BMP Binding Endothelial Regulator (BMPER) ELISA Kits

Fruit Fly (Drosophila melanogaster) BMP Binding Endothelial Regulator (BMPER) interaction partners

1. The bone morphogenetic protein- binding protein Cv-2 negatively regulates bone morphogenetic protein signaling.

2. Cv-2 is a short-range, concentration-dependent, biphasic modulator of BMP signaling.

Zebrafish BMP Binding Endothelial Regulator (BMPER) interaction partners

1. Data show that in endothelial cells, bone morphogenetic protein endothelial precursor-derived regulator (BMPER) and twisted gastrulation protein homolog 1 (TWSG1) are necessary for regular Notch signaling activity.

2. The NMR structure of the Danio rerio CV2 VWC1 domain in its unbound state shows the key features for high affinity binding to BMP-2 are a pre-oriented peptide loop.

3. Crossveinless 2 functions in a positive-feedback loop to locally enhance BMP activity and is required for neural crest fate determination.

4. LRP1 acts as an endocytic receptor for Bmper and a coreceptor of Bmp4 to mediate the endocytosis of the Bmper/Bmp4 signaling complex.

5. Binding of CV2 to Chordin promotes BMP-2 signaling.

6. Cvl2 was identified as an essential pro-bone morphogenetic protein factor during zebrafish embryogenesis.

7. Bmper is a conserved regulator of hematopoietic and vascular development in zebrafish.

8. Initial crystallographic analysis suggests that a complete binary complex consisting of one BMP2 dimer bound to two crossveinless 2 (CV2) von Willebrand type C (VWC1) domains is present in the asymmetric unit.

9. The structure of the complex between CV-2 Von Willebrand factor type C (VWC) domain 1 and BMP-2, is reported.

Xenopus laevis BMP Binding Endothelial Regulator (BMPER) interaction partners

1. CV2/Chordin interaction may help coordinate bone morphogenetic protein (BMP) diffusion to the ventral side of the embryo, ensuring that BMPs liberated from Chordin inhibition by tolloid proteolysis cause peak signaling levels.

Human BMP Binding Endothelial Regulator (BMPER) interaction partners

1. Internal cleavage and synergy with TWSG1 enhance BMP-4 inhibition by BMPER.

2. BMPER possesses valuable discriminative capacity for urosepsis and is a strong predictor of adverse outcome in patients with urosepsis.

3. A novel homozygous mutation in BMPER (c.410T>A; p.Val137Asp) was found in three fetuses with diaphanospondylodysostosis.

4. Overexpression of BMPER remarkably enhanced BMP-2-induced osteogenic differentiation, while suppression of BMPER effectively inhibited this process both in vitro and in vivo.

5. that BMPER-modulated BMP pathway activity regulates VE-cadherin expression and vascular barrier function

6. BMPER variants associated with a novel, attenuated subtype of diaphanospondylodysostosis.

7. BMPER-dependent pathway involved in high glucose induced alkaline phosphatase expression in vascular smooth muscle cells.

8. The proangiogenic BMPER effect in endothelial cells is mediated by inhibition of antiangiogenic thrombospondin-1 and enhanced expression and activation of the FGF signaling pathway that is crucial in the promotion of angiogenesis.

9. these results suggest that BMPER and Tsg maintain a fine-tuned equilibrium that controls BMP pathway activity and is necessary for vascular cell homeostasis.

10. BMPER is a novel regulator of the osteoblast-like differentiation of HCASMCs.

11. Bmper is a critical regulator of Bmp-mediated vascular inflammation and that the fine-tuning of Bmp and Bmper levels is essential in the maintenance of normal vascular homeostasis.

12. The data unequivocally demonstrated that BMPER is highly expressed in malignant tumors and that the growth of lung, colon, and uterine carcinomas is dependent on the presence of BMPER.

13. Mutual regulation by BMP-9 and CV2 is essential in regulating the development of the vascular endothelium.

14. Diaphonospondylodysostosis is caused by loss of BMPER function.

15. BMPER-mediated signaling plays an essential role in vertebral segmentation early in human development, while defects in BMPER produce Diaphanospondylodysostosis.

