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- W1966682240 abstract "Laminin α 3 chain, a functionally key subunit of laminin-5, contains a large globular module (G module) which consists of a tandem repeat of five homologous LG modules (LG1∼ 5). We previously demonstrated that the LG4 module of laminin α 3 chain (α 3 LG4) induces a matrix metalloproteinase-1 (MMP-1) expression through the interaction with syndecans leading to MAPK activation/IL-1β expression signaling loop (Utani et al., J. Biol. Chem. 278, 34483–34490, 2003). Here, we show that a recombinant α 3 LG4 and synthetic peptides containing syndecan binding motif induced a cell motility and a MMP-9 expression in ketarinocytes. The synthetic peptide (A3G756)-induced cell migration and MMP-9 upregulation were inhibited by each application of a heparin and an IL-1 receptor antagonist (IL-1RA), suggesting the involvement of syndecans and IL-1β autocrine. Furthermore, the A3G756-induced cell motility was inhibited by an MMP-9 inhibitor and a neutralizing antibody of MMP-9, indicating induced cell motility was dependent on an MMP-9 activity. Taken these together, laminin-5 α 3 LG4 module may play an important role in re-epithelialization at tissue remodeling." @default.
- W1966682240 created "2016-06-24" @default.
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- W1966682240 date "2005-01-01" @default.
- W1966682240 modified "2023-10-15" @default.
- W1966682240 title "Lamininα3 LG4 Module Induces Keratinocyte Migration: Involvement of Matrix Metalloproteinase-9" @default.
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- W1966682240 doi "https://doi.org/10.1081/rrs-200047870" @default.
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