Kinase insert domain receptor (KDR) and Adrenoceptor beta 2 (ADRB2) (KDR, ADRB2)

The entry 'KDR, ADRB2 and other predicted hub targets' refers to a set of proteins identified as central nodes (hubs) within biological networks, often in the context of network pharmacology studies investigating multi-target drug effects (PMID: 32355477). The Kinase insert domain receptor (KDR), also known as Vascular endothelial growth factor receptor 2 (VEGFR2), is a receptor tyrosine kinase that serves as the primary mediator of angiogenesis, vascular permeability, and endothelial cell proliferation (UniProt P35968). It is a major therapeutic target in oncology, where its inhibition limits tumor blood supply, and in ophthalmology for treating neovascular diseases. The Adrenoceptor beta 2 (ADRB2) is a G protein-coupled receptor that mediates smooth muscle relaxation, particularly in the bronchi, and is the primary target for bronchodilators used in asthma and chronic obstructive pulmonary disease (UniProt P07550). These proteins are frequently identified as hub targets because they are highly connected in protein-protein interaction networks, suggesting that their simultaneous modulation may provide synergistic benefits in treating complex inflammatory or proliferative diseases (PMID: 31431849). Because this entry groups multiple distinct proteins with different structures and functions, it represents a polypharmacological profile rather than a single molecular target.

Other names

VEGFR2Vascular endothelial growth factor receptor 2Kinase insert domain receptorBeta-2 adrenergic receptorADRB2RB2ARCD309FLK1

KDR: Inhibition of the tyrosine kinase activity of the receptor, preventing downstream signaling pathways such as MAPK and PI3K/Akt that drive angiogenesis (PMID: 25133335). ADRB2: Agonism of the receptor leads to activation of adenylate cyclase, increasing intracellular cAMP and resulting in smooth muscle relaxation (StatPearls: Beta 2 Agonists).