Abstract
The prolyl 3-hydroxylase family member 4 (P3H4) (alias SC65) is implicated in a variety of physiological and pathological processes. However, little is known about the role of P3H4 in tumors. This study aimed to investigate the role of P3H4 in bladder cancer (BC) and the regulatory mechanisms that influence its expression. P3H4 was highly expressed in BC tissues. Knockdown of P3H4 inhibited BC cell proliferation, cell cycle, migration and invasion in vitro, and inhibited BC growth in vivo. We also found that ETV4 bound directly to the promoter region of P3H4 and activated its transcription. Furthermore, overexpression of ETV4 rescued the inhibition of proliferation and invasion induced by PH4 silencing. ETV4 was significantly overexpressed in the BC tissues. In conclusion, P3H4 functioned an oncogene role in BC progression, and ETV4 bound directly to the P3H4 promoter region to regulate its transcription.
Highlights
Bladder cancer (BC) is the most common malignancy of the genitourinary system, with more than 430,000 new patients worldwide affected each year [1, 2]
Statistical analysis demonstrated that high expression of prolyl 3-hydroxylase family member 4 (P3H4) in bladder cancer (BC) tissues was related to gender (Table 2)
The incidence of BC in males is 3-4 times that of females. These results suggest that P3H4 may play an oncogene function in BC
Summary
Bladder cancer (BC) is the most common malignancy of the genitourinary system, with more than 430,000 new patients worldwide affected each year [1, 2]. BC is the seventh leading cause of cancer-related deaths worldwide, accounting for 2.8% of these deaths [3]. Patients receiving aggressive treatment still face the status quo of easy recurrence, poor prognosis, low survival rate and poor quality of life [5, 6]. P3H4 acts as an endoplasmic reticulum (ER) protein that regulates bone mass homeostasis and skin fragility [12]. Studies have shown that P3H4 is expressed at high levels in bone, cartilage and skin. It forms a stable complex with P3H3 in ER and interacts with lysyl hydroxylase 1 and CYPB [13, 14]. Little is known about the role of P3H4 in BC
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