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Inhibition of Notch1 signaling by Runx2 during osteoblast differentiation
Ann, Eun-Jung,Kim, Hwa-Young,Choi, Yun-Hee,Kim, Mi-Yeon,Mo, Jung-Soon,Jung, Jane,Yoon, Ji-Hye,Kim, Su-Man,Moon, Jeong-Sik,Seo, Mi-Sun,Hong, Ji-Ae,Jang, Won-Gu,Shore, Paul,Komori, Toshihisa,Koh, Jeong- Wiley (John WileySons) 2011 Journal of bone and mineral research Vol.26 No.2
Mo, Jung-Soon,Jung, Jane,Yoon, Ji-Hye,Hong, Ji-Ae,Kim, Mi-Yeon,Ann, Eun-Jung,Seo, Mi-Sun,Choi, Yun-Hee,Park, Hee-Sae Wiley Subscription Services, Inc., A Wiley Company 2010 Journal of cellular biochemistry Vol.110 No.1
<P>DJ-1 has been reported as a gene linked to early onset familial Parkinson's disease, and is functionally involved in transcriptional regulation and oxidative stress-induced cell death. To understand the role of DJ-1 in cellular stress, this study investigated DJ-1's effect on stress-activated protein kinase signaling and H<SUB>2</SUB>O<SUB>2</SUB>-induced activation of apoptosis signal-regulating kinase 1 (ASK1). According to the results, the overexpression of DJ-1 inhibited H<SUB>2</SUB>O<SUB>2</SUB>-induced activation of ASK1 as well as the activation of downstream kinases in the p38 mitogen-activated protein kinase (MAPK) signaling cascade. The results of both in vivo binding and kinase studies have revealed that ASK1 is the direct target of DJ-1, whereas it has shown no effect on either MKK3 or p38. DJ-1 blocked both the homo-oligomerization of ASK1 and inhibited ASK1 activity. Taken together, our data strongly suggest that DJ-1, by directly inhibiting ASK1, may act as a negative regulator in ASK1 signaling cascades. J. Cell. Biochem. 110: 229–237, 2010. © 2010 Wiley-Liss, Inc.</P>
Mo, Jung-Soon,Ann, Eun-Jung,Yoon, Ji-Hye,Jung, Jane,Choi, Yun-Hee,Kim, Hwa-Young,Ahn, Ji-Seon,Kim, Su-Man,Kim, Mi-Yeon,Hong, Ji-Ae,Seo, Mi-Sun,Lang, Florian,Choi, Eui-Ju,Park, Hee-Sae Cambridge University Press 2011 Journal of cell science Vol.124 No.1
<P>Notch is a transmembrane protein that acts as a transcriptional factor in the Notch signaling pathway for cell survival, cell death and cell differentiation. Notch1 and Fbw7 mutations both lead the activation of the Notch1 pathway and are found in the majority of patients with the leukemia T-ALL. However, little is known about the mechanisms and regulators that are responsible for attenuating the Notch signaling pathway through Fbw7. Here, we report that the serum- and glucocorticoid-inducible protein kinase SGK1 remarkably reduced the protein stability of the active form of Notch1 through Fbw7. The protein level and transcriptional activity of the Notch1 intracellular domain (Notch1-IC) were higher in SGK1-deficient cells than in SGK1 wild-type cells. Notch1-IC was able to form a trimeric complex with Fbw7 and SGK1, thereby SGK1 enhanced the protein degradation of Notch1-IC via a Fbw7-dependent proteasomal pathway. Furthermore, activated SGK1 phosphorylated Fbw7 at serine 227, an effect inducing Notch1-IC protein degradation and ubiquitylation. Moreover, accumulated dexamethasone-induced SGK1 facilitated the degradation of Notch1-IC through phosphorylation of Fbw7. Together our results suggest that SGK1 inhibits the Notch1 signaling pathway via phosphorylation of Fbw7.</P>
Yi, Ann,Cho, Nariya,Im, Seock-Ah,Chang, Jung Min,Kim, Seung Ja,Moon, Hyeung-Gon,Han, Wonshik,Park, In-Ae,Noh, Dong-Young,Moon, Woo Kyung RSNA 2013 Radiology Vol.268 No.3
<P>Patients with tumors that had smaller reductions of enhancing volume and washout component on dynamic contrast agent–enhanced MR imaging before and after neoadjuvant chemotherapy showed increased recurrence and mortality risks compared with those who had greater reductions in tumor volume and washout component.</P>