Proteins that interact with calgranulin B in the human colon cancer cell line HCT-116
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Jae Kyung Myung1,*, Seung-Gu Yeo2,*, Kyung Hee Kim3,4, Kwang-Soo Baek3,5, Daye Shin1,6, Jong Heon Kim1,6, Jae Youl Cho5, Byong Chul Yoo3
1Department of System Cancer Science, Graduate School of Cancer Science and Policy, National Cancer Center, Goyang, Korea
2Department of Radiation Oncology, Soonchunhyang University College of Medicine, Cheonan, Korea
3Colorectal Cancer Branch, Research Institute, National Cancer Center, Goyang, Korea
4Omics Core, Research Institute, National Cancer Center, Goyang, Korea
5Department of Genetic Engineering, Sungkyunkwan University, Suwon, Korea
6Cancer Cell and Molecular Biology Branch, Research Institute, National Cancer Center, Goyang, Korea
*These authors have contributed equally to this work
Byong Chul Yoo, email: email@example.com
Jong Heon Kim, email: firstname.lastname@example.org
Keywords: calgranulin B, S100A9, colon cancer, HCT-116, anti-tumor effect
Received: September 20, 2016 Accepted: December 12, 2016 Published: December 27, 2016
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.
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