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The collagen structure of C1q induces wound healing by engaging discoidin domain receptor 2
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The collagen structure of C1q induces wound healing by engaging discoidin domain receptor 2
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Journal Article
The collagen structure of C1q induces wound healing by engaging discoidin domain receptor 2
2021
Overview
Background
C1q has been reported to reveal complement-independent roles in immune and non-immune cells. C1q binds to its specific receptors to regulate distinct functions that rely on the environment and cell types. Discoidin domain receptor 2 (DDR2) is activated by collagen and functions in wound healing by controlling matrix metalloproteinase (MMP) expression. Since C1q exhibits a collagen-like structure, we hypothesized that C1q might engage DDR2 to regulate wound healing and extracellular matrix (ECM) remodeling.
Methods
Cell-based assay, proximity ligation assay, ELISA, and surface plasmon analysis were utilized to investigate DDR2 and C1q binding. We also investigate the C1q-mediated in vitro wound healing ability using the human fibrosarcoma cell line, HT1080.
Results
C1q induced the phosphorylation of DDR2, p38 kinase, and ERK1/2. C1q and DDR2 binding improved cell migration and induced MMP2 and MMP9 expression. DDR2-specific shRNA reduced C1q-mediated cell migration for wound healing.
Conclusions
C1q is a new DDR2 ligand that promotes wound healing. These findings have therapeutic implications in wound healing-related diseases.
Publisher
BioMed Central,BMC
Subject
/ Biomedical and Life Sciences
/ C1q
/ Collagen
/ DDR2
/ Discoidin Domain Receptor 1 - genetics
/ Discoidin Domain Receptor 1 - metabolism
/ Discoidin Domain Receptor 2 - genetics
/ Discoidin Domain Receptor 2 - metabolism
/ Humans
/ Matrix Metalloproteinase 2 - genetics
/ Matrix Metalloproteinase 2 - metabolism
/ Matrix Metalloproteinase 9 - genetics
