Cargando…
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...
Autores principales: | , , , , , , , |
---|---|
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 |
_version_ | 1782514809894338560 |
---|---|
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. |
format | Online Article Text |
id | pubmed-5351672 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Impact Journals LLC |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT myungjaekyung proteinsthatinteractwithcalgranulinbinthehumancoloncancercelllinehct116 AT yeoseunggu proteinsthatinteractwithcalgranulinbinthehumancoloncancercelllinehct116 AT kimkyunghee proteinsthatinteractwithcalgranulinbinthehumancoloncancercelllinehct116 AT baekkwangsoo proteinsthatinteractwithcalgranulinbinthehumancoloncancercelllinehct116 AT shindaye proteinsthatinteractwithcalgranulinbinthehumancoloncancercelllinehct116 AT kimjongheon proteinsthatinteractwithcalgranulinbinthehumancoloncancercelllinehct116 AT chojaeyoul proteinsthatinteractwithcalgranulinbinthehumancoloncancercelllinehct116 AT yoobyongchul proteinsthatinteractwithcalgranulinbinthehumancoloncancercelllinehct116 |