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A novel missense mutation in CCM2 were detected in cerebral cavernous malformations patient. Several CCM2 gene polymorphisms in sporadic CCM patients were reported.
Data suggest that signaling via ANP (show NPPA Proteins)/ANPR (atrial natriuretic factor/ANP (show NPPA Proteins) receptor (show PPP5C Proteins)) in vascular endothelial cells activates PAK4 (p21-activated kinase 4 (show PAK4 Proteins)) and CCM2 (cerebral cavernous malformation 2 protein), resulting in phosphorylation of MLC (myosin light chain), cytoskeletal reorganization, and cell spreading; kinase homology domain of ANPRA (guanylyl cyclase-A (show NPR1 Proteins)) activates downstream targets of ANP (show NPPA Proteins)/ANPR signaling.
Studies suggest that the 3 proteins of the Cerebral Cavernous Malformations (CCM) complex KRIT1/CCM1 (show KRIT1 Proteins), CCM2/malcavernin and CCM3/PDCD10 (show PDCD10 Proteins) not only require one another for reciprocal stabilization, but also act as a platform for signal transduction.
a new mutation in MGC4607/CCM2 was identified in several family members with spinal and cutaneous angiomas.
both CCM2 and CCM3 (show PDCD10 Proteins) are required for normal endothelial cell network formation.
Data find that several disease-associated missense mutations in CCM2 have the potential to interrupt the KRIT1 (show KRIT1 Proteins)-CCM2 interaction by destabilizing the CCM2 PTB (show PTBP1 Proteins) domain and that a KRIT1 (show KRIT1 Proteins) mutation also disrupts this interaction
Prevalence, frequency and characterization of CCM1 (show KRIT1 Proteins), CCM2 and CCM3 (show PDCD10 Proteins) variants in cerebral cavernous malformation Spanish patients.
Cerebral cavernous malformation(CCM)s develop because of loss of heart of glass (HEG (show HEG1 Proteins))-independent CCM2 signaling in murine transgenic endothelium of central nervous system after birth.
DNA sequencing and deletion/duplication testing of the CCM1 (show KRIT1 Proteins), CCM2, and CCM3 (show PDCD10 Proteins) genes in the proband revealed a CCM1 (show KRIT1 Proteins) c.601CNG mutation.
CCM2 mutations are associated with cerebral cavernous malformation in some Japanese patients.
Loss of CCM2 is associated with Cerebral Cavernous Malformations.
CCM2 expression and it's role during ovary and testis development
CCM2:MEKK3 (show MAP3K3 Proteins)-mediated regulation of Rho-ROCK signalling is required for maintenance of neurovascular integrity, a mechanism by which CCM2 loss leads to disease.
Down-modulation of STK25 (show STK25 Proteins), but not STK24 (show STK24 Proteins), rescued medulloblastoma cells from NGF (show NGFB Proteins)-induced TrkA (show NTRK1 Proteins)-dependent cell death, suggesting that STK25 (show STK25 Proteins) is part of the death-signaling pathway initiated by TrkA (show NTRK1 Proteins) and CCM2.
The inducible deletion of Ccm2 in adult mice recapitulates the cerebral cavernous malformations-like brain lesions in humans.
Developmental timing of CCM2 loss influences cerebral cavernous malformations in mice.
Rac1/osmosensing scaffold for MEKK3 contributes via phospholipase C (show PLC Proteins)-gamma1 to activation of the osmoprotective transcription factor NFAT5 (show NFAT5 Proteins).
Pdcd10 (show PDCD10 Proteins) has a different role in cerebral cavernous malformation than Ccm2 and Krit1 (show KRIT1 Proteins)
The KRIT1 (show KRIT1 Proteins)-CCM2 interaction regulates endothelial junctional stability and vascular barrier function by suppressing activation of the RhoA (show RHOA Proteins)/ROCK signaling pathway.
CCM1 (show KRIT1 Proteins) associates with CCM2, indicating that the genetic heterogeneity observed in familial cavernous malformation pathogenesis may reflect mutation of different molecular members of a coordinated signaling complex.
This gene encodes a scaffold protein that functions in the stress-activated p38 Mitogen-activated protein kinase (MAPK) signaling cascade. The protein interacts with SMAD specific E3 ubiquitin protein ligase 1 (also known as SMURF1) via a phosphotyrosine binding domain to promote RhoA degradation. The protein is required for normal cytoskeletal structure, cell-cell interactions, and lumen formation in endothelial cells. Mutations in this gene result in cerebral cavernous malformations. Multiple transcript variants encoding different isoforms have been found for this gene.
cerebral cavernous malformations 2 protein
, cerebral cavernous malformation 2
, cerebral cavernous malformation 2 homolog
, cerebral cavernous malformations protein 2 homolog
, osmosensing scaffold for MEKK3