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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 (zeige NPPA Proteine)/ANPR (atrial natriuretic factor/ANP (zeige NPPA Proteine) receptor (zeige PPP5C Proteine)) in vascular endothelial cells activates PAK4 (p21-activated kinase 4 (zeige PAK4 Proteine)) 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 (zeige NPR1 Proteine)) activates downstream targets of ANP (zeige NPPA Proteine)/ANPR signaling.
Studies suggest that the 3 proteins of the Cerebral Cavernous Malformations (CCM) complex KRIT1/CCM1 (zeige KRIT1 Proteine), CCM2/malcavernin and CCM3/PDCD10 (zeige PDCD10 Proteine) 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 (zeige PDCD10 Proteine) 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 (zeige KRIT1 Proteine)-CCM2 interaction by destabilizing the CCM2 PTB (zeige PTBP1 Proteine) domain and that a KRIT1 (zeige KRIT1 Proteine) mutation also disrupts this interaction
Prevalence, frequency and characterization of CCM1 (zeige KRIT1 Proteine), CCM2 and CCM3 (zeige PDCD10 Proteine) variants in cerebral cavernous malformation Spanish patients.
Cerebral cavernous malformation(CCM)s develop because of loss of heart of glass (HEG (zeige HEG1 Proteine))-independent CCM2 signaling in murine transgenic endothelium of central nervous system after birth.
DNA sequencing and deletion/duplication testing of the CCM1 (zeige KRIT1 Proteine), CCM2, and CCM3 (zeige PDCD10 Proteine) genes in the proband revealed a CCM1 (zeige KRIT1 Proteine) c.601CNG mutation.
CCM2 mutations are associated with cerebral cavernous malformation in some Japanese patients.
CCM2 expression and it's role during ovary and testis development
CCM2:MEKK3 (zeige MAP3K3 Proteine)-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 (zeige STK25 Proteine), but not STK24 (zeige STK24 Proteine), rescued medulloblastoma cells from NGF (zeige NGFB Proteine)-induced TrkA (zeige NTRK1 Proteine)-dependent cell death, suggesting that STK25 (zeige STK25 Proteine) is part of the death-signaling pathway initiated by TrkA (zeige NTRK1 Proteine) 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 (zeige PLC Proteine)-gamma1 to activation of the osmoprotective transcription factor NFAT5 (zeige NFAT5 Proteine).
Pdcd10 (zeige PDCD10 Proteine) has a different role in cerebral cavernous malformation than Ccm2 and Krit1 (zeige KRIT1 Proteine)
The KRIT1 (zeige KRIT1 Proteine)-CCM2 interaction regulates endothelial junctional stability and vascular barrier function by suppressing activation of the RhoA (zeige RHOA Proteine)/ROCK signaling pathway.
CCM1 (zeige KRIT1 Proteine) 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.
CCM1 (zeige KRIT1 Proteine) and CCM2 have similar expression patterns during development and are involved in the same pathway important for central nervous system vascular development
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 malformation 2
, cerebral cavernous malformations 2 protein
, cerebral cavernous malformation 2 homolog
, cerebral cavernous malformations protein 2 homolog
, osmosensing scaffold for MEKK3