Abstract:

BACKGROUND: Studies have confirmed that basic fibroblast growth factor (bFGF) can promote wound surface healing. Scholars have paid great attention on whether bFGF can induce fibroblastic proliferation and lead to scar hyperplasia during wound surface healing.
OBJECTIVE: To investigate the regulatory effects of bFGF on the synthesis and degradation of fibroblast I and III collagen protein.
METHODS: Hyperplastic scar tissue was obtained from patients undergoing scar plasty at the Department of Burn, First Affiliated Hospital, Sun Yat-Sen University. Fibroblasts of scar tissue were cultured by tissue block method. The second passage of cells was collected. Effects of bFGF (0-500 µg/L) on synthesis and secretion of I and III collagen protein and cell matrix metalloproteinase 1 in scar-derived fibroblasts were measured by chloramines T, RT-PCR and Western blot assay.
RESULTS AND CONCLUSION: bFGF stimulation had no effect on hydroxyproline, I and III collagen protein mRNA expression. Low mass concentration of bFGF did not affect cell matrix metalloproteinase 1 expression, but cell matrix metalloproteinase 1 expression was increased with increased mass concentration of bFGF, especially 50, 100, 500 µg/L groups (P < 0.05 or P < 0.01). Simultaneously, changes in cell matrix metalloproteinase 1 expression were identical in cells and supernatant. Results have suggested that high mass concentration of bFGF contributes to degradation of collagen protein by increasing cell matrix metalloproteinase 1 synthesis, resulting in avoiding excessive deposition of extracellular matrix.