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
High plasma VEGF-B levels are associated with type 2 diabetes mellitus.
Data from clinical studies point out the changes in circulating or tissue expression levels of VEGF-B in obese compared with lean patients.
Cardiac transgenic vascular endothelial growth factor-B overexpression failed to protect heart transplants from ischemia-reperfusion injury.
renal VEGF-B expression correlates with the severity of Diabetic Kidney Disease.
Data show that metformin treatment reduces serum vascular endothelial growth factor B (VEGF-B) levels and ameliorates insulin (show INS Proteins) resistance.
VEGFA (show VEGFA Proteins) and VEGFB associated sub-network, kinase insert domain receptor (KDR (show KDR Proteins)), fibronectin 1 (FN1 (show FN1 Proteins)), transforming growth factor beta induced (TGFBI) and proliferating cell nuclear antigen (PCNA (show PCNA Proteins)) found to interact with at least two of the three hub genes.
Frameshift mutations of VEGFB gene is associated with stomach and colorectal cancers.
plasma VEGF (show VEGFA Proteins) levels before treatment were lower in patients with schizophrenia and that their VEGF (show VEGFA Proteins) levels increased after treatment.
fluid shear stress induces the synthesis of Insulin growth factor-2 and vascular endothelial growth factor (VEGF (show VEGF Proteins)) B and D, which in turn transactivate MMP-12 (show MMP12 Proteins).
MMP9 (show MMP9 Proteins) may activate VEGF-B via PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins) signaling pathway.
Data suggest that dietary fatty acids create epigenetic/nutrigenomic changes in methylation levels of CpG island at Vegfb promoter and changes in Vegfb expression in white adipocytes in vivo and in vitro, with particular up-regulation of DNA methylation (show HELLS Proteins) by linoleic acid; Vegfb promoter methylation levels are closely related to Vegfb gene expression in visceral and subcutaneous adipose tissue.
PGC-1alpha is a master metabolic sensor that regulates the expression of Vegfa (show VEGFA Proteins) and Vegfb, coordinates blood vessels growth and fatty acid uptake with mitochondrial fatty acid oxidation.
These data therefore support a tightly controlled, paracrine signaling mechanism of VEGF-B to VEGFR1 (show FLT1 Proteins).
VEGFB-Induced Vascular Remodeling in Adipose Tissue Requires VEGF (show VEGFA Proteins)/VEGFR2 (show KDR Proteins). VEGFB-Induced Vascular Remodeling Improves Insulin (show INS Proteins) Supply, Signaling, and Function in Obese Mice.
VEGF-B is dispensable for normal cardiac function under unstressed conditions and for high fat diet-induced metabolic changes.
VEGF-B is a vascular remodeling factor promoting cancer metastasis.
Data indicate that vascular endothelial growth factor B knockout (Vegf-b-/-) mice showed impaired nerve repair with concomitant impaired trophic function.
Data indicate that VEGF-B is a high-affinity VEGFR-1 (show FLT1 Proteins) ligand that, unlike PlGF (show PGF Proteins), cannot efficiently induce signaling downstream of VEGFR-1 (show FLT1 Proteins).
results demonstrate that the vascular endothelium can function as an efficient barrier to excess muscle lipid uptake even under conditions of severe obesity and type 2 diabetes, and that this barrier can be maintained by inhibition of VEGF-B signalling
PCR-SSCP and DNA sequencing methods were applied to reveal 3 SNPs and a duplication in the bovine VEGF-B gene among 675 samples belonging to three native Chinese cattle breeds.
This gene encodes a member of the PDGF (platelet-derived growth factor)/VEGF (vascular endothelial growth factor) family. The VEGF family members regulate the formation of blood vessels and are involved in endothelial cell physiology. This member is a ligand for VEGFR-1 (vascular endothelial growth factor receptor 1) and NRP-1 (neuropilin-1). Studies in mice showed that this gene was co-expressed with nuclear-encoded mitochondrial genes and the encoded protein specifically controlled endothelial uptake of fatty acids. Alternatively spliced transcript variants encoding distinct isoforms have been identified.