American Association for Cancer Research
crc-23-0087_fig1.png (174.06 kB)

FIGURE 1 from EphA2 Proteolytic Fragment as a Sensitive Diagnostic Biomarker for Very Early-stage Pancreatic Ductal Carcinoma

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posted on 2023-09-15, 14:20 authored by Shinya Sato, Masatoshi Nakagawa, Takeshi Terashima, Soichiro Morinaga, Yohei Miyagi, Eisaku Yoshida, Toru Yoshimura, Motoharu Seiki, Shuichi Kaneko, Makoto Ueno, Taro Yamashita, Naohiko Koshikawa

Antigens and antibody epitopes used in the CLIA. A, Schematic of EphA2 molecules. Wild-type EphA2 is an intact form that contains a transmembrane (TM) cytoplasmic domain. EphA2-NF is an N-terminal fragment released by MT1-MMP processing. EphA2-FL (full-length) is an extracellular form without the TM and cytoplasmic domains. Epitopes of the EphA2 antibodies are shown. SP, ligand-binding signal peptide; CR, cysteine-rich. B, Standard curves of EphA2-NF (circles) and EphA2-FL (squares) for the CLIA using mAbs against 76A1 and 62A1. The detection range of EphA2-NF was 10–105 pg/mL, while the detection of EphA2-FL was negligible (squares).


Abbott Laboratories (Abbott)

Japan Agency for Medical Research and Development (AMED)

MEXT | Japan Society for the Promotion of Science (JSPS)

Princess Takamatsu Cancer Research Fund



EphA2 N-terminus deletion is involved in pancreatic ductal carcinoma development from high-risk IPMN and EphA2-NF produced by cleavage can be used as a serum biomarker to diagnose pancreatic ductal carcinoma and predict pancreatic ductal carcinoma development from high-risk IPMN.