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Dpep2  -  dipeptidase 2

Mus musculus

Synonyms: Dipeptidase 2, F630103D06Rik, MBD-2, Mbd2, Membrane-bound dipeptidase 2
 
 
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Disease relevance of Dpep2

  • In this report, we examined the antileukemia activity of MBD2 in a murine model of acute lymphoid leukemia (ALL) L1210 [1].
 

High impact information on Dpep2

  • Genetic and biochemical data together favor the view that MBD3 is a key component of the Mi-2/NuRD corepressor complex, whereas MBD2 may be one of several factors that can recruit this complex to DNA [2].
  • Similar to MeCP2, another methyl CpG-binding protein, MBD2, also increased during myogenic differentiation and could induce clustering of pericentric regions, arguing for functional redundancy [3].
  • This MeCP2- and MBD2-mediated chromatin reorganization may thus represent a molecular link between nuclear genome topology and the epigenetic maintenance of cellular differentiation [3].
  • Murine beta-defensin 2 (MBD2) is a small antimicrobial peptide of the innate immune system [1].
  • Interestingly, NK cells were also required for the MBD2-mediated antileukemia response, although ALL generally display a high degree of resistance to NK-mediated lysis [1].
 

Biological context of Dpep2

 

Anatomical context of Dpep2

  • Expression of MBD2, a component of MeCP1, starts in the blastula stage [5].
  • Expression of MBD-2 and MBD-3 in Cos cells indicated that both are membrane-bound through a glycosylphosphatidyl-inositol linkage [6].
  • MBD-1 is expressed at highest levels in kidney, lung, and heart and is absent in spleen, while MBD-2 is expressed at highest levels in lung, heart, and testis and at somewhat lower levels in spleen [6].
  • Depletion of CD8+ T cells but not CD4+ T cells completely abrogated the antileukemia activity of MBD2 [1].
  • Recent study showed that MBD2 could not only recruit immature dendritic cells but also activate them by Toll-like receptor 4 and thus may provide a critical link between the innate immune system and the adaptive immune response [1].
 

Associations of Dpep2 with chemical compounds

 

Other interactions of Dpep2

  • MBD-2 cDNA is 56% identical to MBD-1 with a predicted amino acid identity of 33% [6].
 

Analytical, diagnostic and therapeutic context of Dpep2

  • Our results suggest that MBD2 can activate both innate and adaptive immunity to generate potent antileukemia response, and MBD2 immunotherapy warrants further evaluation as a potential treatment for ALL [1].

References

 
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