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Article ; Online: SMAD2/3 mediate oncogenic effects of TGF-β in the absence of SMAD4.

Communications biology

2022 Volume 5, Issue 1, Page(s) 1068

Abstract: TGF-β signaling is involved in pancreatic ductal adenocarcinoma (PDAC) tumorigenesis, representing one of the four major pathways genetically altered in 100% of PDAC cases. TGF-β exerts complex and pleiotropic effects in cancers, notably via the ... ...

Abstract	TGF-β signaling is involved in pancreatic ductal adenocarcinoma (PDAC) tumorigenesis, representing one of the four major pathways genetically altered in 100% of PDAC cases. TGF-β exerts complex and pleiotropic effects in cancers, notably via the activation of SMAD pathways, predominantly SMAD2/3/4. Though SMAD2 and 3 are rarely mutated in cancers, SMAD4 is lost in about 50% of PDAC, and the role of SMAD2/3 in a SMAD4-null context remains understudied. We herein provide evidence of a SMAD2/3 oncogenic effect in response to TGF-β1 in SMAD4-null human PDAC cancer cells. We report that inactivation of SMAD2/3 in SMAD4-negative PDAC cells compromises TGF-β-driven collective migration mediated by FAK and Rho/Rac signaling. Moreover, RNA-sequencing analyses highlight a TGF-β gene signature related to aggressiveness mediated by SMAD2/3 in the absence of SMAD4. Using a PDAC patient cohort, we reveal that SMAD4-negative tumors with high levels of phospho-SMAD2 are more aggressive and have a poorer prognosis. Thus, loss of SMAD4 tumor suppressive activity in PDAC leads to an oncogenic gain-of-function of SMAD2/3, and to the onset of associated deleterious effects.
MeSH term(s)	Carcinogenesis/genetics ; Carcinoma, Pancreatic Ductal/metabolism ; Humans ; Pancreatic Neoplasms/metabolism ; RNA ; Smad2 Protein/genetics ; Smad2 Protein/metabolism ; Smad3 Protein/metabolism ; Smad4 Protein/genetics ; Smad4 Protein/metabolism ; Transforming Growth Factor beta/pharmacology ; Transforming Growth Factor beta1/metabolism ; Pancreatic Neoplasms
Chemical Substances	SMAD2 protein, human ; SMAD3 protein, human ; SMAD4 protein, human ; Smad2 Protein ; Smad3 Protein ; Smad4 Protein ; Transforming Growth Factor beta ; Transforming Growth Factor beta1 ; RNA (63231-63-0)
Language	English
Publishing date	2022-10-07
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2399-3642
ISSN (online)	2399-3642
DOI	10.1038/s42003-022-03994-6
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Article ; Online: Generation of a conditional Flpo/FRT mouse model expressing constitutively active TGFβ in fibroblasts.

Cardot-Ruffino, Victoire / Chauvet, Véronique / Caligaris, Cassandre / Bertrand-Chapel, Adrien / Chuvin, Nicolas / Pommier, Roxane M / Valcourt, Ulrich / Vincent, David F / Martel, Sylvie / Aires, Sophie / Kaniewski, Bastien / Dubus, Pierre / Cassier, Philippe / Sentis, Stéphanie / Bartholin, Laurent

Scientific reports

2020 Volume 10, Issue 1, Page(s) 3880

Abstract: Transforming growth factor (TGFβ) is a secreted factor, which accumulates in tissues during many physio- and pathological processes such as embryonic development, wound healing, fibrosis and cancer. In order to analyze the effects of increased ... ...

