Disease relevance of MAGED1

• The data demonstrate the importance of human NRAGE in homotypic cell-to-cell adhesion and illuminate the mechanism of human NRAGE in the process of inhibition of cell adhesion, which suggests that human NRGAE plays a potential negative role in cancer metastasis [1].
• Tissue distribution of a melanoma-associated antigen D-1 immunogenic in patients with melanoma [2].

High impact information on MAGED1

• It was also found that the majority of cellular Dlxin-1 is retained in the membrane fractions of wild-type but not Ror2-/- mouse embryonic fibroblasts [3].
• Glutathione S-transferase pull-down and immunoprecipitation/Western blotting assays following co-transfection of Dlxin-1 and Praja1 revealed that Praja1 binds to the C-terminal necdin homology domain of Dlxin-1 in vitro and in vivo, respectively [4].
• Transfection and reporter gene assays indicate that Dlxin-1 activates the transcriptional function of Dlx5 [5].
• During embryogenesis, a strong signal for Dlxin-1 mRNA was found in cell layers surrounding cartilaginous elements in bone rudiment during digit formation [5].
• Therefore, Dlxin-1 may act as a regulator of the function of Dlx family members in bone formation [5].

Biological context of MAGED1

• Chromosome mapping linked MAGED1 to marker AFM119xd6 (DXS1039) on chromosome Xp11.23 [6].
• When overexpressed in 32D cells NRAGE augments interleukin-3 withdrawal induced apoptosis, possibly through binding endogenous XIAP [7].
• Moreover, the cell cycle inhibiting protein p21(WAF) is induced by hNRAGE in a p53 dependent manner [8].
• The data provide original evidence that hNRAGE arrests cell growth through a p53 dependent pathway [8].
• Interestingly, hNRAGE also increases the p53 protein level as well as its phosphorylation (Ser392) [8].

Anatomical context of MAGED1

• Northern hybridization and RT-PCR demonstrated that the expression level of MAGED1 in different normal adult tissues is comparable to that in testis and fetal liver [6].
• Dlxin-1 mRNA is expressed in various adult tissues, but not the spleen, and also in osteoblastic and chondrogenic cell lines [5].
• Further studies demonstrated that hNRAGE does not affect the proliferation of mouse p53-/- embryonic fibroblasts, suggesting that p53 function is required for hNRAGE induced cell cycle arrest [8].

Physical interactions of MAGED1

• NRAGE additionally coimmunoprecipitates with XIAP [7].

Regulatory relationships of MAGED1

• Among the other MAGE family members only MAGEB2 and -C1 and the broadly expressed MAGED1, -D2, -F1 and -H1 were expressed in RCC [9].

Other interactions of MAGED1

• We have identified a novel member of the MAGE gene family, MAGED1 [6].
• More importantly, knock down of NRAGE by RNA interference in PANC-1 cell significantly reinforces E-cadherin/beta-catenin homotypic cell adhesion [1].
• Synchronously, NRAGE also decreases the total protein level of beta-catenin, especially when NRAGE expresses for a long time [1].
• We show that AEG3482 blocks apoptosis induced by the p75 neurotrophin receptor (p75NTR) or its cytosolic interactor, NRAGE, and demonstrate that AEG3482 blocks proapoptotic JNK activity [10].

References