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- W2463687777 abstract "Epidermal growth factor (EGF) is a 53-amino-acid cytokine (6.2 kDa) secreted by ectodermic cells, monocytes, kidneys, and duodenal glands (1). EGF stimulates growth of epidermal and epithelial cells. EGF and at least seven other growth factors and their transmembrane receptor kinases play important roles in cell proliferation, survival, adhesion, migration, and differentiation. The EGF receptor (EGFR) family consists of four transmembrane receptors, including EGFR (HER1/erbB-1), HER2 (erbB-2/neu), HER3 (erbB-3), and HER4 (erbB-4) (2). HER1, HER3, and HER4 comprise three major functional domains: an extracellular ligand-binding domain, a hydrophobic transmembrane domain, and a cytoplasmic tyrosine kinase domain (2, 3). EGFR, which is overexpressed in many malignant epithelial tumors, contributes to gene amplification, which is believed to introduce mutations in the receptor (4). The overexpression, amplification, and/or mutation of EGFR can lead to the development of cancer. The most common mutation observed in the receptor is the deletion of a segment (amino acid residues 6–273 of the EGFR extracellular domain), including the ligand-binding region, which results in the generation of a variant known as constitutively activated variant III EGFR (EGFRvIII) (5). Although EGFRvIII is nonresponsive to EGF, it remains a constantly operating downstream tyrosine kinase signaling pathway that appears to promote the development of a neoplastic phenotype, particularly for glioblastoma and to some extent for other cancers such as those of the prostate and the breast (6). EGFRvIII has not been identified in normal tissues.Monoclonal antibody (mAb) 806 and chimeric antibody ch806 (7, 8), which specifically target EGFRvIII, were radiolabeled for imaging EGFRvIII expression in tumors. However, the pharmacokinetics of the intact radiolabeled mAb, with high liver uptake and slow blood elimination, are generally not ideal for imaging because of poor tissue and tumor penetration (9). Smaller antibody fragments and peptides have better imaging pharmacokinetics because they are rapidly excreted by the kidneys. Denholt et al. (10) identified an EGFRvIII-targeting peptide, H-Phe-Ala-Leu-Gly-Glu-Ala-NH2 (H-FALGEA-NH2) using a Positional Scanning Synthetic Combinatorial Library. H-FALGEA-NH2 was labeled with 4-[18F]fluorobenzoic acid ([18F]FBA) to form [18F]FBA-FALGEA-NH2 (11). [18F]FBA-FALGEA-NH2 has been evaluated for imaging of EGFRvIII expression in human glioblastoma multiforme (GBM) tumors in nude mice using positron emission tomography (PET)." @default.
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- W2463687777 date "2011-12-08" @default.
- W2463687777 modified "2023-09-24" @default.
- W2463687777 title "4-[18F]Fluorobenzoyl-Phe-Ala-Leu-Gly-Glu-Ala-NH2" @default.
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