatin B) is an endogenous inhibitor of lysosomal cysteine cathepsins but not calpains. We have observed increased cleavage of MARCKS in the brain, macrophages, but not in the liver and kidney extracts of stefin B-deficient mice compared to the wild type mice. Processing of cathepsin B was unaltered in the brain of stefin B-deficient mice and we concluded that increased cleavage of MARCKS could be attributed to the lack of inhibito
Biological Chemistry, Walter de Gruyter
Print ISSN: 1431-6730
Volume: 2007
Pages: -