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Biochimie. 2013 Apr;95(4):772-81. doi: 10.1016/j.biochi.2012.11.002. Epub 2012 Nov 14.

Autoactivation of prolegumain is accelerated by glycosaminoglycans.

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1
School 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.

PMID:
23160071
DOI:
10.1016/j.biochi.2012.11.002
[Indexed for MEDLINE]
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