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Proteins that interact with calgranulin B in the human colon cancer cell line HCT-116

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-tu...

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Autores principales: Myung, Jae Kyung, Yeo, Seung-Gu, Kim, Kyung Hee, Baek, Kwang-Soo, Shin, Daye, Kim, Jong Heon, Cho, Jae Youl, Yoo, Byong Chul
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Impact Journals LLC 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5351672/
https://www.ncbi.nlm.nih.gov/pubmed/28036279
http://dx.doi.org/10.18632/oncotarget.14301
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author Myung, Jae Kyung
Yeo, Seung-Gu
Kim, Kyung Hee
Baek, Kwang-Soo
Shin, Daye
Kim, Jong Heon
Cho, Jae Youl
Yoo, Byong Chul
author_facet Myung, Jae Kyung
Yeo, Seung-Gu
Kim, Kyung Hee
Baek, Kwang-Soo
Shin, Daye
Kim, Jong Heon
Cho, Jae Youl
Yoo, Byong Chul
author_sort Myung, Jae Kyung
collection PubMed
description 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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spelling pubmed-53516722017-04-13 Proteins that interact with calgranulin B in the human colon cancer cell line HCT-116 Myung, Jae Kyung Yeo, Seung-Gu Kim, Kyung Hee Baek, Kwang-Soo Shin, Daye Kim, Jong Heon Cho, Jae Youl Yoo, Byong Chul Oncotarget Research Paper 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. Impact Journals LLC 2016-12-27 /pmc/articles/PMC5351672/ /pubmed/28036279 http://dx.doi.org/10.18632/oncotarget.14301 Text en Copyright: © 2017 Myung et al. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Paper
Myung, Jae Kyung
Yeo, Seung-Gu
Kim, Kyung Hee
Baek, Kwang-Soo
Shin, Daye
Kim, Jong Heon
Cho, Jae Youl
Yoo, Byong Chul
Proteins that interact with calgranulin B in the human colon cancer cell line HCT-116
title Proteins that interact with calgranulin B in the human colon cancer cell line HCT-116
title_full Proteins that interact with calgranulin B in the human colon cancer cell line HCT-116
title_fullStr Proteins that interact with calgranulin B in the human colon cancer cell line HCT-116
title_full_unstemmed Proteins that interact with calgranulin B in the human colon cancer cell line HCT-116
title_short Proteins that interact with calgranulin B in the human colon cancer cell line HCT-116
title_sort proteins that interact with calgranulin b in the human colon cancer cell line hct-116
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5351672/
https://www.ncbi.nlm.nih.gov/pubmed/28036279
http://dx.doi.org/10.18632/oncotarget.14301
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