collagen

Overview

Collagen is the most abundant structural protein in the extracellular matrix of animals and a central determinant of tissue architecture, tensile strength, and mechanical signaling. It forms fibrillar and non-fibrillar networks that support skin, bone, tendon, vessel walls, and many internal organs. Beyond its structural role, collagen influences cell adhesion, migration, differentiation, wound repair, fibrosis, and tumor behavior through interactions with integrins and other matrix receptors, thereby affecting pathways such as FAK/MAPK mechanotransduction and epithelial-mesenchymal transition (EMT).

In biomedical research, collagen is studied both as a native matrix component and as a biomaterial. It is widely used in hydrogels, membranes, films, bioinks, decellularized scaffolds, and composite delivery systems because of its biocompatibility and bioactivity. At the same time, excessive collagen deposition, cross-linking, or remodeling is implicated in fibrosis, tumor stroma stiffening, and age-related tissue dysfunction, making collagen a frequent target in studies of cancer, wound healing, cardiovascular disease, and regenerative medicine.

Focus of Latest Publications

Recent publications have examined collagen in several distinct biomedical contexts, most prominently as a structural component of the extracellular matrix and as a therapeutic or biomaterial target. In castration-resistant prostate cancer, collagen-rich stroma was linked to therapy resistance and immunosuppression. Dual inhibition of DNMTs and EZH2 reactivated ADAMTS1, a collagenase, leading to collagen degradation, suppression of FAK/MAPK mechanotransduction, reversal of EMT, and marked tumor control in immunocompetent models. This strategy also increased cytotoxic CD8+ T cell infiltration and reduced immunosuppressive macrophages and Tregs, highlighting collagenolysis as part of a broader epigenetic-ECM intervention.

Other studies focused on collagen as a regenerative material or tissue component. A transdermal delivery system using ginsenoside Rh2-based liposomes was developed to improve the permeability of natural collagen for aging skin rejuvenation. The formulation preserved the collagen triple-helical structure, improved transdermal delivery more than fourfold versus free collagen, and in a photoaged mouse model reduced wrinkling, improved elasticity, and promoted restoration of skin structure and function through collagen supplementation and induction of collagen regeneration. In airway tissue engineering, decellularized airway mucosa-derived extracellular matrix retained collagen and glycosaminoglycans and outperformed collagen controls in supporting epithelial differentiation, mucociliary function, and complete re-epithelialization in a rat tracheal defect model.

Collagen was also assessed as a tissue property and as a component of engineered biomaterials. In pituitary neuroendocrine tumors, intratumoral collagen content was evaluated by digital pathology and correlated with intraoperative tumor consistency, reflecting the surgical relevance of fibrous collagen-rich tumors. In food and biomaterials research, collagen interactions were examined in bovine bone broth stabilization, where xanthan gum was reported to interact with collagen through electrostatic bonding and contribute to a more stable interfacial protein film. Separately, a biomimetic semi-IPN hydrogel platform incorporated collagen with ovalbumin and polysaccharides to create a multifunctional scaffold with improved viscoelasticity, thermal stability, cytocompatibility, hemocompatibility, antibacterial activity, reduced TNF-α expression, and enhanced mineralization.

Across these studies, collagen was investigated both as a biological barrier and as a regenerative scaffold component. The recent literature emphasizes collagen-rich extracellular matrices in disease progression and surgical behavior, while also showing that collagen-containing or collagen-preserving biomaterials can support tissue repair, epithelial regeneration, and mineralization.

Key Publications

NEWJun Targeting the DNA methylation-H3K27me3 switch reverses castration resistance and immunosuppression via ADAMTS1-driven collagenolysis. (Proceedings of the National Academy of Sciences of the United States of America, 2026, PMID 42313934): "...reactivating ADAMTS1 to degrade collagen-rich stroma, suppress FAK/MAPK mechanotransduction signaling, and reverse epithelial-mesenchymal transition (EMT)."
Jun Breaching the Skin Barrier: Efficient Transdermal Delivery of Natural Collagen for Aging Skin Rejuvenation. (Langmuir : the ACS journal of surfaces and colloids, 2026, PMID 42246872): "The supplementation of exogenous collagen is an effective strategy for combating skin aging—a complex physiological process characterized by the continuous degradation of endogenous collagen."
May Assessment of intratumoral collagen in pituitary neuroendocrine tumors (pituitary adenomas/PitNets) via digital pathology and its correlation with intraoperative consistency. (Pituitary, 2026, PMID 42177361): "This study evaluated the relationship between intraoperative tumor consistency and collagen content using digital image analysis."
May Airway mucosa-derived extracellular matrix bioink for 3D bioprinting of functional airway tissue. (Biofabrication, 2026, PMID 42030975): "HTEpCs cultured on MudECM hydrogels in vitro showed enhanced mucociliary differentiation, tight junction formation, goblet cell development, and directional mucus transport, compared to collagen controls."
Apr Enhanced stability of bovine bone broth via xanthan gum and guar gum synergy: A multiscale analysis from molecular interactions to macroscopic structure. (Food chemistry, 2026, PMID 42013772): "Molecular docking revealed that XG interacts with collagen through electrostatic bonding, while GG contributes hydrophobic interactions."
May Biomimetic Double-Protein Semi-IPN Hydrogels: Synergistic Protein-Polysaccharide Biomatrices for Healing, Immunomodulation, and Mineralization. (Biopolymers, 2026, PMID 41889002): "This study introduces a biomimetic dual-protein semi-interpenetrating polymer network (semi-IPN) platform integrating collagen (C) and the phosphorylated globular protein ovalbumin within a bioactive polyurethane (PU) cross-linked matrix."