The collagen structure of C1q induces wound healing by engaging discoidin domain receptor 2.
Mol Med
; 27(1): 125, 2021 10 03.
Article
em 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.Palavras-chave
Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Complemento C1q
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Movimento Celular
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Colágeno
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Receptor com Domínio Discoidina 2
Limite:
Humans
Idioma:
En
Revista:
Mol Med
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
2021
Tipo de documento:
Article