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Protocadherin 12

PCDH12, protocadherin 12, vascular endothelial cadherin-2, VE-cadherin 2, VE-cad-2
This gene belongs to the protocadherin gene family, a subfamily of the cadherin superfamily. The encoded protein consists of an extracellular domain containing 6 cadherin repeats, a transmembrane domain and a cytoplasmic tail that differs from those of the classical cadherins. The gene localizes to the region on chromosome 5 where the protocadherin gene clusters reside. The exon organization of this transcript is similar to that of the gene cluster transcripts, notably the first large exon, but no significant sequence homology exists. The function of this cellular adhesion protein is undetermined but mouse protocadherin 12 does not bind catenins and appears to have no affect on cell migration or growth. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Protocadherin, Protocadherins, VE-cadherin, HAD, ACID
Papers on PCDH12
Treatment of pregnant spiny mice at mid gestation with a synthetic glucocorticoid has sex-dependent effects on placental glycogen stores.
Dickinson et al., Australia. In Placenta, 2013
METHOD: We examined the short and long term consequences of a single, 60 h exposure to DEX at mid gestation on the glycogen pathway in the placenta of the spiny mouse, with a focus on identifying sex-dependent differences in expression of genes involved in glycogen cell formation (PCDH12), and regulation of glycogen synthesis (GSK3B, GYS1, GBE1, FOXO1, UGP2).
Gestational protein restriction affects trophoblast differentiation.
Yallampalli et al., Galveston, United States. In Front Biosci (elite Ed), 2012
At Day 18 of pregnancy, PR increased expressions of Esrrb, Id1 andId2 (trophoblast stem cell markers), decreased expressions of Ascl2 (spongiotrophblast cell marker) and Prl2c1 (trophoblast giant cell marker), but did not alter expressions of Gjb3 and Pcdh12(glycogen cell markers) in the junctional zone (JZ).
Cadherins and neuropsychiatric disorders.
Hübner et al., Jena, Germany. In Brain Res, 2012
For example, CDH15 and PCDH19 are associated with cognitive impairment; CDH5, CDH8, CDH9, CDH10, CDH13, CDH15, PCDH10, PCDH19 and PCDHb4 with autism; CDH7, CDH12, CDH18, PCDH12 and FAT with bipolar disease and schizophrenia; and CDH11, CDH12 and CDH13 with methamphetamine and alcohol dependency.
Protocadherin-12 deficiency leads to modifications in the structure and function of arteries in mice.
Faury et al., Grenoble, France. In Pathol Biol (paris), 2012
The reactivity to acetylcholine and the circumferential mid-wall stress decreased with ageing in the PCDH12(-/-) mice, as opposed to the increase observed in the wild types.
Protocadherin-12 cleavage is a regulated process mediated by ADAM10 protein: evidence of shedding up-regulation in pre-eclampsia.
Huber et al., Grenoble, France. In J Biol Chem, 2011
PCDH12 may play an important role in human placental development, and proteolytic cleavage in response to external factors, such as cytokines and pathological settings, regulates its activity
Non-clustered protocadherin.
Kim et al., Seoul, South Korea. In Cell Adh Migr, 2011
The phylogenetic analysis with full sequences of non-clustered PCDHs enabled them to be further classified into three subgroups: δ1 (PCDH1, PCDH7, PCDH9, PCDH11 and PCDH20), δ2 (PCDH8, PCDH10, PCDH12, PCDH17, PCDH18 and PCDH19) and ε (PCDH15, PCDH16, PCDH21 and MUCDHL).
Fine mapping of the hereditary haemorrhagic telangiectasia (HHT)3 locus on chromosome 5 excludes VE-Cadherin-2, Sprouty4 and other interval genes.
Shovlin et al., London, United Kingdom. In J Angiogenes Res, 2009
Strong candidates VE-cadherin-2 and Sprouty4 cannot be HHT3.
Polymorphisms in genes involved in neurodevelopment may be associated with altered brain morphology in schizophrenia: preliminary evidence.
Dias-Neto et al., São Paulo, Brazil. In Psychiatry Res, 2009
A putative association was also found between protocadherin 12 and cortical folding (asymmetry coefficient of gyrification index).
Protocadherin 12 deficiency alters morphogenesis and transcriptional profile of the placenta.
Huber et al., Grenoble, France. In Physiol Genomics, 2008
Loss of PCDH12 leads to morphological alterations of the placenta and to notable changes in its gene expression profile.
Tracing the glycogen cells with protocadherin 12 during mouse placenta development.
Huber et al., Grenoble, France. In Placenta, 2006
We previously established that GC specifically expressed protocadherin 12 (PCDH12).
Endothelial cadherins and tumor angiogenesis.
Dejana et al., Italy. In Exp Cell Res, 2006
T cadherin, R-cadherin and VE-cadherin 2 were found in specific regions of the vascular tree but their role in vascular development or angiogenesis is still unclear.
Protocadherin 12 (VE-cadherin 2) is expressed in endothelial, trophoblast, and mesangial cells.
Huber et al., Grenoble, France. In Exp Cell Res, 2005
PCDH12 has a unique expression pattern and its deficiency does not lead to conspicuous abnormalities; it is the first specific marker for both glycogen-rich trophoblasts and mesangial cells.
cDNA cloning, chromosomal mapping, and expression analysis of human VE-Cadherin-2.
Pytowski et al., New York City, United States. In Mamm Genome, 2000
Murine vascular endothelial cadherin-2 (VE-cad-2) is a cellular adhesion molecule that is distinct from vascular endothelial cadherin 1 (VE-cad-1) in that it does not interact with catenins and does not appear to affect cell migration or growth.
Large exons encoding multiple ectodomains are a characteristic feature of protocadherin genes.
Maniatis et al., Cambridge, United States. In Proc Natl Acad Sci U S A, 2000
These genes include protocadherin 12 (Pcdh12), an ortholog of the mouse vascular endothelial cadherin-2 gene; hFmi1 and hFmi2, homologs of the Drosophila planar cell polarity gene, flamingo; hFat2, a homolog of the Drosophila tumor suppressor gene fat; and the Drosophila DN-cadherin and DE-cadherin genes.
Identification of a novel cadherin (vascular endothelial cadherin-2) located at intercellular junctions in endothelial cells.
Dejana et al., Milano, Italy. In J Biol Chem, 1998
We propose for this new protein the name of vascular endothelial cadherin-2.
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