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Activation and activity of glycosylated KLKs 3, 4 and 11 by Shihui Guo; Peter Briza; Viktor Magdolen; Hans Brandstetter; Peter Goettig is a scholarly article available to read on EtoBox.

What is Activation and activity of glycosylated KLKs 3, 4 and 11 about?

Human kallikrein-related peptidases 3, 4, 11, and KLK2, the activator of KLK3/PSA, belong to the prostatic group of the KLKs, whose major physiological function is semen liquefaction during the fertilization process. Notably, these KLKs are upregulated in prostate cancer and are used as clinical biomarkers or have been proposed as therapeutic targets. However, this potential awaits a detailed characterization of these proteases. In order to study glycosylated prostatic KLKs resembling the natural proteases, we used Leishmania (LEXSY) and HEK293 cells for secretory expression. Both systems allowed the subsequent purification of soluble pro-KLK zymogens with correct propeptides and of the mature forms. Periodic acid-Schiff reaction, enzymatic deglycosylation assays, and mass spectrometry confirmed the glycosylation of these KLKs. Activation of glycosylated pro-KLKs 4 and 11 turned out to be most efficient by glycosylated KLK2 and KLK4, respectively. By comparing the glycosylated prostatic KLKs with their non-glycosylated counterparts from Escherichia coli, it was observed that the N-glycans stabilize the KLK proteases and change their activation profiles and their enzymatic activity

Author

Shihui Guo; Peter Briza; Viktor Magdolen; Hans Brandstetter; Peter Goettig

Publisher

Walter de Gruyter GmbH

Published

2018

Language

EN