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. 2018 Aug 31;9:868. doi: 10.3389/fphar.2018.00868

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Copyright © 2018 Houde, Schwertani, Touil, Desbiens, Sarrhini, Lecomte, Lepage, Gagnon, Takai, Pejler, Jacques, Gobeil, Day and D’Orléans-Juste.

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(s) 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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Analysis of the in vitro hydrolysis of recombinant mouse IGF-1 (LC/MS/MS) and Big ET-1 (HPLC) by recombinant mMCP-4, with the chymase inhibitor TY-51469 (10 μM). In (A), the results of recombinant mMCP-4 activity on mouse IGF-1 are shown using trypsin-degradation products, with GFYFNKPTGYGSSIR coming from the complete IGF-1 sequence and GFYFNKPTGY coming from the mMCP-4-cleaved sequence. In (B), the area under the curve (AUC) was measured for Big ET-1 and ET-1 (1–31) using HPLC at 214 nm detection. n = 3 (one-way ANOVA with multiple comparisons Holms-Šidak post-test). In (C), the complete sequence of mouse IGF-1 is shown, with the disulfide bonds shown with brackets, the analyzed trypsin-digested product in bold and the cleavage site in increased type size.