MROH7‐TTC4 read‐through lncRNA suppresses vascular endothelial cell apoptosis and is upregulated by inhibition of ANXA7 GTPase activity

  title={MROH7‐TTC4 read‐through lncRNA suppresses vascular endothelial cell apoptosis and is upregulated by inhibition of ANXA7 GTPase activity},
  author={Xiaoying He and Xuan Zhao and Le Su and Baoxiang Zhao and Junying Miao},
  journal={The FEBS Journal},
Apoptosis of vascular endothelial cells (VEC) is the main form of vascular injury that is closely linked to numerous cardiovascular diseases. Therefore, it is important to find new factors that can suppress VEC apoptosis. By using long noncoding RNA (lncRNA) microarray analysis, we found a new read‐through lncRNA, MROH7‐TTC4, which acted as an apoptosis inhibitor in VECs. Furthermore, by using the inhibitor (ABO) of annexin A7 (ANXA7) GTPase, we discovered that ANXA7 translocated into nucleus… 
5 Citations
Promoting TTC4 and HSP70 interaction and translocation of annexin A7 to lysosome inhibits apoptosis in vascular endothelial cells
  • Xiaoying He, Zhao-Min Lin, J. Miao
  • Biology, Chemistry
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 2020
A special mechanism by which TTC4 inhibited apoptosis via HSP70 in VECs was discovered, on the one hand, increasing TTC4 and H SP70 interaction upregulated Akt that inhibition of apoptosis was increased, and on the other hand, decreasingHSP70 and ANXA7 interaction promoted the translocation of ANXa7 to lysosome, which inhibited apoptotic through protecting the lysOSomal membrane stability.
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This study found that nuclear-enriched abundant transcript 1 (NEAT1), a lncRNA essential for the formation of nuclear body paraspeckles, is significantly repressed in primary CML cells and demonstrated that NEAT1 is regulated by c-Myc, and revealed that SFPQ regulates cell growth and death pathway-related genes, confirming its function in IM-induced apoptosis.
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The roles of ANXA7 GTPase activity in autophagy, senescence and apoptosis as well as its potential action mechanisms are summarized and discussed in the present review.
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It is suggested that TTC4 is an H SP90 co-chaperone protein which forms a link between HSP90 chaperone activity and DNA replication, and the loss of the interaction with CDC6 or with additional client proteins could provide one route through which TTC4 could influence malignant development of cells.