Abstract:
:We investigated whether activation of integrin receptors could modulate the expression of monocyte chemotactic protein-1 (MCP-1) in human hepatic stellate cells (HSC), mesenchymal cells responsible for extracellular matrix synthesis within the liver. When compared to non-adherent cells, HSC plated on collagen types I or IV, or fibronectin, showed increased MCP-1 gene expression and protein secretion in the conditioned medium. Increased MCP-1 secretion was also observed when cells were plated on dishes coated with a monoclonal antibody directed against the beta1-integrin subunit, demonstrating that ligation of beta1-integrins is sufficient to stimulate MCP-1 expression. Conversely, integrin-independent cell adhesion on poly-L-lysine did not modify MCP-1 secretion. Disruption of the actin cytoskeleton by cytochalasin D blocked the collagen-dependent increase in MCP-1 secretion. Chemotactic assay of HSC-conditioned medium showed that HSC plated on collagen secrete higher amounts of chemotactic factors for lymphomonocytes, and that MCP-1 accounts for the great majority of this effect. These findings indicate a novel mechanism of MCP-1 regulation possibly relevant in those conditions where HSC interact with an altered extracellular matrix.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Marra F,Pastacaldi S,Romanelli RG,Pinzani M,Ticali P,Carloni V,Laffi G,Gentilini Pdoi
10.1016/s0014-5793(97)01004-1subject
Has Abstractpub_date
1997-09-08 00:00:00pages
221-5issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(97)01004-1journal_volume
414pub_type
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