OBJECTIVES: To investigate whether tissue expression of plasminogen activator inhibitor type 1 (PAI-1) is increased in the fibrotic plaque of human Peyronie's disease (PD). Increased tissue levels of PAI-1, an inhibitor of both fibrinolysis and collagenolysis, have been found in a variety of fibrotic conditions. Recently, it was reported that PAI-1 expression was also increased in the fibrotic plaque of an animal model of PD induced by the injection of fibrin into the tunica albuginea (TA) of the penis. METHODS: Tissue (n = 10/group) and cells (n = 4/group) obtained from the penile TA plaque of patients with PD or from normal TA were subjected to RNA extraction and real-time reverse transcriptase-polymerase chain reaction. Tissues were also analyzed by immunohistochemistry (n = 8/group) for the detection of PAI-1 expression at the transcription and protein levels. RESULTS: A significant 3.5-fold to 16-fold increase was found in both PAI-1 mRNA and protein levels in the human PD plaque and the respective fibroblast cultures compared with the normal non-PD TA. CONCLUSIONS: The observed increase in PAI-1 in the human PD plaque agrees with what has been observed in the rat and suggests that PAI-1 may be a key pro-fibrotic factor in the development of human PD.
OBJECTIVES: To investigate whether tissue expression of plasminogen activator inhibitor type 1 (PAI-1) is increased in the fibrotic plaque of humanPeyronie's disease (PD). Increased tissue levels of PAI-1, an inhibitor of both fibrinolysis and collagenolysis, have been found in a variety of fibrotic conditions. Recently, it was reported that PAI-1 expression was also increased in the fibrotic plaque of an animal model of PD induced by the injection of fibrin into the tunica albuginea (TA) of the penis. METHODS: Tissue (n = 10/group) and cells (n = 4/group) obtained from the penile TA plaque of patients with PD or from normal TA were subjected to RNA extraction and real-time reverse transcriptase-polymerase chain reaction. Tissues were also analyzed by immunohistochemistry (n = 8/group) for the detection of PAI-1 expression at the transcription and protein levels. RESULTS: A significant 3.5-fold to 16-fold increase was found in both PAI-1 mRNA and protein levels in the humanPD plaque and the respective fibroblast cultures compared with the normal non-PD TA. CONCLUSIONS: The observed increase in PAI-1 in the humanPD plaque agrees with what has been observed in the rat and suggests that PAI-1 may be a key pro-fibrotic factor in the development of humanPD.