Abstract	Transforming growth factor (TGFβ) is a secreted factor, which accumulates in tissues during many physio- and pathological processes such as embryonic development, wound healing, fibrosis and cancer. In order to analyze the effects of increased microenvironmental TGFβ concentration in vivo, we developed a conditional transgenic mouse model (Flpo/Frt system) expressing bioactive TGFβ in fibroblasts, a cell population present in the microenvironment of almost all tissues. To achieve this, we created the genetically-engineered [Fsp1-Flpo;
MeSH term(s)	Animals ; Fibroblasts/metabolism ; Gene Expression ; Genetic Engineering ; Hep G2 Cells ; Humans ; Mice ; Mice, Transgenic ; Models, Animal ; Transforming Growth Factor beta/genetics
Chemical Substances	Transforming Growth Factor beta
Language	English
Publishing date	2020-03-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-020-60272-3
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Article ; Online: Generation of an Fsp1 (fibroblast-specific protein 1)-Flpo transgenic mouse strain.

Cardot-Ruffino, Victoire / Chauvet, Véronique / Caligaris, Cassandre / Bertrand-Chapel, Adrien / Chuvin, Nicolas / Pommier, Roxane M / Valcourt, Ulrich / Vincent, David / Martel, Sylvie / Aires, Sophie / Kaniewski, Bastien / Dubus, Pierre / Cassier, Philippe / Sentis, Stéphanie / Bartholin, Laurent

Genesis (New York, N.Y. : 2000)

2020 Volume 58, Issue 5, Page(s) e23359

Abstract: Recombination systems represent a major breakthrough in the field of genetic model engineering. The Flp recombinases (Flp, Flpe, and Flpo) bind and cleave DNA Frt sites. We created a transgenic mouse strain ([Fsp1-Flpo]) expressing the Flpo recombinase ... ...

Abstract	Recombination systems represent a major breakthrough in the field of genetic model engineering. The Flp recombinases (Flp, Flpe, and Flpo) bind and cleave DNA Frt sites. We created a transgenic mouse strain ([Fsp1-Flpo]) expressing the Flpo recombinase in fibroblasts. This strain was obtained by random insertion inside mouse zygotes after pronuclear injection. Flpo expression was placed under the control of the promoter of Fsp1 (fibroblast-specific protein 1) gene, whose expression starts after gastrulation at Day 8.5 in cells of mesenchymal origin. We verified the correct expression and function of the Flpo enzyme by several ex vivo and in vivo approaches. The [Fsp1-Flpo] strain represents a genuine tool to further target the recombination of transgenes with Frt sites specifically in cells of mesenchymal origin or with a fibroblastic phenotype.
MeSH term(s)	Animals ; Cells, Cultured ; DNA Nucleotidyltransferases/genetics ; DNA Nucleotidyltransferases/metabolism ; Fibroblasts/metabolism ; Gastrula/metabolism ; Gene Targeting/methods ; HaCaT Cells ; Humans ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Promoter Regions, Genetic ; S100 Calcium-Binding Protein A4/genetics ; Zygote/metabolism
Chemical Substances	S100 Calcium-Binding Protein A4 ; S100a4 protein, mouse ; DNA Nucleotidyltransferases (EC 2.7.7.-) ; FLP recombinase (EC 2.7.7.-)
Language	English
Publishing date	2020-03-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2004544-X
ISSN	1526-968X ; 1526-954X
ISSN (online)	1526-968X
ISSN	1526-954X
DOI	10.1002/dvg.23359
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Article ; Online: Correction: Schwann cells support oncogenic potential of pancreatic cancer cells through TGFβ signaling.

Roger, Elodie / Martel, Sylvie / Bertrand-Chapel, Adrien / Depollier, Arnaud / Chuvin, Nicolas / Pommier, Roxane M / Yacoub, Karam / Caligaris, Cassandre / Cardot-Ruffino, Victoire / Chauvet, Véronique / Aires, Sophie / Mohkam, Kayvan / Mabrut, Jean-Yves / Adham, Mustapha / Fenouil, Tanguy / Hervieu, Valérie / Broutier, Laura / Castets, Marie / Neuzillet, Cindy /

Cassier, Philippe A / Tomasini, Richard / Sentis, Stéphanie / Bartholin, Laurent

Cell death & disease

2020 Volume 11, Issue 1, Page(s) 57

Abstract: The original version of this article contained an error in the name of one of the co-authors (Kayvan Mohkam). This has been corrected in the PDF and HTML versions. ...

