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. 2018 Jun 4;9:1081. doi: 10.3389/fimmu.2018.01081

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Copyright © 2018 Gouwy, De Buck, Abouelasrar Salama, Vandooren, Knoops, Pörtner, Vanbrabant, Berghmans, Opdenakker, Proost, Van Damme and Struyf.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Cleavage of serum amyloid A1 (SAA1) by matrix metalloproteinase-9 (MMP-9). Pro-MMP-9 was activated with the catalytic domain of MMP-3, and recombinant human SAA1 was incubated at 37°C with activated gelatinase B/MMP-9 at an enzyme:substrate molar ratio of 1:50. Samples taken at the indicated time points were analyzed by SDS–PAGE and Coomassie brilliant blue protein staining. The relative molecular weight of the standard marker proteins (St) is indicated in kilodaltons. After incubation for prolonged time intervals (22 and 30 h), some autocatalysis of MMP-9 was detected, slowing down the conversion of SAA1 into reaction products (RP).