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Human VEGFB Protein expressed in HEK-293 Cells - ABIN2181909
Olofsson, Pajusola, Kaipainen, von Euler, Joukov, Saksela, Orpana, Pettersson, Alitalo, Eriksson: Vascular endothelial growth factor B, a novel growth factor for endothelial cells. in Proceedings of the National Academy of Sciences of the United States of America 1996
Show all 2 references for ABIN2181909
Human VEGFB Protein expressed in Escherichia coli (E. coli) - ABIN666735
Claesson-Welsh: VEGF-B taken to our hearts: specific effect of VEGF-B in myocardial ischemia. in Arteriosclerosis, thrombosis, and vascular biology 2008
Show all 2 references for ABIN666735
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 (show TGFBI Proteins)) 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 levels before treatment were lower in patients with schizophrenia and that their VEGF levels increased after treatment.
fluid shear stress induces the synthesis of Insulin growth factor-2 and vascular endothelial growth factor (VEGF) B and D, which in turn transactivate MMP-12.
MMP9 (show MMP9 Proteins) may activate VEGF-B via PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins) signaling pathway.
Roles of vascular endothelial growth factor in amyotrophic lateral sclerosis.
Low VEGFB and VEGFD (show Figf Proteins) gene expression is associated with early-stage non-small cell lung cancer.
Our study suggested that VEGF-B was an angiogenesis factor in vitro and that ERK1/2 and p38 (show CRK Proteins)-related signaling pathways were involved in these VEGF-B activities.
VEGF-B has possible roles in cardiac protection, energy metabolism support, and neuroprotectin [review]
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
the RTEF-1 (show TEAD4 Proteins)-driven increase of VEGF-B plays an important role in communication between the endothelium and myocardium
Study indicates that VEGF-B, instead of acting as an angiogenic factor (show VEGFA Proteins), exerts direct neuroprotective effects through FLT1 (show FLT1 Proteins).
Data show that no differences in vascular density, perfusion or immune cell infiltration upon altered Vegfb gene dosage were noted.
VEGF-B appears to be a coronary growth factor in rats but not in mice.
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.