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We report a case of a highly penetrant but variably expressed form of cerebral cavernous malformation syndrome with cerebral, cutaneous, and retinal cavernomas in a family found to harbor a nonsense mutation of the CCM1 gene.
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 (show CCM2 Proteins) and c.150 G/A in CCM3 (show PDCD10 Proteins)) 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.
The finding of this study suggests that the novel nonsense mutation c.1159G>T in CCM1 gene is associated with multiple cerebral cavernous malformations, and that CCM1 haploinsufficiency may be the underlying mechanism of multiple cerebral cavernous malformations.
A novel KRIT1 heterozygous nonsense mutation (c.1864C>T) segregated with familial cerebral cavernous malformation in a Chinese family.
A novel heterozygous insertion KRIT1 mutation identified in cerebral cavernous malformation patient. mRNA level of KRIT1 were significantly decreased in FCCM subjects.
A novel nonsense mutation in CCM1 were detected in cerebral cavernous malformations patient.
nuclear-cytoplasmic shuttling of ICAP1 (show ITGB1BP1 Proteins) influences both integrin activation and KRIT1 localization, presumably impacting nuclear functions of KRIT1.
New Krit1 mutations segregated with cerebral cavernous malformation in Chinese families.
Studies suggest that the 3 proteins of the Cerebral Cavernous Malformations (CCM) complex KRIT1/CCM1, CCM2/malcavernin (show CCM2 Proteins) and CCM3/PDCD10 (show PDCD10 Proteins) not only require one another for reciprocal stabilization, but also act as a platform for signal transduction.
Valproic acid reduces intracellular ROS (show ROS1 Proteins) level by the modulation of KRIT1 and its correlated proteins, FoxO1 (show FOXO1 Proteins), SOD2 (show SOD2 Proteins), and cyclin D1 (show CCND1 Proteins) in mesenchymal stromal cells.
Data show that the reduced expression of thrombospondin1 (TSP1 (show GZMA Proteins)) that follows Krit1 inactivation contributes to cavernous malformation (CCM) lesion pathogenesis.
Lesions develop in a stereotypic location and pattern, preceded by endothelial hypersprouting as confirmed in a zebrafish model of disease. The vascular defects seen with loss of Ccm1 suggest a defect in endothelial flow response.
CCM1 silencing in endothelial cells caused decreased Notch3 (show NOTCH3 Proteins) activity in cocultured pericytes
Data indicate that vascular endothelial growth factor (VEGF (show VEGF Proteins)) signaling contributes to modifying endothelial function in Krev-interaction trapped 1 (KRIT1)-deficient cells and microvessel permeability in Krit1(+/-) mice.
The CCM1 loss resulted in ICAP-1 (show ITGB1BP1 Proteins) destabilization, which increased beta1 integrin activation and led to increased RhoA (show RHOA Proteins)-dependent contractility.
Data indicate an integral role for KRIT1 in microvessel homeostasis and the vascular response to inflammation.
Pdcd10 (show PDCD10 Proteins) has a different role in cerebral cavernous malformation than Ccm2 (show CCM2 Proteins) and Krit1
Results suggests that KRIT1 limits the accumulation of intracellular oxidants and prevents oxidative stress-mediated cellular dysfunction and DNA damage by enhancing the cell capacity to scavenge intracellular ROS (show ROS1 Proteins).
The KRIT1-CCM2 (show CCM2 Proteins) interaction regulates endothelial junctional stability and vascular barrier function by suppressing activation of the RhoA (show RHOA Proteins)/ROCK signaling pathway.
KRIT1 regulates beta-catenin (show CTNNB1 Proteins) signaling, and Krit1(+/-) mice are more susceptible to beta-catenin (show CTNNB1 Proteins)-driven intestinal adenomas.
Rap1 (show TERF2IP Proteins) increases KRIT-1 targeting to endothelial cell-cell junctions where it suppresses stress fibers and stabilizes junctional integrity.
In turn, Heg1 stabilizes levels of Krit1 protein, and both Heg1 and Krit1 dampen expression levels of klf2a, a major mechanosensitive gene. The correct balance of blood-flow-dependent induction and Krit1 protein-mediated repression of klf2a and notch1b ultimately shapes cardiac valve leaflet morphology.
CCM3 (show PDCD10 Proteins) signals through sterile 20-like kinases to regulate both endothelial and epithelial cell junctions in development and disease.
endothelial cellular morphogenesis is regulated by CCM1 proteins during development and pathogenesis. [CCM1]
the direct interaction between Rap1 (show TERF2IP Proteins) and KRIT1 is required for KRIT1 function in cardiovascular development.
Ccm1 has been identified as a key angiogenic modulator in microvascular tubulogenesis.
Zebrafish embryos with the recessive lethal mutations santa (san) and valentine (vtn (show VTN Proteins)) do not thicken, but do add the proper number of cells to the myocardium.
This gene encodes a protein containing four ankyrin repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and multiple NPXY sequences. The encoded protein is localized in the nucleus and cytoplasm. It binds to integrin cytoplasmic domain-associated protein-1 alpha (ICAP1alpha), and plays a critical role in beta1-integrin-mediated cell proliferation. It associates with junction proteins and RAS-related protein 1A (Rap1A), which requires the encoded protein for maintaining the integrity of endothelial junctions. It is also a microtubule-associated protein and may play a role in microtubule targeting. Mutations in this gene result in cerebral cavernous malformations. Multiple alternatively spliced transcript variants have been found for this gene.
ankyrin repeat-containing protein Krit1
, cerebral cavernous malformations 1 protein
, krev interaction trapped 1
, krev interaction trapped protein 1
, cerebral cavernous malformations 1 protein homolog
, Krev interaction trapped protein 1