| الوصف: |
// Jae Kyung Myung 1, * , Seung-Gu Yeo 2, * , Kyung Hee Kim 3, 4 , Kwang-Soo Baek 3, 5 , Daye Shin 1, 6 , Jong Heon Kim 1, 6 , Jae Youl Cho 5 , Byong Chul Yoo 3 1 Department of System Cancer Science, Graduate School of Cancer Science and Policy, National Cancer Center, Goyang, Korea 2 Department of Radiation Oncology, Soonchunhyang University College of Medicine, Cheonan, Korea 3 Colorectal Cancer Branch, Research Institute, National Cancer Center, Goyang, Korea 4 Omics Core, Research Institute, National Cancer Center, Goyang, Korea 5 Department of Genetic Engineering, Sungkyunkwan University, Suwon, Korea 6 Cancer Cell and Molecular Biology Branch, Research Institute, National Cancer Center, Goyang, Korea * These authors have contributed equally to this work Correspondence to: Byong Chul Yoo, email: yoo_akh@ncc.re.kr Jong Heon Kim, email: jhkim@ncc.re.kr Keywords: calgranulin B, S100A9, colon cancer, HCT-116, anti-tumor effect Received: September 20, 2016 Accepted: December 12, 2016 Published: December 27, 2016 ABSTRACT Calgranulin B is released from immune cells and can be internalized into colon cancer cells to prevent proliferation. The present study aimed to identify proteins that interact with calgranulin B to suppress the proliferation of colon cancer cells, and to obtain information on the underlying anti-tumor mechanism(s) of calgranulin B. Calgranulin B expression was induced in colon cancer cell line HCT-116 by infection with calgranulin B-FLAG expressing lentivirus, and it led to a significant suppression of cell proliferation. Proteins that interacted with calgranulin B were obtained by immunoprecipitation using whole homogenate of lentivirus-infected HCT-116 cells which expressing calgranulin B-FLAG, and identified using liquid chromatography-mass spectrometry/mass spectrometry analysis. A total of 454 proteins were identified that potentially interact with calgranulin B, and most identified proteins were associated with RNA processing, post-transcriptional modifications and the EIF2 signaling pathway. Direct interaction of calgranulin B with flotillin-1, dynein intermediate chain 1, and CD59 glycoprotein has been confirmed, and the molecules N-myc proto-oncogene protein, rapamycin-insensitive companion of mTOR, and myc proto-oncogene protein were shown to regulate calgranulin B-interacting proteins. Our results provide new insight and useful information to explain the possible mechanism(s) underlying the role of calgranulin B as an anti-tumor effector in colon cancer cells. |
