Press Release


New methodology established to characterize collagens in molecular detail

Claudia Staab-Weijnitz; Source: ILBD/CPC, Helmholtz Zentrum München

Collagens are major components of the extracellular matrix but difficult to analyse in molecular detail. Claudia Staab-Weijnitz, head of the Core Unit “Matrix Genotyping” at the CPC/ILBD and PI in the German Center for Lung Research (DZL), and Juliane Merl-Pham (PROT), in close collaboration with researchers from Vanderbilt University, have now established a mass spectrometry-based methodology to assess collagen properties like chain stoichiometries and post-translational modifications in addition to overall ECM composition. The study has been published in Matrix Biology Plus, the new online-only open access journal of the matrix biology community.

Collagens are the main component of the extracellular matrix (ECM) in essentially every tissue. Nevertheless, our understanding of collagen biosynthesis, post-translational modifications (PTMs), chain stoichiometries, and other molecular properties is limited and relies mainly on studies on type I collagen. In particular, the biological function of relatively rare collagen PTMs like e.g. collagen prolyl-3-hydroxylations is unknown. Assessment of these collagen PTMs is inherently demanding and has previously required the use of purified or highly enriched collagen samples.

PD Dr. Claudia Staab-Weijnitz (CPC/ILBD) and Dr. Juliane Merl-Pham (PROT) have now established the methodology to assess collagen properties like chain stoichiometries and PTMs in complex samples, in addition to overall ECM composition. For this, they took advantage of a previously established in vitro model of lung fibrosis (Staab-Weijnitz CA et al, Am J Resp Crit Care Med, 2015; Knüppel et al, Am J Resp Cell Mol Biol, 2017; Knüppel et al, Resp Res, 2018), based on IPF-patient derived primary human lung fibroblasts from the CPC bioArchive. The proteomics pipeline was developed in the Core Facility Proteomics at HMGU in collaboration with the Vanacore lab at Vanderbilt University. Overall ECM composition and chain stoichiometries were analysed in-house, while the Vanacore lab established a bioinformatics pipeline for in-depth analysis of the collagen PTMs.

The study revealed numerous previously unknown collagen PTMs in 15 collagen chains of in total nine collagen types and lays the foundation for studying their function in fibrotic disease. Notably, as ECM remodelling plays a key role in many pathologies beyond fibrosis, the technology may prove useful for studies in other disease models. In addition, in line with PD Dr. Staab-Weijnitz’ efforts to establish in vitro models for chronic lung disease, the results also revealed that, for ECM changes in lung fibrosis, the in vitro model reflected clinical IPF better than the most frequently used mouse model in this context.

 Link to published article:

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