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Human Polyclonal PKD2 Primary Antibody for IHC (p), ELISA - ABIN543268
Watnick, He, Wang, Liang, Parfrey, Hefferton, St George-Hyslop, Germino, Pei: Mutations of PKD1 in ADPKD2 cysts suggest a pathogenic effect of trans-heterozygous mutations. in Nature genetics 2000
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Human Polyclonal PKD2 Primary Antibody for ELISA, WB - ABIN4346790
Fencl, Janda, Bláhová, Hríbal, Stekrová, Puchmajerová, Seeman: Genotype-phenotype correlation in children with autosomal dominant polycystic kidney disease. in Pediatric nephrology (Berlin, Germany) 2009
Identification of PKD1 and PKD2 gene variants in a cohort of 125 Asian Indian patients of ADPKD.
Expression of PC1DeltaL and PC2 complexes in transfected CHO cells failed to support PC2 channel activity, suggesting that the role of PC1 is to activate G-protein signaling to regulate the PC1/PC2 calcium channel.
The present study for the first time demonstrates that PKD2 functions to promote autophagy under glucose starvation, thereby protects cardiomyocytes from apoptotic cell death.
PKD2 and PKD1 genes are mutated in autosomal dominant polycystic kidney disease. PKD2 can form either a homomeric cation channel or a heteromeric complex with the PKD1 receptor, presumed to respond to ligand(s) and/or mechanical stimuli. Here, we identify a two-residue hydrophobic gate in PKD2L1, and a single-residue hydrophobic gate in PKD2.
this is the first report of autosomal dominant polycystic kidney disease complicated with aortic dissection caused by PKD2 mutation
this study reports the 3.6-angstrom cryo-electron microscopy structure of truncated human PKD1-PKD2 complex assembled in a 1:3 ratio.
newly identified sites for known mutations will facilitate the early diagnosis and prediction of prognosis in patients with ADPKD
This noticeable hot spot regions hold higher frequency (50%) of pathogenic / likely pathogenic genetic variants constituting single nucleotide variants than large deletion and insertion that actually represents only 41.08% of coding sequence of PKD2. Statistically significant association for IVS3-22AA genotype was observed with PKD, while association of IVS4+62C>T was found insignificant.
the PKD1/PKD2 mutation status differed by ethnicity, and the PKD1/PKD2 genotype may affect the clinical phenotype of autosomal dominant polycystic kidney disease
The novel pathogenic variant in c.637C> T in PKD2 is very interesting since they may represent Italian clusters.
Upregulation of miR-106b-5p or downregulation of PKD2 expression can cause A549/DDP cells to become considerably more sensitive to cisplatin. The results showed that miR-106b-5p enhanced the sensitivity of A549/DDP cells to cisplatin by targeting the expression of PKD2.
investigated the interaction network of human PKD2 in the cytosol and in Golgi-enriched subcellular protein fractions
SNX3-retromer complex regulates the surface expression and function of PC1 and PC2
We aimed to revisit PKD2 prevalence, clinical presentation, mutation spectrum, and prognosis through the Genkyst cohort. Patients with PKD2-related dominant polycystic kidney disease typically present with mild disease
Hyperactivation of the ERK pathway may be caused by down-regulation of PC-1 and PC-2 in lymphatic malformations, contributing to increased proliferation of lymphatic endothelial cells.
Annualized median liver growth rates were 1.68, 1.5 and 1.24% for PKD1-T, PKD1-NT and PKD2 mutations, respectively (P = 0.49), and remained unaffected by the ADPKD genotype when adjusted for age, gender and baseline HtLV.
Here, we review previous studies that connect the molecular properties of the domains of PC2 Cterm to distinct aspects of PC2 functions and regulation.
TRPP2 mutations are associated with autosomal dominant polycystic kidney disease.
Data show that in 82 (87.2%) of the patients, pathogenic mutations were detected in PKD1 (79.0%-92.5%), whereas in 12 (12.8%) patients pathogenic mutations were detected in PKD2 (7.5%-21.0%).
