The collagen structure of C1q induces wound healing by engaging discoidin domain receptor 2.
Mol Med
; 27(1): 125, 2021 10 03.
Article
in En
| MEDLINE
| ID: mdl-34602056
ABSTRACT
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.Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Complement C1q
/
Cell Movement
/
Collagen
/
Discoidin Domain Receptor 2
Limits:
Humans
Language:
En
Journal:
Mol Med
Journal subject:
BIOLOGIA MOLECULAR
Year:
2021
Type:
Article