16. BMPER is a novel BMP-binding protein that is expressed by endothelial cell precursors, has BMP-antagonizing activity, and may play a role in endothelial cell differentiation by modulating local BMP activity

17. Crossveinless-2 is an inhibitor of BMP function

18. BMPER is an endothelial cell regulator and controls bone morphogenetic protein-4-dependent angiogenesis.

Cow (Bovine) BMP Binding Endothelial Regulator (BMPER) interaction partners

1. Results identified variant SNPs in BMPER gene associated with phenotypic variation in cattle that can be used as genetic markers for breeding.

Pig (Porcine) BMP Binding Endothelial Regulator (BMPER) interaction partners

1. Study in a Large White pig population show that the positive effect on growth is induced by a heterozygous loss-of-function of the BBS9 gene, associated with obesity in human and mouse. However, late fetal mortality is induced by insufficient expression of the BMPER gene located directly downstream of the deletion which affects its regulatory elements required for gene expression.

2. BMPER promoter polymorphisms have an effect on the intramuscular fat deposition in longissimus dorsi muscle content.

Mouse (Murine) BMP Binding Endothelial Regulator (BMPER) interaction partners

1. BMPER contributes to the precise control of BMP activity within the aorta-gonad-mesonephros region, enabling the maturation of hematopoietic stem cells within a BMP-negative environment.

2. CV2 binds directly to BMP10, as determined by co-immunoprecipitation, and inhibits BMP10 from initiating SMAD signaling, as determined by luciferase reporter gene assays. BMP10 and CV2 have important roles in coordinating cardiomyogenesis in progenitor cells.

3. BMPER/low-density lipoprotein receptor-related protein 1 axis plays a pivotal role in pulmonary inflammatory response.

4. The proangiogenic BMPER effect in endothelial cells is mediated by inhibition of antiangiogenic thrombospondin-1 and enhanced expression and activation of the FGF signaling pathway that is crucial in the promotion of angiogenesis.

5. BMPER-induced BMP signaling promotes coronary artery remodeling.

6. BMPER appears to play a role in regulating both vessel density and cardiac development

7. BMPER expression is decreased following lung injury, which in turn impairs epithelial integrity, characterized by reduction of E-cadherin and epithelial leakage in vitro and in vivo.

8. Bmper is a critical regulator of Bmp-mediated vascular inflammation and that the fine-tuning of Bmp and Bmper levels is essential in the maintenance of normal vascular homeostasis.

9. The data unequivocally demonstrated that BMPER is highly expressed in malignant tumors and that the growth of lung, colon, and uterine carcinomas is dependent on the presence of BMPER.

10. Bmper may play an important role in suppressing hepcidin production in hypotransferrinemic mice.

11. BMP modulator BMPER is a new protective regulator of vascular inflammation that modulates leukocyte adhesion and migration in vitro and in vivo.

12. BMPER is important in the regulation of BMP signaling and revascularization in the hypoxic retina.

13. The data indicate a role for CV2 and Chd in the establishment of the vertebral morphogenetic field through the long-range relocalization of Chd/BMP complexes.

14. Cv2 enhances pro-BMP activity of Tsg.

15. Cv2 is a conserved, positive regulator of bone morphogenetic protein signaling. Its cysteine-rich domains acts as both positive and negative modulators of BMP signaling.

16. crossveinless 2 has essential pro-Bmp functions for locally restricted signal enhancement in multiple aspects of mammalian organogenesis.

17. The context-dependent functional relationship between Tsg and Cv2 during mouse development, is presented.

18. Cv2 may specify cardiac mesodermal lineage through inhibition of BMP signaling at early stage of cardiogenesis.

19. Development of the vertebral morphogenetic field is reported in the interactions of CV-2 and Twg.

20. Study demonstrates that as molar concentrations of Bmper exceed Bmp4, Bmper dynamically switches from an activator to an inhibitor of Bmp4 signaling.