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Identification of calgranulin B interacting proteins and network analysis in gastrointestinal cancer cells
Calgranulin B is known to be involved in tumor development, but the underlying molecular mechanism is not clear. To gain insight into possible roles of calgranulin B, we screened for calgranulin B-interacting molecules in the SNU-484 gastric cancer and the SNU-81 colon cancer cells. Calgranulin B-in...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5289589/ https://www.ncbi.nlm.nih.gov/pubmed/28152021 http://dx.doi.org/10.1371/journal.pone.0171232 |
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author | Kim, Kyung-Hee Yeo, Seung-Gu Yoo, Byong Chul Myung, Jae Kyung |
author_facet | Kim, Kyung-Hee Yeo, Seung-Gu Yoo, Byong Chul Myung, Jae Kyung |
author_sort | Kim, Kyung-Hee |
collection | PubMed |
description | Calgranulin B is known to be involved in tumor development, but the underlying molecular mechanism is not clear. To gain insight into possible roles of calgranulin B, we screened for calgranulin B-interacting molecules in the SNU-484 gastric cancer and the SNU-81 colon cancer cells. Calgranulin B-interacting partners were identified by yeast two-hybrid and functional information was obtained by computational analysis. Most of the calgranulin B-interacting partners were involved in metabolic and cellular processes, and found to have molecular function of binding and catalytic activities. Interestingly, 46 molecules in the network of the calgranulin B-interacting proteins are known to be associated with cancer and FKBP2 was found to interact with calgranulin B in both SNU-484 and SNU-81 cells. Polyubiquitin-C encoded by UBC, which exhibited an interaction with calgranulin B, has been associated with various molecules of the extracellular space and plasma membrane identified in our screening, including Na-K-Cl cotransporter 1 and dystonin in SNU-484 cells, and ATPase subunit beta-1 in SNU-81 cells. Our data provide novel insight into the roles of calgranulin B of gastrointestinal cancer cells, and offer new clues suggesting calgranulin B acts as an effector molecule through which the cell can communicate with the tumor microenvironment via polyubiquitin-C. |
format | Online Article Text |
id | pubmed-5289589 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-52895892017-02-17 Identification of calgranulin B interacting proteins and network analysis in gastrointestinal cancer cells Kim, Kyung-Hee Yeo, Seung-Gu Yoo, Byong Chul Myung, Jae Kyung PLoS One Research Article Calgranulin B is known to be involved in tumor development, but the underlying molecular mechanism is not clear. To gain insight into possible roles of calgranulin B, we screened for calgranulin B-interacting molecules in the SNU-484 gastric cancer and the SNU-81 colon cancer cells. Calgranulin B-interacting partners were identified by yeast two-hybrid and functional information was obtained by computational analysis. Most of the calgranulin B-interacting partners were involved in metabolic and cellular processes, and found to have molecular function of binding and catalytic activities. Interestingly, 46 molecules in the network of the calgranulin B-interacting proteins are known to be associated with cancer and FKBP2 was found to interact with calgranulin B in both SNU-484 and SNU-81 cells. Polyubiquitin-C encoded by UBC, which exhibited an interaction with calgranulin B, has been associated with various molecules of the extracellular space and plasma membrane identified in our screening, including Na-K-Cl cotransporter 1 and dystonin in SNU-484 cells, and ATPase subunit beta-1 in SNU-81 cells. Our data provide novel insight into the roles of calgranulin B of gastrointestinal cancer cells, and offer new clues suggesting calgranulin B acts as an effector molecule through which the cell can communicate with the tumor microenvironment via polyubiquitin-C. Public Library of Science 2017-02-02 /pmc/articles/PMC5289589/ /pubmed/28152021 http://dx.doi.org/10.1371/journal.pone.0171232 Text en © 2017 Kim et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Kim, Kyung-Hee Yeo, Seung-Gu Yoo, Byong Chul Myung, Jae Kyung Identification of calgranulin B interacting proteins and network analysis in gastrointestinal cancer cells |
title | Identification of calgranulin B interacting proteins and network analysis in gastrointestinal cancer cells |
title_full | Identification of calgranulin B interacting proteins and network analysis in gastrointestinal cancer cells |
title_fullStr | Identification of calgranulin B interacting proteins and network analysis in gastrointestinal cancer cells |
title_full_unstemmed | Identification of calgranulin B interacting proteins and network analysis in gastrointestinal cancer cells |
title_short | Identification of calgranulin B interacting proteins and network analysis in gastrointestinal cancer cells |
title_sort | identification of calgranulin b interacting proteins and network analysis in gastrointestinal cancer cells |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5289589/ https://www.ncbi.nlm.nih.gov/pubmed/28152021 http://dx.doi.org/10.1371/journal.pone.0171232 |
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