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Lrp6 asymmetry is controlled by Wnt/PCP signaling, indicating that this pathway regulates not only planar- but also apicobasal cell polarity.
PTK7 and LRP6 proteins physically interact, suggesting that PTK7 stabilization of LRP6 protein reciprocally regulates both canonical and noncanonical Wnt activities in the embryo.
Results suggest that Rap2 acts via TNIK to regulate the stability of LRP6 receptor for Wnt signaling.
The extracellular domains of Lrp5/6 behave as physiologically relevant inhibitors of noncanonical Wnt signaling during Xenopus and mouse development in vivo.
Lrp6 plays a critical role in the switch from Wnt/PCP to Wnt/beta-catenin signaling.
Kremen2 knockdown specifically reduces LRP6 protein levels in neural crest explants.
Waif1a binds to the Wnt coreceptor LRP6 and inhibits Wnt-induced LRP6 internalization into endocytic vesicles, a process that is required for pathway activation.
Results identify GRK5/6 as novel kinases for the single transmembrane receptor LRP6 during Wnt signaling.
we focus on the role of LRP6 genetic polymorphisms and Wnt signaling in complex diseases, and the mechanisms from mouse models and cell lines. It is also highly anticipated that LRP6 variants will be applied clinically in the future
knockdown of LRP6 inhibited the cell viability by activation of Drp1 in glucose deprived-cardiomyocytes.
Three rare missense mutations (c.1514A>G, p.Y505C); c.2984A>G, p.D995G; and c.4280C>A, p.P1427Q) of the LRP6 gene were identified in Chinese NTD patients. The Y505C mutation is a loss-of-function mutation on both WNT/beta-catenin and PCP signaling. The D995G mutation partially lost inhibition on PCP signaling without affecting WNT/beta-catenin signaling. The P1427Q mutation dramatically increased WNT/beta-catenin signa...
LRP6 endocytosis proceeds by two routes, depending on the presence of LDL, and that LRP6 controls the intracellular destination of NPC1L1 in hepatocytes.
High Expressions of LRP6 is associated with cancer.
LRP6 expression was found to be upregulated in oral squamous cell carcinoma tissues, and correlated with a cluster of clinicopathologic parameters, including smoking, drinking, tumor differentiation status, lymph node metastasis and survival time.
CCN2 plays a promoting role in hepatocellular carcinoma (HCC)progression through activating LRP6 in a HSPGs-dependent manner. Heparin in combination with chemotherapy has a synergic effect and could be a treatment choice for HCCs with a high CCN2 expression.
Increased LRP6 gene expression is associated with colorectal cancer.
Therefore, our study demonstrates that miR-183 is a tumor suppressor microRNA that plays a major role in OS.
data suggest that LRP6 promotes negative breast cancer cell migration and invasion by regulating the expression and function of S100A4 via the Wnt/beta-catenin signaling pathway
sustained activation of Wnt/beta-catenin signaling due to abrogation of Merlin-mediated inhibition of LRP6 phosphorylation may be a cause of Neurofibromatosis type II disease.
LRP6 ectodomain becomes highly compact upon complexation with the Wnt antagonist Dkk1, suggesting a potential role for the ectodomain conformational change in the regulation of receptor oligomerization and signaling.
identify ANGPTL4 as a Wnt signaling antagonist that binds to syndecans and forms a ternary complex with the Wnt co-receptor Lipoprotein receptor-related protein 6
The authors show that folding of the Wnt signaling coreceptor LRP6 is promoted by ubiquitination of a specific lysine, retaining it in the ER while avoiding degradation.
Taken together, this study reveals evidence demonstrating a mechanism by which the LPR6/ GSK3beta/E2F1 axis-upregulated LSH promoted gliomas.
Structure of the dual-mode Wnt regulator Kremen1 and insight into ternary complex formation with LRP6 and DKK1 have been presented.
VAP1 cleaved the extracellular region of LRP6 at Glu1196-Leu1197, the C-terminus of the 4th propeller domain. This cleavage removes four inhibitory beta-propeller structures, resulting in activation of LRP5/6.
We identified a frameshift (c.4594delG, p.Cys1532fs) and a canonical splice-site mutation (c.3398-2A>C, p.?) in LRP6, respectively, in the patient with tooth agenesis (TA) and orofacial clefting (OFC) and in the patient with severe TA only. Mutations in LRP6 cause TA in humans
findings revealed an unrecognized role of Caprin-2 in facilitating LRP5/6 constitutive phosphorylation at G2/M through forming a quaternary complex with CDK14, Cyclin Y, and LRP5/6.
results suggest that miR-29b inhibits expression of LRP6 and HuR post-transcriptionally, thus playing a role in the regulation of IEC proliferation and intestinal epithelial homoeostasis.
