Header

UZH-Logo

Maintenance Infos

Clusterin is a specific stabilizer and liberator of extracellular cathepsin K


Novinec, Marko; Lenarčič, Brigita; Baici, Antonio (2012). Clusterin is a specific stabilizer and liberator of extracellular cathepsin K. FEBS Letters, 586(7):1062-1066.

Abstract

The cysteine peptidase cathepsin K is a major player in extracellular proteolysis. Here we describe the identification of the multifunctional extracellular chaperone clusterin as a cathepsin K-binding protein. Clusterin increases the stability of cathepsin K in dilute solution and in the presence of high protein concentration. It does not alter the activity of the enzyme but acts as a liberator by preventing substrate inhibition. Kinetic measurements show that clusterin binds cathepsin K with high affinity (K(d) = 0.5-0.6 nM). Altogether these results provide novel insights into the mechanisms involved in the fine-tuning of cysteine cathepsin activity in the extracellular space.

Abstract

The cysteine peptidase cathepsin K is a major player in extracellular proteolysis. Here we describe the identification of the multifunctional extracellular chaperone clusterin as a cathepsin K-binding protein. Clusterin increases the stability of cathepsin K in dilute solution and in the presence of high protein concentration. It does not alter the activity of the enzyme but acts as a liberator by preventing substrate inhibition. Kinetic measurements show that clusterin binds cathepsin K with high affinity (K(d) = 0.5-0.6 nM). Altogether these results provide novel insights into the mechanisms involved in the fine-tuning of cysteine cathepsin activity in the extracellular space.

Statistics

Citations

Dimensions.ai Metrics
9 citations in Web of Science®
12 citations in Scopus®
Google Scholar™

Altmetrics

Downloads

0 downloads since deposited on 09 Oct 2012
0 downloads since 12 months

Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
Dewey Decimal Classification:570 Life sciences; biology
Scopus Subject Areas:Life Sciences > Biophysics
Life Sciences > Structural Biology
Life Sciences > Biochemistry
Life Sciences > Molecular Biology
Life Sciences > Genetics
Life Sciences > Cell Biology
Language:English
Date:2012
Deposited On:09 Oct 2012 15:48
Last Modified:23 Jan 2022 22:28
Publisher:Elsevier
ISSN:0014-5793
OA Status:Closed
Publisher DOI:https://doi.org/10.1016/j.febslet.2012.03.004
PubMed ID:22569264