Two cryo-EM structures of distinct channel states of full-length human PC2 in complex with lipids and cations.
Arterial myocyte PKD2 controls systemic blood pressure.
The lack of a PC2-dependent cardio-protective function may contribute to the severity of cardiac dysfunction in Pkd2(+/-) mice.
Pkhd1(Flox67HA) is a valid mouse model of autosomal recessive polycystic kidney disease to track Pkhd1-derived products containing the C-terminus. Significantly, exon 67 containing the nuclear localization signal and the polycystin-2 binding domain is not essential for Fibrocystin function in this model.
Knocking out TRPP2 by CRISPR/Cas9 genome editing eliminated the channel current, establishing it as TRPP2 dependent
olycystin 2 provides a critical function in the heart, independent of renal involvement
The TRPP2 functionally interacts with both ryanodine and InsP3 receptors. These interactions were not similar in adult and old mice.
Pkd2(-/-) mice with homozygous PKD2(tg)-transgene alleles (Pkd2(-/-);PKD2(tg/tg)) showed significant further amelioration of the cystic severity compared to that in Pkd2(-/-) mice
Pkd1 and Pkd2 have coordinate effects on osteoblast differentiation and opposite effects on adipogenesis, suggesting that Pkd1 and Pkd2 signaling pathways can have independent effects on mesenchymal lineage commitment in bone
novel protein complex composed of Rabep1, GGA1 and Arl3 is responsible for the sorting and targeting of the polycystin 1 andpolycystin 2 to the cilium.
PKD2 regulates directly and indirectly about 5% of the cytotoxic T-cell phosphoproteome.
The results of this study demonstrate that PC1 trafficking and expression require GPS cleavage and PC2 interaction, respectively, and provide a framework for functional assays to categorize the effects of missense mutations in polycystins.
In inner medullary collecting duct, flow, via polycystin-2 and P2 receptors, engages Ca(2+)-dependent signaling pathways that stimulate ET-1 synthesis.
Pkd2(+/-) cardiomyocytes shift the beta adrenergic receptor pathway and have altered calcium handling, independent of desensitized calcium-contraction coupling.
Epithelial-specific disruption of Pkd2 disrupts male reproductive tract development.
AGT inhibition resulted in significant decreases in kidney size and cyst volume and an improvement in kidney function in mice with targeted mutation in Pkd2.
PC2 regulates PC1 maturation; therefore, mature PC1 levels are a determinant of disease severity in PKD2 as well as PKD1.
Our data reveal for the first time differences between TRPP1 and TRPP2 deficiency
an epidermal growth factor activated TRPP2\TRPV4 channel may play an important role in increased cell proliferation and cystogenesis.
Expression of PC2 and PC1 in osteocyte-like cells is increased by oscillatory fluid flow
this uncovered a new pathway suggesting that when PC1 is expressed, PC2 that is not bound to PC1 is directed to aggresomes and subsequently degraded via autophagy, a control mechanism that may play a role in autosomal dominant polycystic kidney disease pathogenesis.
These data link RABS-5 and VPS-45 ciliary functions to the processing of periciliary-derived endocytic vesicles and regulation of ciliary membrane homeostasis. Our findings also provide insight into the regulation of PKD-2 ciliary levels via integrated endosomal sorting and CAV-1-mediated endocytosis.
MAPK-15 is a ciliary protein required for PKD-2 localization and male mating behavior in Caenorhabditis elegans
acts as a major calcium-release channel in the endoplasmic reticulum in cells where rapid calcium signaling is required, and is essential in those excitable cells for rapid responses to stimuli (polycystin-2)
expressed in male-specific neurons, required for mating
Both general and cell-type-specific factors govern TRPP2/PKD-2 subcellular distribution by forming at least two steps involving somatodendritic and ciliary sorting decisions.
These data reveal that the STAM-Hrs complex, which down-regulates ligand-activated growth factor receptors from the cell surface of yeast and mammalian cells, also regulates the localization and signaling of a ciliary PC1 receptor-TRPP2 complex.
