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Updated: May 16, 2026

Detection of Glycosaminoglycans by Polyacrylamide Gel Electrophoresis and Silver Staining
Published on: February 25, 2021
Autoactivation of prolegumain is accelerated by glycosaminoglycans
Lise Berven1, Harald Thidemann Johansen, Rigmor Solberg
1School of Pharmacy, University of Oslo, Norway.
Abstract:
The cysteine protease legumain participates in several biological and pathological processes including tumour invasion and metastasis. Legumain is synthesized as a zymogen and undergoes pH-dependent autoactivation of the proform in order to reach an enzymatically active form. Here we demonstrate that the naturally occurring polyanionic glycosaminoglycans (GAGs) chondroitin 4-sulphate (C4S), chondroitin 6-sulphate (C6S), chondroitin 4,6-sulphate (C4,6S), heparin, heparan sulphate (HS) as well as chondroitin sulphate (CS)-derived decasaccharides accelerated the autocatalytic activation of prolegumain through ionic interactions in a concentration-, size- and time-dependent manner at pH 4.0. In contrast, at pH 5.0 only C4S and C4,6S were able to promote prolegumain activation, while CS-derived decasaccharides, C6S, heparin and HS lost their effect at this pH.
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