Clusterin is a specific stabilizer and liberator of extracellular cathepsin K

FEBS Letters
Marko NovinecAntonio Baici

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.

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Citations

Aug 13, 2015·Tumour Biology : the Journal of the International Society for Oncodevelopmental Biology and Medicine·Wenjie ZhengDengfu Yao
Jan 21, 2015·Tumour Biology : the Journal of the International Society for Oncodevelopmental Biology and Medicine·Wenjie ZhengDengfu Yao
May 1, 2013·Biological Chemistry·Marko Novinec, Brigita Lenarčič
Jun 1, 2013·Biomolecular Concepts·Marko Novinec, Brigita Lenarčič

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