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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.
Data show that in zebrafish, lrp5 also controls cell migration during early morphogenetic processes and contributes to shaping the craniofacial skeleton.
VAP1 cleaved the extracellular region of LRP5. This cle (show AOC3 Proteins)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 (show NDP Proteins) (3/31, 9.7%), FZD4 (show FZD4 Proteins) (2/31, 6.5%), TSPAN12 (show TSPAN12 Proteins) (1/31, 3.2%), and KIF11 (show KIF11 Proteins) (1/31, 3.2%). All the novel changes were predicted to be pathogenic by a series of bioinformatics analyses.
wild-type and all five mutant LRP5 proteins were assayed for the ability to activate the Norrin (show NDP Proteins)/beta-catenin (show CTNNB1 Proteins) pathway by established luciferase reporter assays, and all mutants failed to activate the pathway.
findings revealed an unrecognized role of Caprin-2 (show CAPRIN2 Proteins) in facilitating LRP5/6 constitutive phosphorylation at G2/M through forming a quaternary complex with CDK14 (show CDK14 Proteins), Cyclin Y (show CCNY Proteins), and LRP5/6.
This study did not identify LRP5 polymorphisms as a risk factor for osteoporosis in Thai menopausal women.
We identified four novel LRP5 missense mutations in these FEVR (show NDP Proteins) families: c.C1042T (p.R348W), c.G1141A (p.D381N), c.C1870T (p.R624W), and c.A4550G (p.Y1517C). All four of these LRP5 mutations led to significant reduction of enzymatic activity with response to NORRIN (show NDP Proteins). Our findings expand the mutational spectrum of FEVR (show NDP Proteins) in the Indian population and provide some guidelines in clinical diagnosis.
In this study, the splice site mutation c.2827thorn1G > A found in LRP5 (603506) gene is thought to cause microphthalmia in this family.
A genetic evaluation of the known genes associated with familial exudative vitreoretinopathy (FEVR (show NDP Proteins)) revealed a novel variant in the LRP5 gene that co-segregated with the phenotype in the family.
Meta-analysis indicates that the LRP5 Ala1330Val polymorphism may not be correlated with fracture susceptibility.
Independently or combined with APOE (show APOE Proteins), LRP5 polymorphisms may lead to dyslipidemia and are associated with generalized aggressive periodontitis. Dyslipidemia may be a risk indicator for generalized aggressive periodontitis in the Chinese population. Furthermore, two LRP5 polymorphisms (rs682429 and rs312016) might be useful for identifying subjects at higher risk of generalized aggressive periodontitis.
Lrp5(-/-) mice displayed significantly delayed retinal vascular development, absence of deep layer retinal vessels, leading to increased levels of vascular endothelial growth factor 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.
These results revealed a new role of the canonical Lrp5/6-beta-catenin (show CTNNB1 Proteins) pathway in regulating the morphogenesis of the cerebellum during postnatal development.
LRP5 function in mice causes retinal hypovascularization during development as well as retinal neovascularization in adulthood with disorganized and leaky vessels.
Lrp5 is required for glucose uptake, and glucose uptake regulates the growth rate of mammary epithelial cells in culture.
Data show that LDL receptor (show LDLR Proteins)-related protein 5 (show CAPS Proteins) (LRP5) gain-of-function mutations do not activate beta-catenin (show CTNNB1 Proteins) signaling in osteoblasts.
These in vivo data support in vitro studies regarding the mechanism of HBM-causing mutations, and imply that HBM LRP5 receptors differ in their relative sensitivity to inhibition by SOST (show SOST Proteins) and DKK1 (show DKK1 Proteins).
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