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Biological Chemistry

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Cleavage of the myristoylated alanine-rich C kinase substrate (MARCKS) by cysteine cathepsins in cells and tissues of stefin B-deficient mice

Nataša Kopitar-Jerala1 / Boris Turk2

1Department of Biochemistry, Molecular and Structural Biology, Jožef Stefan Institute, Jamova 39, SI-1000 Ljubljana, Slovenia

2Department of Biochemistry, Molecular and Structural Biology, Jožef Stefan Institute, Jamova 39, SI-1000 Ljubljana, Slovenia

Corresponding author

Citation Information: Biological Chemistry. Volume 388, Issue 8, Pages 847–852, ISSN (Online) 14316730, ISSN (Print) 14374315, DOI: 10.1515/BC.2007.092, August 2007

Publication History

Published Online:


The myristoylated alanine-rich C kinase substrate (MARCKS) is a substrate of protein kinase C (PKC). Besides regulation at the level of gene transcription, MARCKS concentrations within the cell are also regulated by proteolytic cleavage by cathepsins and calpains, which are cysteine proteinases. Stefin B (cystatin B) is an endogenous inhibitor of lysosomal cysteine cathepsins, but not calpains. We have observed increased cleavage of MARCKS in brain and macrophages, but not in liver and kidney extracts of stefin B-deficient mice compared to wild-type mice. Processing of cathepsin B was unaltered in the brain of stefin B-deficient mice and we conclude that increased cleavage of MARCKS could be attributed to the lack of inhibitor.

Keywords: cathepsin; inhibitor; MARCKS; progressive myoclonus epilepsy

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