Idioma:

Molecular Pharmacology of VEGF-A Isoforms: Binding and Signalling at VEGFR2

Peach, Chloe J ; Mignone, Viviane W ; Arruda, Maria Augusta ; Alcobia, Diana C ; Hill, Stephen J ; Kilpatrick, Laura E ; Woolard, Jeanette

International journal of molecular sciences, 2018-04, Vol.19 (4), p.1264 [Periódico revisado por pares]

Switzerland: MDPI AG

Texto completo disponível

Citações Citado por

Enviar para

Título:
Molecular Pharmacology of VEGF-A Isoforms: Binding and Signalling at VEGFR2
Autor: Peach, Chloe J ; Mignone, Viviane W ; Arruda, Maria Augusta ; Alcobia, Diana C ; Hill, Stephen J ; Kilpatrick, Laura E ; Woolard, Jeanette
Assuntos: Alternative splicing ; Angiogenesis ; Animals ; Binding ; Bioavailability ; blood vessel ; Cancer ; Cardiovascular disease ; Cell proliferation ; Cell survival ; Drug discovery ; Endothelial cells ; Endothelial Cells - metabolism ; Exons ; Extracellular matrix ; Genes ; Growth factors ; Humans ; Isoforms ; Kinases ; Macular degeneration ; Molecular modelling ; Neuropilin ; Permeability ; Pharmacology ; Physiology ; Protein Isoforms - metabolism ; Protein-tyrosine kinase receptors ; Proteins ; receptor tyrosine kinase inhibitors ; Review ; Signal Transduction - physiology ; Signaling ; Smooth muscle ; Splicing ; Tyrosine ; Vascular endothelial growth factor ; Vascular Endothelial Growth Factor A - metabolism ; Vascular Endothelial Growth Factor Receptor-2 - metabolism ; Vascular endothelial growth factor receptors
É parte de: International journal of molecular sciences, 2018-04, Vol.19 (4), p.1264
Descrição: Vascular endothelial growth factor-A (VEGF-A) is a key mediator of angiogenesis, signalling via the class IV tyrosine kinase receptor family of VEGF Receptors (VEGFRs). Although VEGF-A ligands bind to both VEGFR1 and VEGFR2, they primarily signal via VEGFR2 leading to endothelial cell proliferation, survival, migration and vascular permeability. Distinct VEGF-A isoforms result from alternative splicing of the gene at exon 8, resulting in VEGF a or VEGF b isoforms. Alternative splicing events at exons 5⁻7, in addition to recently identified posttranslational read-through events, produce VEGF-A isoforms that differ in their bioavailability and interaction with the co-receptor Neuropilin-1. This review explores the molecular pharmacology of VEGF-A isoforms at VEGFR2 in respect to ligand binding and downstream signalling. To understand how VEGF-A isoforms have distinct signalling despite similar affinities for VEGFR2, this review re-evaluates the typical classification of these isoforms relative to the prototypical, "pro-angiogenic" VEGF a. We also examine the molecular mechanisms underpinning the regulation of VEGF-A isoform signalling and the importance of interactions with other membrane and extracellular matrix proteins. As approved therapeutics targeting the VEGF-A/VEGFR signalling axis largely lack long-term efficacy, understanding these isoform-specific mechanisms could aid future drug discovery efforts targeting VEGF receptor pharmacology.
Editor: Switzerland: MDPI AG
Idioma: Inglês

Links

View this record in MEDLINE/PubMed

Voltar para lista de resultados

Anterior Resultado 2 Avançar Ir para próxima página

Realização: Logos de Redes Sociais:

Molecular Pharmacology of VEGF-A Isoforms: Binding and Signalling at VEGFR2

Peach, Chloe J ; Mignone, Viviane W ; Arruda, Maria Augusta ; Alcobia, Diana C ; Hill, Stephen J ; Kilpatrick, Laura E ; Woolard, Jeanette

Switzerland: MDPI AG

Buscando em bases de dados remotas. Favor aguardar.