• Title/Summary/Keyword: selenoprotein N

Search Result 3, Processing Time 0.018 seconds

The Influence of Bisphenol A on Selenoprotein N Expression Genes during Zebrafish Embryogenesis (Bisphenol A가 Zebrafish 발생과정 중 Selenoprotein N 발현 유전자에 미치는 영향)

  • Gwak, Young-Gook;Yeo, Min-Kyeong
    • Environmental Analysis Health and Toxicology
    • /
    • v.23 no.3
    • /
    • pp.179-186
    • /
    • 2008
  • 내분비계 장애물질 중 에스트로겐성 특성을 지닌 것으로 알려진 bisphenol A에 폭로되었을 때에 나타나는 이상 증상과 selenoprotein N 결핍 증상은 유사성이 있는 것으로 관찰되었다. 이에 본 연구에서는 bisphenol A에 폭로된 생물체의 selenoprotein N 유전자 발현에 영향을 미치는지에 관해 연구하였다. 실험동물은 zebrafish (Danio rerio, wild type)의 수정란을 사용하였다. Zebrafish의 수정란은 서로 다른 농도의 bisphenol A (0.1, 1, 10 ppm)에 노출하였다. 각각의 폭로 환경에서 부화된 치어를 시료로 selenoprotein N 유전자 발현을 RT-PCR방법에 의해 알아보았다. 그 결과, bisphenol A는 척추이상과 심장이상이 나타나 selenoprotein N 이상시 나타나는 현상과 유사성을 보였다. Selenoprotein N 유전자 발현은 bisphenol A 폭로 농도가 높아짐에 따라 유전자 발현 농도가 낮아지는 것으로 관찰되었다. 특히 1 ppm 농도에서는 대조군이나 0.1 ppm 농도보다 catalase의 활성이 높게 나타나 특정 농도에서 bisphenol A에 의한 영향이 나타나는 것을 알 수 있었다.

Cell Proliferation and Motility Are Inhibited by G1 Phase Arrest in 15-kDa Selenoprotein-Deficient Chang Liver Cells

  • Bang, Jeyoung;Huh, Jang Hoe;Na, Ji-Woon;Lu, Qiao;Carlson, Bradley A.;Tobe, Ryuta;Tsuji, Petra A.;Gladyshev, Vadim N.;Hatfield, Dolph L.;Lee, Byeong Jae
    • Molecules and Cells
    • /
    • v.38 no.5
    • /
    • pp.457-465
    • /
    • 2015
  • The 15-kDa selenoprotein (Sep15) is a selenoprotein residing in the lumen of the endoplasmic reticulum (ER) and implicated in quality control of protein folding. Herein, we established an inducible RNAi cell line that targets Sep15 mRNA in Chang liver cells. RNAi-induced Sep15 deficiency led to inhibition of cell proliferation, whereas cell growth was resumed after removal of the knockdown inducer. Sep15-deficient cells were arrested at the G1 phase by upregulating p21 and p27, and these cells were also characterized by ER stress. In addition, Sep15 deficiency led to the relocation of focal adhesions to the periphery of the cell basement and to the decrease of the migratory and invasive ability. All these changes were reversible depending on Sep15 status. Rescuing the knockdown state by expressing a silent mutant Sep15 mRNA that is resistant to siRNA also reversed the phenotypic changes. Our results suggest that SEP15 plays important roles in the regulation of the G1 phase during the cell cycle as well as in cell motility in Chang liver cells, and that this selenoprotein offers a novel functional link between the cell cycle and cell motility.

Quantification of seleno proteins in Korean blood serum using solid phase extraction and affinity chromatography-inductively coupled plasma/mass spectrometry (고체상 추출과 친화 크로마토 그라피-유도결합 플라즈마 질량분석법을 이용한 한국인 혈청에서의 셀레노 단백질 정량)

  • Ahn, Ji-Yun;Kwon, Hyo-Sik;Pak, Yong-Nam
    • Analytical Science and Technology
    • /
    • v.27 no.2
    • /
    • pp.92-99
    • /
    • 2014
  • Interferences were removed using anion exchange solid phase extraction (AE SPE) in quantification of selenoproteins in Korean human blood serum with affinity high performance liquid chromatography (AF HPLC)-inductively coupled plasma/mass spectrometry (ICP/MS). The average selenium level obtained for healthy Koreans was $94.3{\pm}2.3ngg^{-1}$ using isotope dilution method. AE SPE was coupled to AF column to separate 3 selenoproteins, glutathione peroxidase GPx, selenoprotein SelP, and selenoalbumin SeAlb. Post column isotope dilution was employed to quantify the proteins. The certified reference material of human blood serum BCR-637 was analyzed to give total selenoprotein concentration of $85.4{\pm}3.4ngg^{-1}$, which agreed well with the reference value of $81{\pm}7ngg^{-1}$. The pooled concentration of GPx, SelP, and SeAlb from healthy Koreans (n=20) was $12.1{\pm}1.4ngg^{-1}$, $57.2{\pm}2.0ngg^{-1}$, and $20.0{\pm}1.9ngg^{-1}$, respectively. The sum of selenoproteins is $89.3ngg^{-1}$, which is about the same as the total selenium concentration of $94.3ngg^{-1}$. The fact suggests that selenium in blood serum is mostly consisted of selenoproteins. After the removal of interference, GPx showed a significant decrease (more than 50%) from $25.0ngg^{-1}$ to $12.1ngg^{-1}$. It was identified that the interference in blood serum was mostly from GPx and the use of AE SPE was proven to be efficient in eliminating Cl and Br that cause interference to GPx.