EGF-like repeats and discoidin I-like domains 3 (EDIL3) (EDIL3)

EGF-like repeats and discoidin I-like domains 3 (EDIL3), also known as DEL-1, is a secreted extracellular matrix glycoprotein that plays a pivotal role in vascular development and the regulation of the innate immune response [1]. It consists of three EGF-like repeats and two discoidin-like domains, which facilitate its binding to various integrins, most notably αvβ3 and αvβ5, to promote endothelial cell adhesion and migration during angiogenesis [2][3]. Beyond its role in blood vessel formation, EDIL3 serves as a critical anti-inflammatory factor by competitively inhibiting the interaction between the leukocyte integrin LFA-1 and the endothelial adhesion molecule ICAM-1, thereby limiting excessive leukocyte infiltration into tissues [4]. In oncology, EDIL3 is frequently upregulated in various solid tumors, where it contributes to tumor-associated angiogenesis and immune evasion, making it an attractive target for therapeutic intervention [5]. While no drugs targeting EDIL3 are currently FDA-approved, experimental strategies including monoclonal antibodies and recombinant proteins are being explored to modulate its activity in cancer and chronic inflammatory conditions [1][6]. Sources: [1] UniProt (O43854) [2] PubMed (PMID: 9529252) [3] NCBI Gene (ID: 10085) [4] PubMed (PMID: 18787104) [5] PubMed (PMID: 28651543) [6] PubMed (PMID: 31110263)

Other names

Developmentally regulated endothelial cell locus 1 proteinDEL-1DEL1

EDIL3 acts as an antagonist to leukocyte adhesion by interfering with the LFA-1/ICAM-1 interaction and promotes endothelial cell migration and adhesion through binding to integrins such as αvβ3 and αvβ5 [1][2].