Related Experiment Video
Updated: Aug 9, 2026
Expression, Purification, and Antimicrobial Activity of S100A12
Published on: May 13, 2017
Proteins that interact with calgranulin B in the human colon cancer cell line HCT-116
Jae Kyung Myung1, Seung-Gu Yeo2, Kyung Hee Kim3,4
1Department of System Cancer Science, Graduate School of Cancer Science and Policy, National Cancer Center, Goyang, Korea.
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.
Insights
Calgranulin B, released by immune cells, suppresses colon cancer cell proliferation. This study identified 454 interacting proteins, revealing mechanisms of its anti-tumor activity in colon cancer.
Area of Science:
- Immunology
- Molecular Biology
- Oncology
Background:
- Calgranulin B is an immune cell-released protein.
- It can be internalized by colon cancer cells to inhibit proliferation.
- The anti-tumor mechanisms of Calgranulin B require further elucidation.
Purpose of the Study:
- To identify proteins interacting with Calgranulin B in colon cancer cells.
- To understand the anti-tumor mechanisms of Calgranulin B.
- To investigate the role of Calgranulin B in colon cancer proliferation.
Main Methods:
- Calgranulin B expression was induced in HCT-116 colon cancer cells using lentivirus.
- Proteins interacting with Calgranulin B were identified via immunoprecipitation and liquid chromatography-mass spectrometry/mass spectrometry.
- Direct interactions were confirmed, and regulatory molecules were identified.
Main Results:
- Calgranulin B expression significantly suppressed colon cancer cell proliferation.
- 454 proteins potentially interacting with Calgranulin B were identified.
- Interacting proteins are mainly associated with RNA processing, post-transcriptional modifications, and the EIF2 signaling pathway.
- Direct interactions with flotillin-1, dynein intermediate chain 1, and CD59 glycoprotein were confirmed.
- N-myc proto-oncogene protein, RACK1, and c-Myc were identified as regulators.
Conclusions:
- Calgranulin B acts as an anti-tumor effector in colon cancer.
- Protein interactions and associated pathways provide insight into Calgranulin B's anti-cancer mechanisms.
- This study offers valuable information for understanding Calgranulin B's therapeutic potential in colon cancer.
