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Innovative workflow for the identification of cathepsin K cleavage sites in type I collagen

Demeuse, Justine ; Massonnet, Philippe ; Schoumacher, Matthieu ; Grifnée, Elodie ; Huyghebaert, Loreen ; Dubrowski, Thomas ; Peeters, Stéphanie ; Le Goff, Caroline ; Cavalier, Etienne

Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 2023-08, Vol.1228, p.123864-123864, Article 123864 [Periódico revisado por pares]

Elsevier BV

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Título:
Innovative workflow for the identification of cathepsin K cleavage sites in type I collagen
Autor: Demeuse, Justine ; Massonnet, Philippe ; Schoumacher, Matthieu ; Grifnée, Elodie ; Huyghebaert, Loreen ; Dubrowski, Thomas ; Peeters, Stéphanie ; Le Goff, Caroline ; Cavalier, Etienne
Assuntos: Analytical Chemistry ; Biochemistry ; Cathepsin K ; Cell Biology ; Cleavage sites identification ; Clinical Biochemistry ; Degradomics ; General Medicine ; High resolution mass spectrometry ; Human health sciences ; Laboratory medicine & medical technology ; Médecine de laboratoire & technologie médicale ; Nano liquid chromatography ; Sciences de la santé humaine ; Type I collagen digestion
É parte de: Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 2023-08, Vol.1228, p.123864-123864, Article 123864
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
scopus-id:2-s2.0-85169297214
Descrição: Since the late 1990s, cathepsin K cleavage sites in type I collagen have been extensively studied due to its ability to release bone resorption biomarkers such as CTX and NTX. However, gel-based methods and N-sequencing used in these studies lack sensitivity, especially for small to medium peptides. In this work, we propose a degradomics mass spectrometry-based workflow that combines protein digestion, Nano-LC-UDMSE, and several software tools to identify cathepsin K cleavage sites. This workflow not only identified previously known cleavage sites, but also discovered new ones. Multiple cleavage hotspots were found and described in type I α1 and type I α2 collagen, many of which coincided with pyridinoline crosslinks, known to stabilize the triple helix. Our results allowed us to establish a chronology of digestion and conclude that cathepsin K preferentially cleaves the extremities of type I collagen before the helical part. We also found that cathepsin K preferentially cleaves amino acid residues with long and hydrophobic lateral chains at the beginning of digestion, whereas no preferred amino acid residues were identified later in the digestion. In conclusion, our workflow successfully identified new cleavage sites and can be easily applied to other proteins or proteases.
Editor: Elsevier BV
Idioma: Inglês

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Innovative workflow for the identification of cathepsin K cleavage sites in type I collagen

Demeuse, Justine ; Massonnet, Philippe ; Schoumacher, Matthieu ; Grifnée, Elodie ; Huyghebaert, Loreen ; Dubrowski, Thomas ; Peeters, Stéphanie ; Le Goff, Caroline ; Cavalier, Etienne

Elsevier BV

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