Objective: To examine the expression of basic fibroblast growth factor receptor (FGF R1) and transforming growth factor-beta receptors (TGF-beta RI and TGF-beta RII) in cultured human scleral fibroblasts.
Methods: Scleral fibroblasts of passages 2-4 were used for the present studies. Polyclonal antibodies against FGF R1, TGF-beta RI and TGF-beta RII were used to detect the proteins of these receptors. Indirect immunofluorescence staining method (IIF) was used.
Results: Antibodies for FGF R1, TGF-beta RI and TGF-beta RII produced specific staining of the entire cell surface, including the cell membrane enveloping cytoplasmic projections; positive staining in some cells was most intensive in the perinuclear region. Immunostaining mainly originated from the cell membranes, indicating that the presence of the receptor proteins on the cell surface. The intensity of staining for TGF-beta RI and TGF-beta RII was relatively strong, while staining of FGF R1 was relatively weak. The cells treated with PBS instead of primary antibodies did not produce specific staining.
Conclusion: This study shows that cultured human scleral fibroblasts express the receptor protein for FGF R1, TGF-beta RI and TGF-beta RII and also indicates that these growth factors may influence these cells. Exogenous bFGF and TGF-beta administration may elicit actions through the binding with these receptors in the scleral fibroblasts.