Cargando…

Semantic Analysis of Posttranslational Modification of Proteins Accumulated in Thyroid Cancer Cells Exposed to Simulated Microgravity

When monolayers of tissue cancer cells of various origins are exposed to real or simulated microgravity, many cells leave the monolayer and assemble to three-dimensional (3D) aggregates (spheroids). In order to define the cellular machinery leading to this change in growth behavior of FTC-133 human...

Descripción completa

Detalles Bibliográficos
Autores principales: Bauer, Johann, Wehland, Markus, Infanger, Manfred, Grimm, Daniela, Gombocz, Erich
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6121900/
https://www.ncbi.nlm.nih.gov/pubmed/30071661
http://dx.doi.org/10.3390/ijms19082257
_version_ 1783352558920663040
author Bauer, Johann
Wehland, Markus
Infanger, Manfred
Grimm, Daniela
Gombocz, Erich
author_facet Bauer, Johann
Wehland, Markus
Infanger, Manfred
Grimm, Daniela
Gombocz, Erich
author_sort Bauer, Johann
collection PubMed
description When monolayers of tissue cancer cells of various origins are exposed to real or simulated microgravity, many cells leave the monolayer and assemble to three-dimensional (3D) aggregates (spheroids). In order to define the cellular machinery leading to this change in growth behavior of FTC-133 human thyroid cancer cells and MCF-7 breast cancer cells, we recently performed proteome analyses on these cell lines and determined the proteins’ accumulation in monolayer cells grown under 1g-conditions as well as in the cells of spheroids assembled under simulated microgravity during three and 14 days, respectively. At that time, an influence of the increment or decrement of some of the more than 5000 proteins detected in each cell line was investigated. In this study, we focused on posttranslational modifications (PTMs) of proteins. For this purpose, we selected candidates from the list of the proteins detected in the two preceding proteome analyses, which showed significant accumulation in spheroid cells as compared to 1g monolayer cells. Then we searched for those PTMs of the selected proteins, which according to the literature have already been determined experimentally. Using the Semantic Protocol and RDF Query Language (SPARQL), various databases were examined. Most efficient was the search in the latest version of the dbPTM database. In total, we found 72 different classes of PTMs comprising mainly phosphorylation, glycosylation, ubiquitination and acetylation. Most interestingly, in 35 of the 69 proteins, N6 residues of lysine are modifiable.
format Online
Article
Text
id pubmed-6121900
institution National Center for Biotechnology Information
language English
publishDate 2018
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-61219002018-09-07 Semantic Analysis of Posttranslational Modification of Proteins Accumulated in Thyroid Cancer Cells Exposed to Simulated Microgravity Bauer, Johann Wehland, Markus Infanger, Manfred Grimm, Daniela Gombocz, Erich Int J Mol Sci Article When monolayers of tissue cancer cells of various origins are exposed to real or simulated microgravity, many cells leave the monolayer and assemble to three-dimensional (3D) aggregates (spheroids). In order to define the cellular machinery leading to this change in growth behavior of FTC-133 human thyroid cancer cells and MCF-7 breast cancer cells, we recently performed proteome analyses on these cell lines and determined the proteins’ accumulation in monolayer cells grown under 1g-conditions as well as in the cells of spheroids assembled under simulated microgravity during three and 14 days, respectively. At that time, an influence of the increment or decrement of some of the more than 5000 proteins detected in each cell line was investigated. In this study, we focused on posttranslational modifications (PTMs) of proteins. For this purpose, we selected candidates from the list of the proteins detected in the two preceding proteome analyses, which showed significant accumulation in spheroid cells as compared to 1g monolayer cells. Then we searched for those PTMs of the selected proteins, which according to the literature have already been determined experimentally. Using the Semantic Protocol and RDF Query Language (SPARQL), various databases were examined. Most efficient was the search in the latest version of the dbPTM database. In total, we found 72 different classes of PTMs comprising mainly phosphorylation, glycosylation, ubiquitination and acetylation. Most interestingly, in 35 of the 69 proteins, N6 residues of lysine are modifiable. MDPI 2018-08-01 /pmc/articles/PMC6121900/ /pubmed/30071661 http://dx.doi.org/10.3390/ijms19082257 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Bauer, Johann
Wehland, Markus
Infanger, Manfred
Grimm, Daniela
Gombocz, Erich
Semantic Analysis of Posttranslational Modification of Proteins Accumulated in Thyroid Cancer Cells Exposed to Simulated Microgravity
title Semantic Analysis of Posttranslational Modification of Proteins Accumulated in Thyroid Cancer Cells Exposed to Simulated Microgravity
title_full Semantic Analysis of Posttranslational Modification of Proteins Accumulated in Thyroid Cancer Cells Exposed to Simulated Microgravity
title_fullStr Semantic Analysis of Posttranslational Modification of Proteins Accumulated in Thyroid Cancer Cells Exposed to Simulated Microgravity
title_full_unstemmed Semantic Analysis of Posttranslational Modification of Proteins Accumulated in Thyroid Cancer Cells Exposed to Simulated Microgravity
title_short Semantic Analysis of Posttranslational Modification of Proteins Accumulated in Thyroid Cancer Cells Exposed to Simulated Microgravity
title_sort semantic analysis of posttranslational modification of proteins accumulated in thyroid cancer cells exposed to simulated microgravity
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6121900/
https://www.ncbi.nlm.nih.gov/pubmed/30071661
http://dx.doi.org/10.3390/ijms19082257
work_keys_str_mv AT bauerjohann semanticanalysisofposttranslationalmodificationofproteinsaccumulatedinthyroidcancercellsexposedtosimulatedmicrogravity
AT wehlandmarkus semanticanalysisofposttranslationalmodificationofproteinsaccumulatedinthyroidcancercellsexposedtosimulatedmicrogravity
AT infangermanfred semanticanalysisofposttranslationalmodificationofproteinsaccumulatedinthyroidcancercellsexposedtosimulatedmicrogravity
AT grimmdaniela semanticanalysisofposttranslationalmodificationofproteinsaccumulatedinthyroidcancercellsexposedtosimulatedmicrogravity
AT gomboczerich semanticanalysisofposttranslationalmodificationofproteinsaccumulatedinthyroidcancercellsexposedtosimulatedmicrogravity