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. 2021 Mar 19;8:643178. doi: 10.3389/fmolb.2021.643178

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Copyright © 2021 Leduc, Dupont, Joannes, Monseur, Baiwir, Mazzucchelli, Deroanne, Colige and Bekhouche.

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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ADAMTS2 and/or ADAMTS14 cleavages of type I and V collagens. Schematic view of the pro alpha-1(I) and alpha-2(I) chains showing the signal peptides (PS), the main triple helix collagenous domain (COL1) and the short triple helix collagenous domain (COL2) and the N- and C-propeptides (N- and C-Pro) (A). Schematic view of the pro alpha-1(V) and alpha-2(V) chains showing the collagenous (COL) and non collagenous (NC) domains (B). The ADAMTS2 and ADAMTS14 cleavage sites are indicated by arrows. The red arrows correspond to the already reported ADAMTS2 cleavage sites (Colige et al., 2005; Bekhouche and Colige, 2015). Table showing the P/C ratio for type V collagens, according to the cleavage sites observed by proteomic. Ratios above the average 3σ cut-offs are highlighted in green. The previously described ADAMTS2 cleavage site within alpha-1(V) chain is in bold (C).