Abstract
Epidermal growth factor receptor (EGFR) and vascular endothelial growth factor receptor (VEGFR) are two extensively studied membrane-bound receptor tyrosine kinase proteins that are frequently overexpressed in many cancers. As a result, these receptor families constitute attractive targets for imaging and therapeutic applications in the detection and treatment of cancer. This review explores the dynamic structure and structure-function relationships of these two growth factor receptors and their significance as it relates to theranostics of cancer, followed by some of the common inhibition modalities frequently employed to target EGFR and VEGFR, such as tyrosine kinase inhibitors (TKIs), antibodies, nanobodies, and peptides. A summary of the recent advances in molecular imaging techniques, including positron emission tomography (PET), single-photon emission computerized tomography (SPECT), computed tomography (CT), magnetic resonance imaging (MRI), and optical imaging (OI), and in particular, near-IR fluorescence imaging using tetrapyrrolic-based fluorophores, concludes this review.
Highlights
Epidermal growth factor receptor (EGFR) and vascular endothelial growth factor receptor (VEGFR) overexpression is frequently found in several types of tumors, including breast, lung, colon, and ovarian, and it is a very attractive therapeutic and imaging target for cancer treatment research [1,2]
(b) bind to VEGF receptors and activate the immune response. There is another class of molecule, VEGF-Trap, a fusion protein that consists of VEGF receptor-1 (VEGFR-1) and VEGFR-2 binding domains and Fc region of IgG1 antibody
A large number of ligands have been developed that target these families of receptors, from high molecular weight antibodies, affibodies and nanobodies, to low molecular weight tyrosine kinase inhibitors (TKIs) and small peptides. The targeting of these receptors has allowed for efficient imaging and targeted therapy options for various tumors that overexpress these proteins, advancing the field of focused and personalized medicine of cancer
Summary
EGFR and VEGFR overexpression is frequently found in several types of tumors, including breast, lung, colon, and ovarian, and it is a very attractive therapeutic and imaging target for cancer treatment research [1,2]. It is of great importance to enhance our understanding of the structure and structurefunction relationship of the targeted receptors in order to design and create effective drug targets To this end, we will first discuss the structure of the EGFR and VEGFR receptor tyrosine kinase (RTK) domains and their relevant function in kinase activity. Structure of EGFR Each ErbB family member protein consists of a large glycosylated N-terminal extracellular domain (ECD) consisting of ~620 amino acids with a ligand-binding region [7]. It has been shown that seven of the EGF ligands can stimulate different downstream signaling effects: EGF, HB-EGF, and BTC promote receptor downregulation and a shorter signaling pulse, in contrast to TGF-a, AREG, EREG, and EPGN, which promote receptor recycling and a sustained signal [17]
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