Results demonstrate that somatodendritic and ciliary targeting of PKD-2 requires the transmembrane region of PKD-2 and that the PKD-2 cytosolic termini regulate subcellular distribution and function.
11 mutants found with defects in the ciliary localization (cil) of C. elegans PKD-2, a transient receptor potential polycystin (TRPP) channel
Results show that Far Upstream Element-Binding Protein 1 Binds the 3' Untranslated Region of PKD2 to inhibit PKD2 translation, regulating zebrafish disease phenotypes associated with PKD2 knockdown
TRPP2 and TRPV4 are mechanosensitive channels in the endocardium.Oscillatory flow modulates mechanosensitive klf2a expression through trpv4 and trpp2 during heart valve development.
Intraciliary calcium oscillations depend on Pkd2 and are left-biased at the left-right organizer in response to ciliary motility.
TRPP2 utilizes TRPV4 to form a mechano- and thermosensitive molecular sensor in the cilium.[TRPP2]
Isolated pkd2 mutant hearts displayed impaired intracellular calcium cycling and calcium alternans. These results indicate heart failure in the pkd2 mutants.
PKD2 suppression inactivates CaMK-II in pronephric cells and cilia, whereas constitutively active CaMK-II restores pronephric duct formation in pkd2 morphants
Proper heart valve formation in zebrafish critically depends on protein kinase D2-histone deacetylase 5-Kruppel-like factor signaling.
Pkd1a/b and pkd2 interact to regulate extracellular matrix secretion or assembly, and that altered matrix integrity may be a primary defect underlying autosomal dominant polycystic kidney disease tissue pathologies.
PRKCSH functions as a chaperone-like molecule, which prevents endoplasmic reticulum-associated degradation of TRPP2.
atp-2, lov-1, and pkd2 act in the same molecular pathway.
The functions of polaris and pkd2 in LR patterning are conserved between zebrafish and mice and that Kupffer's vesicle
In zebrafish pkd2 is not responsible for the activation of spaw transcription, but is required for a mechanism to restrict spaw expression to the left half of the embryo. pkd2 also appears to play a role in the propagation of Nodal signals in the LPM.
role in the development of normal left-to-right asymmetry depends on endoplasmic reticulum localization
Data indicate that the TRPP2 protein, a member of the transient receptor potential (TRP) channels protein superfamily, is encoded by the PKD2 gene, and TRPP2 mediates Ca(2+) release from intracellular Ca(2+) stores.
The flow-induced calcium signaling depends on the ciliary polycystin-2 calcium channel.
cloning and characterization of the PKD2 cDNA showing that the full-length gene (3370 bases) is highly expressed in kidney, with minimal expression in the liver
EGF may reduce the threshold of PKD2 activation by mechanical and other stimuli by releasing it from PIP(2)-mediated inhibition.
heteromeric cation channels comprised of the TRPP2 mutant and the TRPC3 or TRPC7 protein induce enhanced receptor-activated Ca(2+) influx that may lead to dysregulated cell growth in ADPKD
This gene encodes a member of the polycystin protein family. The encoded protein is a multi-pass membrane protein that functions as a calcium permeable cation channel, and is involved in calcium transport and calcium signaling in renal epithelial cells. This protein interacts with polycystin 1, and they may be partners in a common signaling cascade involved in tubular morphogenesis. Mutations in this gene are associated with autosomal dominant polycystic kidney disease type 2.
, autosomal dominant polycystic kidney disease type II protein
, transient receptor potential cation channel, subfamily P, member 2
, polycystic kidney disease 2 protein homolog
, polycystin 2
, polycystic kidney disease 2 homolog
, polycystic kidney disease 2 membrane protein
, cation channel
, polycystic kidney disease 2 (autosomal dominant) L homeolog
, Curly up
, Polycystic kidney disease 2 protein homolog
, Transient receptor potential cation channel subfamily P member 2
, curly up
, transient receptor potential cation channel subfamily P member 2
, polycystic kidney disease 2 (autosomal dominant)