Collagen Dynamics in Extracellular Matrix Biology

Collagens constitute the principal fibrous proteins of the extracellular matrix (ECM), providing mechanical strength, scaffolding for cell adhesion and migration, and a dynamic platform for biochemical signalling. Their characteristic triple-helical motifs self-assemble into fibrils and networks whose organisation varies with tissue type and functional demand. Collagen dynamics encompass synthesis of pro-collagen precursors, enzymatic modifications, secretion, extracellular cleavage, cross-linking and subsequent fragmentation or turnover by matrix metalloproteinases and endocytic pathways. Through regulated interactions with cell-surface receptors such as integrins and discoidin domain receptors, collagens transmit mechanical cues that influence cell proliferation, differentiation and survival. Aberrant collagen remodelling underlies fibrotic disease, tumour progression and impaired tissue repair, whereas engineered collagen scaffolds and mimetic peptides are advancing regenerative medicine. Emerging studies reveal that collagen isoforms and post-translational modifications fine-tune matrix stiffness and ligand availability, thereby orchestrating developmental morphogenesis, homeostasis and responses to injury. An integrated understanding of collagen assembly, organisation and degradation is critical for the design of therapeutic strategies targeting ECM-mediated pathologies and for the development of biomaterials that recapitulate native tissue mechanics.

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Collagen Dynamics in Extracellular Matrix Biology publication trend

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Technical terms

Extracellular Matrix (ECM): A complex network of proteins and polysaccharides that provides structural support and biochemical cues to cells.

Fibrillogenesis: The process by which collagen triple helices assemble into fibrils and higher-order fibres in the extracellular environment.

Matrix Metalloproteinases (MMPs): A family of zinc-dependent proteases responsible for the cleavage and remodelling of ECM components.

Integrins: Transmembrane receptors that mediate cell adhesion to ECM proteins and transduce mechanical signals into intracellular responses.

Proteoglycan: A glycoprotein with covalently attached glycosaminoglycan chains that modulates ECM hydration, growth factor binding and matrix organisation.

References

1. Collagen in the central nervous system: contributions to neurodegeneration and promise as a therapeutic target. Molecular Neurodegeneration (2024).
2. Targeting collagen XVIII improves the efficiency of ErbB inhibitors in breast cancer models. Journal of Clinical Investigation (2023).
3. Temporally and spatially regulated collagen XVIII isoforms are involved in ureteric tree development via the TSP1-like domain. Matrix Biology (2023).
4. Extracellular Collagenases and the Endocytic Receptor, Urokinase Plasminogen Activator Receptor-associated Protein/Endo180, Cooperate in Fibroblast-mediated Collagen Degradation*. Journal of Biological Chemistry (2007).
5. Mechanical signaling through the discoidin domain receptor 1 plays a central role in tissue fibrosis. Cell Adhesion & Migration (2018).
6. Collagen Type I as a Ligand for Receptor-Mediated Signaling. Frontiers in Physics (2017).