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The current study identified a novel CCM1/KRIT1 heterozygous deletion mutation (c.1919delT) associated with familial cerebral cavernous malformation (FCCM). Our findings expand the CCM gene mutation profiles in the Chinese population and the mutation segregated with the disease in the family.
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 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.
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.
Adrenal calcifications identified on CT scans are common in patients with fCCM and may be a clinically silent manifestation of disease.
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 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 and CCM3/PDCD10 not only require one another for reciprocal stabilization, but also act as a platform for signal transduction.
Valproic acid reduces intracellular ROS level by the modulation of KRIT1 and its correlated proteins, FoxO1, SOD2, and cyclin D1 in mesenchymal stromal cells.
KRIT1 protects endothelial integrity during mechanical stress and trap6 exposure.
Novel CCM1 deletion mutation segregated with cerebral cavernous angioma in a Chinese family.
Case Report: cerebral cavernous malformations and unilateral moyamoya disease in a patient with a new mutation in the KRIT-1 /CCM1 gene.
Here we discuss nuclear functions of adhesion complex proteins with a special focus on the CCM-1/KRIT-1 protein, which may turn out to be yet another adhesion complex protein with a second life.
Data find that several disease-associated missense mutations in CCM2 have the potential to interrupt the KRIT1-CCM2 interaction by destabilizing the CCM2 PTB domain and that a KRIT1 mutation also disrupts this interaction
Genetic analysis of familial cerebral cavernous malformation in Japanese involved the KRIT1 gene.
Data indicate the regulatioin of vascular endothelial growth factor (VEGF) signaling in Krev-interaction trapped 1 (KRIT1)-depleted endothelial cells.
Data indicate that the major binding site for binding of sorting nexin 17 (SNX17) is confined to the NPXF2 motif in cytoplasmic adaptor protein Krev interaction trapped 1 (KRIT1).
Data show that the reduced expression of thrombospondin1 (TSP1) 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 activity in cocultured pericytes
Data indicate that vascular endothelial growth factor (VEGF) 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 destabilization, which increased beta1 integrin activation and led to increased RhoA-dependent contractility.
Data indicate an integral role for KRIT1 in microvessel homeostasis and the vascular response to inflammation.
Pdcd10 has a different role in cerebral cavernous malformation than Ccm2 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.
The KRIT1-CCM2 interaction regulates endothelial junctional stability and vascular barrier function by suppressing activation of the RhoA/ROCK signaling pathway.
KRIT1 regulates beta-catenin signaling, and Krit1(+/-) mice are more susceptible to beta-catenin-driven intestinal adenomas.
evidence of differential Krit1 and Rap1A expression during mouse ontogenesis and suggest a more widespread functional significance of Krit1, not restricted to vascular endothelial cells.
Krit1 mRNA expression during mouse development from E7.5 to E20.5 and in adult tissues
p53 plays a direct role in formation of cerebral vascular malformations by sensitizing mice with a mutation in Ccm1 (KRIT1)
A familial CCM2 missense mutation abrogates the CCM1/CCM2 interaction, suggesting that loss of this interaction may be critical in cavernous malformations pathogenesis.
CCM1 and CCM2 have similar expression patterns during development and are involved in the same pathway important for central nervous system vascular development
The structure-function relationship of the C-terminal region of KRIT1A (cerebral cavernous malformations 1A protein) and the structural and functional impact of the 39 amino acid deletion characterizing the KRIT1B isoform was characterized.
Rap1 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 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 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) 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