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Fibroblast-derived Gremlin1 localises to epithelial cells at the base of the intestinal crypt
Gremlin1 (GREM1) is a secreted glycoprotein member of the differential screening-selected gene in aberrant neuroblastoma (DAN) family of bone morphogenetic protein (BMP) antagonists, which binds to BMPs preventing their receptor engagement. Previous studies have identified that stage II colorectal c...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Impact Journals LLC
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6659803/ https://www.ncbi.nlm.nih.gov/pubmed/31384391 http://dx.doi.org/10.18632/oncotarget.27050 |
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author | Dutton, Louise R. Hoare, Owen P. McCorry, Amy M.B. Redmond, Keara L. Adam, Noor Eisa Canamara, Shannon Bingham, Victoria Mullan, Paul B. Lawler, Mark Dunne, Philip D. Brazil, Derek P. |
author_facet | Dutton, Louise R. Hoare, Owen P. McCorry, Amy M.B. Redmond, Keara L. Adam, Noor Eisa Canamara, Shannon Bingham, Victoria Mullan, Paul B. Lawler, Mark Dunne, Philip D. Brazil, Derek P. |
author_sort | Dutton, Louise R. |
collection | PubMed |
description | Gremlin1 (GREM1) is a secreted glycoprotein member of the differential screening-selected gene in aberrant neuroblastoma (DAN) family of bone morphogenetic protein (BMP) antagonists, which binds to BMPs preventing their receptor engagement. Previous studies have identified that stage II colorectal cancer (CRC) patients with high levels of GREM1 gene expression in their tumour tissue have a poorer prognosis. Using a series of in silico and in situ methodologies, we demonstrate that GREM1 gene expression is significantly higher (p < 0.0001) in CRC consensus molecular subtype 4 (CMS4), compared to the other CMS subtypes and correlates (p < 0.0001) with levels of cancer-associated fibroblasts (CAFs) within the CRC tumour microenvironment (TME). Our optimised immunohistochemistry protocol identified endogenous GREM1 protein expression in both the muscularis mucosa and adjacent colonic crypt bases in mouse intestine, in contrast to RNA expression which was shown to localise specifically to the muscularis mucosa, as determined by in situ hybridisation. Importantly, we demonstrate that cells with high levels of GREM1 expression display low levels of phospho-Smad1/5, consistent with reduced BMP signalling. Taken together, these data highlight a novel paracrine signalling circuit, which involves uptake of mature GREM1 protein by colonic crypt cells following secretion from neighbouring fibroblasts in the TME. |
format | Online Article Text |
id | pubmed-6659803 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Impact Journals LLC |
record_format | MEDLINE/PubMed |
spelling | pubmed-66598032019-08-05 Fibroblast-derived Gremlin1 localises to epithelial cells at the base of the intestinal crypt Dutton, Louise R. Hoare, Owen P. McCorry, Amy M.B. Redmond, Keara L. Adam, Noor Eisa Canamara, Shannon Bingham, Victoria Mullan, Paul B. Lawler, Mark Dunne, Philip D. Brazil, Derek P. Oncotarget Research Paper Gremlin1 (GREM1) is a secreted glycoprotein member of the differential screening-selected gene in aberrant neuroblastoma (DAN) family of bone morphogenetic protein (BMP) antagonists, which binds to BMPs preventing their receptor engagement. Previous studies have identified that stage II colorectal cancer (CRC) patients with high levels of GREM1 gene expression in their tumour tissue have a poorer prognosis. Using a series of in silico and in situ methodologies, we demonstrate that GREM1 gene expression is significantly higher (p < 0.0001) in CRC consensus molecular subtype 4 (CMS4), compared to the other CMS subtypes and correlates (p < 0.0001) with levels of cancer-associated fibroblasts (CAFs) within the CRC tumour microenvironment (TME). Our optimised immunohistochemistry protocol identified endogenous GREM1 protein expression in both the muscularis mucosa and adjacent colonic crypt bases in mouse intestine, in contrast to RNA expression which was shown to localise specifically to the muscularis mucosa, as determined by in situ hybridisation. Importantly, we demonstrate that cells with high levels of GREM1 expression display low levels of phospho-Smad1/5, consistent with reduced BMP signalling. Taken together, these data highlight a novel paracrine signalling circuit, which involves uptake of mature GREM1 protein by colonic crypt cells following secretion from neighbouring fibroblasts in the TME. Impact Journals LLC 2019-07-23 /pmc/articles/PMC6659803/ /pubmed/31384391 http://dx.doi.org/10.18632/oncotarget.27050 Text en Copyright © 2019 Dutton et al. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC BY) 3.0 License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Paper Dutton, Louise R. Hoare, Owen P. McCorry, Amy M.B. Redmond, Keara L. Adam, Noor Eisa Canamara, Shannon Bingham, Victoria Mullan, Paul B. Lawler, Mark Dunne, Philip D. Brazil, Derek P. Fibroblast-derived Gremlin1 localises to epithelial cells at the base of the intestinal crypt |
title | Fibroblast-derived Gremlin1 localises to epithelial cells at the base of the intestinal crypt |
title_full | Fibroblast-derived Gremlin1 localises to epithelial cells at the base of the intestinal crypt |
title_fullStr | Fibroblast-derived Gremlin1 localises to epithelial cells at the base of the intestinal crypt |
title_full_unstemmed | Fibroblast-derived Gremlin1 localises to epithelial cells at the base of the intestinal crypt |
title_short | Fibroblast-derived Gremlin1 localises to epithelial cells at the base of the intestinal crypt |
title_sort | fibroblast-derived gremlin1 localises to epithelial cells at the base of the intestinal crypt |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6659803/ https://www.ncbi.nlm.nih.gov/pubmed/31384391 http://dx.doi.org/10.18632/oncotarget.27050 |
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