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PDCD10 encodes an evolutionarily conserved protein associated with cell apoptosis. Additionally we are shipping PDCD10 Antibodies (69) and and many more products for this protein.
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Over-expression of PDCD10 in HeLa cells increased the resistance to doxorubicin.
The identified endothelial signalling pathway of CCM3-DLL4 (show DLL4 Proteins)/Notch (show NOTCH1 Proteins)-EphB4 (show EPHB4 Proteins)-Erk1/2 may provide an insight into mechanism of CCM3-ablation-mediated angiogenesis.
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 (show KRIT1 Proteins) gene, c.472+127 C/T in CCM2 (show CCM2 Proteins) 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.
CCM3 restrains ANGPT2 release from endothelial cells and maintains endot (show VAMP3 Proteins)helial junctions. CCM3 depletion leads to increa (show ANGPT2 Proteins)sed ANGPT2 release.
Data indicated that rs9853967 and rs11714980 polymorphisms in CCM3 and SERPINI1respectively could be associated with a protective role in cerebral cavernous malformations disease.
Inhibition of Notch (show NOTCH1 Proteins) and activation of VEGF (show VEGFA Proteins)/p38 (show CRK Proteins) signaling were involved in miR (show MLXIP Proteins)-425-5p/CCM3 mediated inhibition of angiogenesis by sodium arsenite.
Loss of endothelial programmed cell death 10 activates glioblastoma cells and promotes tumor growth.
Studies suggest that the 3 proteins of the Cerebral Cavernous Malformations (CCM) complex KRIT1/CCM1 (show KRIT1 Proteins), CCM2/malcavernin (show CCM2 Proteins) and CCM3/PDCD10 not only require one another for reciprocal stabilization, but also act as a platform for signal transduction.
Study highlights the potential role of CCM3 in regulating tight junction complex organization and brain endothelial barrier permeability through CCM3-ERK1/2-cortactin (show CTTN Proteins) cross-talk
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.
CCM3 suppresses UNC13B- and vesicle-associated membrane protein 3 (VAMP3 (show VAMP3 Proteins))-dependent exocytosis of angiopoietin 2 (ANGPT2 (show ANGPT2 Proteins)) in brain endothelial cells. CCM3 deficiency in endothelial cells augments the exocytosis and secretion of ANGPT2 (show ANGPT2 Proteins), which is associated with destabilized endothelial cell junctions, enlarged lumen formation and endothelial cell-pericyte dissociation.
CCM3 expression and it's role during ovary and testis development
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.
Data show that sulindac sulfide (show SQRDL Proteins) and sulindac sulfone, which attenuate beta-catenin (show CTNNB1 Proteins) transcription activity, reduce vascular malformations in endothelial programmed cell death 10 protein CCM3-deficient mice.
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
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.
Pdcd10 has a different role in cerebral cavernous malformation than Ccm2 (show CCM2 Proteins) and Krit1 (show KRIT1 Proteins)
Ccm3 has both neural cell autonomous and nonautonomous functions.
Stabilization of VEGFR2 (show KDR Proteins) signaling by cerebral cavernous malformation 3 (also known as PDCD10) is critical for vascular development.
CCM3 plays a role distinct from CCM1 (show KRIT1 Proteins)/2 in Cerebral cavernous malformations pathogenesis, and acts via GCKIII activity to regulate cranial vasculature integrity and development.
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.
The newly mapped STK25 (show STK25 Proteins) and MST4 (show MST4 Proteins) interaction domain within the CCM3 protein plays a crucial role for vascular development in zebrafish.
This gene encodes an evolutionarily conserved protein associated with cell apoptosis. The protein interacts with the serine/threonine protein kinase MST4 to modulate the extracellular signal-regulated kinase (ERK) pathway. It also interacts with and is phosphoryated by serine/threonine kinase 25, and is thought to function in a signaling pathway essential for vascular developent. Mutations in this gene are one cause of cerebral cavernous malformations, which are vascular malformations that cause seizures and cerebral hemorrhages. Multiple alternatively spliced variants, encoding the same protein, have been identified.
TF-1 cell apoptosis-related protein 15
, apoptosis-related protein 15
, cerebral cavernous malformations 3 protein
, programmed cell death protein 10
, programmed cell death 10
, programmed cell death protein 10-A