A Lysyl Oxidase-Responsive Collagen Peptide Illuminates Collagen Remodeling in Wound Healing
A recent publication in “Matrix Biology”, which resulted from a collaboration between D-CHAB (Wennemers group) and D-BIOL (Werner group) within the frame of the SKINTEGRITY.CH project, demonstrates that an innovative chemical sensor offers visualization of collagen remodeling during tissue repair.
Tissue repair involves the dynamic remodeling of collagen, which must occur correctly to avoid adverse outcomes. Improper collagen remodeling and maturation can lead to the development of various fibrotic diseases. Lysyl oxidases (LOX) play a critical role in the collagen maturation process by oxidizing lysine (Lys) or hydroxylysine to allysine residues, thereby initiating cross-linking within and between collagen fibrils. The precise regulation of LOX is therefore crucial for proper tissue repair.
Traditional methods of examining collagen remodeling are indirect and lack specificity in detecting the extent and precise location of remodeling events. Hiebert et al. use a collagen peptide sensor to visualize collagen formation and remodeling during wound healing in mice and humans. The probe binds selectively to sites of collagen formation and remodeling at different stages of healing. Compared to conventional methods, the peptide sensor localizes in areas of collagen synthesis and remodeling at the wound edge and not in matured fibrillar collagen. The authors also demonstrate its applicability for in vivo wound imaging and for discerning differential remodeling in wounds of transgenic mice with altered collagen dynamics.
These findings show the value of the probe as a diagnostic tool to rapidly identify the sites of matrix remodeling in tissue sections, which will aid in the conception of new therapeutic strategies for fibrotic disorders and defective tissue repair.
Link to the publication in external page"Matrix Biology".