Steroid sulfatase (STS) is an enzym

Steroid sulfatase (STS) is an enzyme that hydrolyzes several steroids, including E1S and DHEA-S. In breast tissue, it catalyzes the biologically inactive oestrone- 3-sulfate to oestrone, which can be further metab- olized to oestradiol by 17b-HSD1. STS activity is

detected in the majority of breast cancers and activity has been correlated with the level of STS mRNA and protein expression in breast cancer cells (Suzuki et al. 2003, Pasqualini 2004). This is higher in carcinoma tissue compared with normal breast tissue (Chetrite et al. 2000, Utsumi et al. 2000, Chetrite et al. 2005), and both immunohistochemical studies and real-time reverse transcriptase (RT)-PCR have localized STS expression in carcinoma cells but not in intratumoral stromal cells (see Suzuki et al. 2005b). The importance of E1S and STS in postmenopausal breast cancer is highlighted by the following facts: E1S is the most abundant circulating oestrogen in postmenopau- sal women, it has a considerably longer half-life in plasma compared with oestrone, levels of E1S in breast tumors are considerably higher than in the plasma, and the activity of STS is 50–200 times that of aromatase (Pasqualini et al. 1996, Pasqualini & Chetrite 2005). STS mRNA expression is negatively correlated with the clinical outcome of breast cancer patients (Utsumi et al. 2000, Miyoshi et al. 2003) and it has been proposed that the sulfatase pathway is more important than the aromatase route, since aromatase mRNA expression has no diagnostic value (Reed et al. 2005).

Oestrogen sulfotransferase (EST, SULT1E1) that converts oestrogens to inactive oestrogen sulfates is present in both normal and cancerous breast tissue, and EST immunoreactivity was detected in the carcinoma cells of 44% patients with breast cancer (Suzuki et al. 2003). Despite the fact that the concentration of E1S in breast cancer tissue is 7–11 times greater than in plasma (Pasqualini et al. 1996), its significance in relation to the formation of active oestrogens in breast carcinoma cells is poorly understood.

ผลลัพธ์ (ไทย) 3:

Steroid sulfatase (STS) is an enzyme that hydrolyzes several steroids, including E1S and DHEA-S. In breast tissue, it catalyzes the biologically inactive oestrone- 3-sulfate to oestrone, which can be further metab- olized to oestradiol by 17b-HSD1. STS activity is

detected in the majority of breast cancers and activity has been correlated with the level of STS mRNA and protein expression in breast cancer cells (Suzuki et al. 2003, Pasqualini 2004). This is higher in carcinoma tissue compared with normal breast tissue (Chetrite et al. 2000, Utsumi et al. 2000, Chetrite et al. 2005),และทั้งการศึกษาในแบบเรียลไทม์ ( RT ) และ Reverse transcriptase PCR มีการแสดงออกในถิ่น STS - เซลล์มะเร็งแต่ไม่ intratumoral stromal เซลล์ ( เห็นซูซูกิ et al . 2005b ) ความสำคัญของ e1s STS และมะเร็งในเต้านม หลังถูกเน้นโดยข้อเท็จจริงต่อไปนี้ : e1s เป็นปริมาณมากที่สุดหมุนเวียนฮอร์โมนเอสโตรเจนใน postmenopau ผู้หญิง - ซัล it has a considerably longer half-life in plasma compared with oestrone, levels of E1S in breast tumors are considerably higher than in the plasma, and the activity of STS is 50–200 times that of aromatase (Pasqualini et al. 1996, Pasqualini & Chetrite 2005). STS mRNA expression is negatively correlated with the clinical outcome of breast cancer patients (Utsumi et al. 2000, Miyoshi et al. 2003) and it has been proposed that the sulfatase pathway is more important than the aromatase route, since aromatase mRNA expression has no diagnostic value (Reed et al. 2005).

Oestrogen sulfotransferase (EST, SULT1E1) that converts oestrogens to inactive oestrogen sulfates is present in both normal and cancerous breast tissue,โดยประมาณการและตรวจพบในเซลล์มะเร็งร้อยละ 44 ของผู้ป่วยมะเร็งเต้านม ( Suzuki et al . 2003 ) แม้จะมีความจริงที่ว่าปริมาณของ e1s ในเนื้อเยื่อมะเร็งเต้านม 7 – 11 ครั้งมากกว่าในพลาสมา ( pasqualini et al . 1996 ) ความสำคัญของมันในความสัมพันธ์กับการเกิดโรคมะเร็งเต้านม ใช้งานโอเอสโตรเจนในเซลล์จะไม่ค่อยเข้าใจ