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- W2240728034 abstract "Thrombin is a multifunctional serine protease which plays a central role in blood coagulation. It has also been implicated in fibroproliferative disorders where it induces migration and proliferation of mesenchymal cells. Stimulation of these processes occurs via activation of PAR-1 (protease activated receptor -1). In this study we have used antisense oligonucleotides (CCCCATTGTCCCGGGCTCTG) to the PAR-1 thrombin receptor in an attempt to down-regulate PAR-1 expression and inhibit thrombin-induced fibroblast proliferation. Antisense oligonucleotides were delivered to the cells alone or complexed with lipofectin and an integrin-targetting peptide (peptide 6, [K]GACRRETAWACG), based on an αβ-specific peptide. Proliferation of human foetal lung fibroblasts (HFL-1) was assessed spectrophotometrically based on the uptake and elution of methylene blue. Thrombin (25nM) stimulated fibroblast proliferation by 54%±8% compared with cells grown in media alone. Antisense oligonucleotides at concentrations of up to 10μM alone failed to inhibit thrombin induced proliferation. However, oligonucleotides at 1μM complexed with lipofectin and an αβ integrin-targetting peptide inhibited thrombin-induced fibroblast proliferation by 76%±12% (p<0.01). Transfection with the oligonucleotide complex did not affect proliferation of fibroblasts grown in media alone. Inhibition of thrombin receptor expression may therefore provide a method of inhibiting thrombin mediated cellular effects without affecting haemostasis. These data suggest that antisense oligonucleotides to PAR-1 may be useful as antifibrotic therapies." @default.
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- W2240728034 date "1998-03-17" @default.
- W2240728034 modified "2023-09-28" @default.
- W2240728034 title "Integrin mediated uptake of antisense oligonucleotides to the PAR-1 thrombin receptor inhibits thrombin induced fibroblast proliferation" @default.
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