کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2047872 | 1074039 | 2012 | 5 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Clusterin is a specific stabilizer and liberator of extracellular cathepsin K Clusterin is a specific stabilizer and liberator of extracellular cathepsin K](/preview/png/2047872.png)
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 (Kd = 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.
► We have identified clusterin as a cathepsin K-binding protein.
► Clusterin stabilizes cathepsin K at physiological plasma pH.
► Clusterin does not directly affect cathepsin K activity.
► Clusterin affects the conformational flexibility of cathepsin K.
Journal: FEBS Letters - Volume 586, Issue 7, 5 April 2012, Pages 1062–1066