Journal: Cancers
Article Title: The Multifaceted Roles of EGFL7 in Cancer and Drug Resistance
doi: 10.3390/cancers13051014
Figure Lengend Snippet: ( a ) Model structure of the EGFL7 protein. EGFL7 contains two EGF-like repeats: an arg-gly-asp integrin-binding motif (RGD) and an Emilin-like region. ( b ) The regulatory network of EGLF7. EGFL7 binds via its RGD domain to ITGAV:ITGB3 integrin and causes among others FAK autophosphorylation. EGFL7 competes for binding to the integrin with the ECM molecules fibronectin, MMP2, and collagen IV. The Emilin-like region of EGFL7 interacts with Notch receptor 1–4 and Notch ligands DLL4 and Jag1 and suppresses Notch signaling, resulting in impaired NIC translocation into the nucleus and reduced Hey1/2 and Hes1 transcription. EGFL7 binding to EGFR results in the activation of the signaling pathways extracellular signal-regulated kinase (ERK) and AKT, among others. EGFL7 competes for binding to EGFR with EGF. Abbreviations: EGF, epidermal growth factor; EGFL7, epidermal growth factor-like protein 7; EGFR, epidermal growth factor receptor; ERK, extracellular signal-regulated kinase; FAK, focal adhesion kinase); MMP2, matrix metalloproteinase 2; DLL4, delta like-protein 4; Jag1, Jagged1; NIC, Notch intracellular domain; ECM, extracellular matrix.
Article Snippet: ECs release so-called angiocrine factors [ ], which include the angiogenic factor vascular endothelial growth factor-A (VEGF-A), Jagged1 (Jag1), endothelin, enzymes such as tissue-type plasminogen activator [ ], and epidermal growth factor-like protein-7 (EGFL7) [ ].
Techniques: Binding Assay, Translocation Assay, Activation Assay, Protein-Protein interactions