Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
The extracellular domains of Lrp5/6 behave as physiologically relevant inhibitors of noncanonical Wnt (show WNT2 Proteins) signaling during Xenopus and mouse development in vivo.
Rescue experiments showed that LRP5 mutation is associated with hearing loss. (show WNT2 Proteins)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.
These findings expand the mutation spectrums of ABCA4 (show ABCA4 Proteins) and LRP5, and will be valuable for genetic counseling and development of therapeutic interventions for patients with Familial exudative vitreoretinopathy.
Data suggest that the risk of type 2 diabetes mellitus (T2DM) may be associated with interactions between the low-density lipoprotein receptor-related protein 5 (LRP5) gene and overweight and obesity.
The data do not support the hypothesis that HBM-causing LRP5 mutations, associated with increased Wnt (show WNT2 Proteins) signaling, improve glucose metabolism in humans. However, it does appear that LRP5 variants may affect LDL metabolism, a major risk factor for coronary artery disease.
In conclusion, the LRP5 mutation influences cell proliferation through the Wnt (show WNT2 Proteins) 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 (show TSPAN12 Proteins), EX8Del] using targeted NGS as a causative mutation for Familial exudative vitreoretinopathy (FEVR (show NDP Proteins)).
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 (show PRKCSH Proteins). Interestingly, all three PLD-associated protein complexes included filamin A (FLNA (show FLNA Proteins)), a multifunctional protein described to play a role in ciliogenesis as well as canonical Wnt (show WNT2 Proteins) 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 (show TSPAN12 Proteins) were more frequent, accounting for 10% and 8%
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 (show LRP6 Proteins) is the key mediator of Wnt3a (show WNT3A Proteins) signaling in osteoblasts and Lrp5 played a less significant role in mediating Wnt3a (show WNT3A Proteins) signaling.
Identification of a link between Wnt (show WNT2 Proteins)-Lrp5 signaling and insulin (show INS Proteins) 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 (show VEGF Proteins) and subsequent pathologic glomeruloid vessels, as well as decreased inner retinal visual function.
A mouse LRP5 ectodomain recombinant was cleaved by VAP1 (show AOC3 Proteins), creating a peptide, VAHLTGIHAVEE, detected by mass spectrometric analysis of the 140-kDa fragment, suggesting that the sessile bond by VAP1 (show AOC3 Proteins) is Glu1206-Val1207.
we revealed miR (show MLXIP Proteins)-375-3p negatively regulated osteogenesis by targeting LRP5 and beta-catenin (show CTNNB1 Proteins)
lung myeloid cells are responsive to Lrp5/beta-catenin (show CTNNB1 Proteins) 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