Anti-LRP5/LRP6 single-domain antibody fragments promote differentiation of Wnt3a-hypersensitive intestinal stem cells.
Cardiac LRP6 deficiency greatly suppressed autophagic degradation and fatty acid utilization, and subsequently leads to lethal dilated cardiomyopathy and cardiac dysfunction through activation of Drp1 signaling.
Low LRP6 expression is associated with chronic social defeat stress.
In this study, we found that the wnt co-receptor Lrp6 was a potent positive regulator of beta-catenin signaling in TDI-induced asthma models, both in vivo and in vitro. Additionally, for the first time, we demonstrated that RAGE could mediate phosphorylation of Lrp6, suggesting a functional cross talk between RAGE and the canonical wnt/beta-catenin signaling pathway involved in mediating beta-catenin activation.
LRP6 acts as a scaffold protein in cardiac gap junction assembly and intracellular protein trafficking.
Data show that reduction of alpha chain of nascent polypeptide associated complex (alphaNAC) levels decreased basal expression of Low density lipoprotein receptor-Related Protein 6 (Lrp6) by 30%.
GPR37 is required for Wnt/beta-catenin signaling and protects LRP6 from ER-associated degradation via CHIP (carboxyl terminus of Hsc70-interacting protein) and the ATPase VCP
Lrp6 is the key mediator of Wnt3a signaling in osteoblasts and Lrp5 played a less significant role in mediating Wnt3a signaling.
VAP1 cleaved recombinant mouse LRP6, producing a 140-kDa fragment. An antibody against a peptide including the LRP6-cleavage site inhibited VAP1-induced VE-cadherin relocation and disruption of cell-cell adhesions and blocked haemorrhage in mice in vivo.
we identified Lrp6, the gene encoding the coreceptor to Frizzled in the Wnt pathway, as a potential negative regulator of precursor proliferation. Overexpression and siRNA silencing confirmed the regulatory role of Lrp6
These results revealed a new role of the canonical Lrp5/6-beta-catenin pathway in regulating the morphogenesis of the cerebellum during postnatal development.
Data (including data from studies in knockout/transgenic mice) suggest Lrp6 is required for suppression of Sost (sclerostin) expression by parathyroid hormone (here, human PTH peptide 1-34); LRP6 regulates osteocytes expression of histone deacetylases.
Lrp5 binds to Frizzled, preventing Frz-regulated non-canonical Wnt pathway activation and further non-canonical pathway-mediated tumour metastasis.
Wt1 expression levels in podocytes regulate Wnt/beta-catenin signaling through modulating the endocytic fate of LRP6, and this indicates a potential target for the therapy of CKD.
N-cadherin modulates Lrp6/PTHR1 interaction, restraining the intensity of parathyroid hormone-induced beta-catenin signaling
LRP6 restrains vascular smooth muscle lineage noncanonical signals that promote osteochondrogenic differentiation, mediated in part via USF1- and arginine methylation-dependent relays.
Urotensin II inhibited the proliferation of cardiac side population cells by JNK/LRP6 signalling during pressure overload.
Hgf as an important transactivator of canonical Wnt signaling that is mediated by Met-stimulated, Gsk3-dependent Lrp5/6 phosphorylation
miR-183, though negatively regulated by Gata3, enhances 3T3-L1 preadipocyte differentiation and adipogenesis by targeting LRP6.
Phosphorylation of LRP6 was increased after tissue plasminogen activator (tPA) treatment and decreased by tPA siRNA transfection.
This gene encodes a member of the low density lipoprotein (LDL) receptor gene family. LDL receptors are transmembrane cell surface proteins involved in receptor-mediated endocytosis of lipoprotein and protein ligands. The protein encoded by this gene functions as a receptor or, with Frizzled, a co-receptor for Wnt and thereby transmits the canonical Wnt/beta-catenin signaling cascade. Through its interaction with the Wnt/beta-catenin signaling cascade this gene plays a role in the regulation of cell differentiation, proliferation, and migration and the development of many cancer types. This protein undergoes gamma-secretase dependent RIP- (regulated intramembrane proteolysis) processing but the precise locations of the cleavage sites have not been determined.
low density lipoprotein receptor-related protein 6
, lipoprotein receptor-related protein 6
, low-density lipoprotein receptor-related protein 6
, low-density lipoprotein receptor-related protein 6-like
, low density lipoprotein receptor-related protein 6; low density lipoprotein-related protein 6
, low density lipoprotein-related protein 6