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The extracellular domains of Lrp5/6 behave as physiologically relevant inhibitors of noncanonical Wnt (Montrer WNT2 Protéines) signaling during Xenopus and mouse development in vivo.
Rescue experiments showed that LRP5 mutation is associated with hearing loss. (Montrer WNT2 Protéines)Knocking down lrp5 in zebrafish results in reduced expression of several genes linked to Wnt signaling pathway and decreased cell proliferation when compared with those in wild-type zebrafish
Data show that in zebrafish, lrp5 also controls cell migration during early morphogenetic processes and contributes to shaping the craniofacial skeleton.
In conclusion, the LRP5 mutation influences cell proliferation through the Wnt (Montrer WNT2 Protéines) signaling pathway, thereby reducing the number of supporting cells and hair cells and leading to nonsyndromic hearing loss in this Chinese family.
LRP5 might be an important genetic marker contributing to bone mass accrual early in life.
We identified two novel heterozygous deletion mutations [LRP5, c.4053 DelC (p.Ile1351IlefsX88); TSPAN12 (Montrer TSPAN12 Protéines), EX8Del] using targeted NGS as a causative mutation for Familial exudative vitreoretinopathy (FEVR (Montrer NDP Protéines)).
A novel heterozygous mutation (p.N198Y) in LRP5 was identified in a patient with significantly increased bone mineral density.
The presence of GIIA in the LRP5 complex pinpoints a potential functional connection with PRKCSH (Montrer PRKCSH Protéines). Interestingly, all three PLD-associated protein complexes included filamin A (FLNA (Montrer FLNA Protéines)), a multifunctional protein described to play a role in ciliogenesis as well as canonical Wnt (Montrer WNT2 Protéines) signalling.
LRP5 (rs556442) had a significant influence on trigylceride (TG) levels in unadjusted analysis and when adjusted for interacting factors. Higher TG levels were observed in AA/AG genotype of rs566442 in comparison to GG genotype (OR = 2.028, 95% CI = 0.997-4.127, p = 0.049).
The detection rate for mutations in the three known genes was 23%. Mutations in LRP5 and TSPAN12 (Montrer TSPAN12 Protéines) were more frequent, accounting for 10% and 8%
To our knowledge, these are the first two cases of the syndrome described in Italy. Genetic testing proved to be fundamental for definition of the syndrome and confirms the importance of early detection of LRP5 variants for management of systemic features of the disease in patients and carrier relatives.
VAP1 cleaved the extracellular region of LRP5. This cle (Montrer AOC3 Protéines)avage removes four inhibitory beta-propeller structures, resulting in activation of LRP5/6.
Among the detected mutations, LRP5 accounted for the largest proportion with a mean mutation rate of 16.1% (5/31, 16.1%), followed by NDP (Montrer NDP Protéines) (3/31, 9.7%), FZD4 (Montrer FZD4 Protéines) (2/31, 6.5%), TSPAN12 (Montrer TSPAN12 Protéines) (1/31, 3.2%), and KIF11 (Montrer KIF11 Protéines) (1/31, 3.2%). All the novel changes were predicted to be pathogenic by a series of bioinformatics analyses.
Megakaryocytes are increased in the bone marrow of Lrp5G170V/G170V mice. Depletion of megakaryocytes does not affect the Lrp5-induced high bone mass.
The phenotype of the Lrp5(tvrm111B) mutant includes abnormalities of the retinal vasculature and of bone mineral density.
the LRP5 mutation in high bone mass transgenic mice shows altered bone matrix composition
Lrp6 (Montrer LRP6 Protéines) is the key mediator of Wnt3a (Montrer WNT3A Protéines) signaling in osteoblasts and Lrp5 played a less significant role in mediating Wnt3a (Montrer WNT3A Protéines) signaling.
Identification of a link between Wnt (Montrer WNT2 Protéines)-Lrp5 signaling and insulin (Montrer INS Protéines) signaling in the osteoblast that has the potential to influence energy balance and compound the detrimental effects of a HFD on whole-body metabolism.
Lrp5(-/-) mice displayed significantly delayed retinal vascular development, absence of deep layer retinal vessels, leading to increased levels of vascular endothelial growth factor (Montrer VEGF Protéines) and subsequent pathologic glomeruloid vessels, as well as decreased inner retinal visual function.
A mouse LRP5 ectodomain recombinant was cleaved by VAP1 (Montrer AOC3 Protéines), creating a peptide, VAHLTGIHAVEE, detected by mass spectrometric analysis of the 140-kDa fragment, suggesting that the sessile bond by VAP1 (Montrer AOC3 Protéines) is Glu1206-Val1207.
we revealed miR (Montrer MLXIP Protéines)-375-3p negatively regulated osteogenesis by targeting LRP5 and beta-catenin (Montrer CTNNB1 Protéines)
lung myeloid cells are responsive to Lrp5/beta-catenin (Montrer CTNNB1 Protéines) signaling, leading to differentiation of an alveolar macrophage subtype that antagonizes the resolution of lung fibrosis.
LRP5 is a novel anti-inflammatory macrophage marker that positively regulates migration, phagocytosis, lipid uptake and metabolism.
This gene encodes a transmembrane low-density lipoprotein receptor that binds and internalizes ligands in the process of receptor-mediated endocytosis. This protein also acts as a co-receptor with Frizzled protein family members for transducing signals by Wnt proteins and was originally cloned on the basis of its association with type 1 diabetes mellitus in humans. This protein plays a key role in skeletal homeostasis and many bone density related diseases are caused by mutations in this gene. Mutations in this gene also cause familial exudative vitreoretinopathy.
Lipoprotein Receptor Related Protein 5
, low density lipoprotein receptor-related protein 5
, low-density lipoprotein receptor-related protein 5
, low-density lipoprotein receptor-related protein 5-like
, low density lipoprotein receptor-related protein 7
, low-density lipoprotein receptor-related protein 7