Programmed Cell Death 10 Proteins (PDCD10)

Human Programmed Cell Death 10 (PDCD10) interaction partners

1. We showed that overexpression of PDCD10 significantly inhibited miR-103-induced inhibition of cell proliferation, increased apoptosis, and decreased invasion and migration in A549 cells.

2. Data show that PDCD10 expression levels are high in bladder cancer (BC) tissues and seems to correlate with worse prognosis. PDCD10 is directly modulated by miR26a/miR26b as a target in BC cells. PDCD10 promotes BC cell proliferation in vitro and growth and progression of BC in vivo.

3. Over-expression of PDCD10 in HeLa cells increased the resistance to doxorubicin.

4. The identified endothelial signalling pathway of CCM3-DLL4/Notch-EphB4-Erk1/2 may provide an insight into mechanism of CCM3-ablation-mediated angiogenesis.

5. Case-control study to investigate the possible association of others polymorphisms (c.485+65 C/G, c.989+63 C/G, c.1980 A/G in CCM1 gene, c.472+127 C/T in CCM2 and c.150 G/A in CCM3) with cerebral cavernous malformations. The five polymorphisms were characterized in 64 sporadic patients and in 90 healthy controls by ASO-PCR. Results suggest that some polymorphisms in CCM genes could play an important role in the disease.

6. CCM3 restrains ANGPT2 release from endothelial cells and maintains endothelial junctions. CCM3 depletion leads to increased ANGPT2 release.

7. Data indicated that rs9853967 and rs11714980 polymorphisms in CCM3 and SERPINI1respectively could be associated with a protective role in cerebral cavernous malformations disease.

8. Inhibition of Notch and activation of VEGF/p38 signaling were involved in miR-425-5p/CCM3 mediated inhibition of angiogenesis by sodium arsenite.

9. Loss of endothelial programmed cell death 10 activates glioblastoma cells and promotes tumor growth.

10. Studies suggest that the 3 proteins of the Cerebral Cavernous Malformations (CCM) complex KRIT1/CCM1, CCM2/malcavernin and CCM3/PDCD10 not only require one another for reciprocal stabilization, but also act as a platform for signal transduction.

11. Study highlights the potential role of CCM3 in regulating tight junction complex organization and brain endothelial barrier permeability through CCM3-ERK1/2-cortactin cross-talk

12. A novel CCM3 missense mutation (c.422T>G) detected in 2 Greek brothers with cerebral cavernous malformations causes a loss of function in Pdcd10 protein due to its localization in the 8th helix. It affects Leu141. It may play a role in angiogenesis.

13. The proto-oncogene PDCD10 is direct target of miR-103 that can suppress Prostate cancer proliferation and migration by down-regulating the PDCD10.

14. We report for the first time that PDCD10 expression is downregulated in GBM, which is associated with the activation of Akt signaling protein

15. miR-181b was upregulated by hypoxia in retinoblastoma in an HIF-1a-independent manner. Additionally, miR-181b exerts its angiogenic function, at least in part, by inhibiting PDCD10 and GATA6.

16. Results broaden our knowledge on the mechanisms by which CCM3 deficiency results in disease and open new avenues of research into both CCM3 and senescence biology.

17. Study shows that PDCD10 mutations result in vascular permeability mediated by ROCK activity and a particularly severe clinical phenotype of patients and mouse model for cerebral cavernous malformation disease.

18. A causative mutation in the PDCD10 gene (p.Gln112PhefsX13) was identified in an Italian family with cerebral cavernous malformations associated with meningioma.

19. Our results suggest that MST4, STK25 and PDCD10 are upregulated in prostate cancer and may play roles in prostate tumorigenesis.

20. DNA mutational analysis in 87 Italian affected individuals with Cerebral cavernous malformations identified mutations in over 97.7% of cases, and PDCD10/CCM3 mutations account for 13.1% four of which already known and four novel ones.

Mouse (Murine) Programmed Cell Death 10 (PDCD10) interaction partners

1. CCM3 suppresses UNC13B- and vesicle-associated membrane protein 3 (VAMP3)-dependent exocytosis of angiopoietin 2 (ANGPT2) in brain endothelial cells. CCM3 deficiency in endothelial cells augments the exocytosis and secretion of ANGPT2, which is associated with destabilized endothelial cell junctions, enlarged lumen formation and endothelial cell-pericyte dissociation.

2. CCM3 expression and it's role during ovary and testis development

3. Study shows that PDCD10 mutations result in vascular permeability mediated by ROCK activity and a particularly severe clinical phenotype of patients and mouse model for cerebral cavernous malformation disease.

4. Data show that sulindac sulfide and sulindac sulfone, which attenuate beta-catenin transcription activity, reduce vascular malformations in endothelial programmed cell death 10 protein CCM3-deficient mice.

5. CCM3 has both cell autonomous and cell non-autonomous functions in neural progenitors and is specifically required in radial glia and newly born pyramidal neurons migrating through the subventricular zone

6. Although CCM3 stabilizes STK24, it counteracts STK24-mediated inhibition of exocytosis by recruiting STK24 away from the C2B domain through its Ca(2+)-sensitive interaction with UNC13D C2A domain.

7. Pdcd10 has a different role in cerebral cavernous malformation than Ccm2 and Krit1

8. Ccm3 has both neural cell autonomous and nonautonomous functions.

9. Stabilization of VEGFR2 signaling by cerebral cavernous malformation 3 (also known as PDCD10) is critical for vascular development.

Zebrafish Programmed Cell Death 10 (PDCD10) interaction partners

1. CCM3 plays a role distinct from CCM1/2 in Cerebral cavernous malformations pathogenesis, and acts via GCKIII activity to regulate cranial vasculature integrity and development.

2. Sequence conservation and binding studies suggest that CCM3 may preferentially heterodimerize with GCKIII proteins through a manner structurally analogous to that employed for CCM3 homodimerization.

3. The newly mapped STK25 and MST4 interaction domain within the CCM3 protein plays a crucial role for vascular development in zebrafish.