Abstract	The original version of this article contained an error in the name of one of the co-authors (Kayvan Mohkam). This has been corrected in the PDF and HTML versions.
Language	English
Publishing date	2020-01-23
Publishing country	England
Document type	Published Erratum
ZDB-ID	2541626-1
ISSN	2041-4889 ; 2041-4889
ISSN (online)	2041-4889
ISSN	2041-4889
DOI	10.1038/s41419-020-2262-1
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Article ; Online: Cracking the estrogen receptor's posttranslational code in breast tumors.

Le Romancer, Muriel / Poulard, Coralie / Cohen, Pascale / Sentis, Stéphanie / Renoir, Jack-Michel / Corbo, Laura

Endocrine reviews

2011 Volume 32, Issue 5, Page(s) 597–622

Abstract: Estrogen signaling pathways, because of their central role in regulating the growth and survival of breast tumor cells, have been identified as suitable and efficient targets for cancer therapies. Agents blocking estrogen activity are already widely used ...

Abstract	Estrogen signaling pathways, because of their central role in regulating the growth and survival of breast tumor cells, have been identified as suitable and efficient targets for cancer therapies. Agents blocking estrogen activity are already widely used clinically, and many new molecules have entered clinical trials, but intrinsic or acquired resistance to treatment limits their efficacy. The basic molecular studies underlying estrogen signaling have defined the critical role of estrogen receptors (ER) in many aspects of breast tumorigenesis. However, important knowledge gaps remain about the role of posttranslational modifications (PTM) of ER in initiation and progression of breast carcinogenesis. Whereas major attention has been focused on the phosphorylation of ER, many other PTM (such as acetylation, ubiquitination, sumoylation, methylation, and palmitoylation) have been identified as events modifying ER expression and stability, subcellular localization, and sensitivity to hormonal response. This article will provide an overview of the current and emerging knowledge on ER PTM, with a particular focus on their deregulation in breast cancer. We also discuss their clinical relevance and the functional relationship between PTM. A thorough understanding of the complete picture of these modifications in ER carcinogenesis might not only open new avenues for identifying new markers for prognosis or prediction of response to endocrine therapy but also could promote the development of novel therapeutic strategies.
MeSH term(s)	Acetylation ; Animals ; Antineoplastic Agents, Hormonal ; Breast Neoplasms/chemistry ; Breast Neoplasms/drug therapy ; Estrogen Receptor Modulators/therapeutic use ; Estrogen Receptor alpha/analysis ; Estrogen Receptor alpha/genetics ; Estrogen Receptor alpha/physiology ; Estrogen Receptor beta/genetics ; Estrogen Receptor beta/physiology ; Estrogens/physiology ; Female ; Humans ; Methylation ; Mutation ; Phosphorylation ; Protein Processing, Post-Translational/drug effects ; Protein Processing, Post-Translational/physiology ; Receptors, Estrogen/chemistry ; Receptors, Estrogen/genetics ; Receptors, Estrogen/physiology ; Signal Transduction ; Ubiquitination
Chemical Substances	Antineoplastic Agents, Hormonal ; Estrogen Receptor Modulators ; Estrogen Receptor alpha ; Estrogen Receptor beta ; Estrogens ; Receptors, Estrogen
Language	English
Publishing date	2011-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	603096-8
ISSN	1945-7189 ; 0163-769X
ISSN (online)	1945-7189
ISSN	0163-769X
DOI	10.1210/er.2010-0016
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Article: Les modifications post-traductionnelles orchestrent l'action du récepteur des oestrogènes ERalpha dans les tumeurs mammaires.

Poulard, Coralie / Bouchekioua-Bouzaghou, Katia / Sentis, Stéphanie / Corbo, Laura / Le Romancer, Muriel

Medecine sciences : M/S

2010 Volume 26, Issue 6-7, Page(s) 636–640

Abstract: Regulation of the proteome by post-translational modifications (PTM) emerges as a major contributing factor to the functional diversity in biology regulating cellular processes. Because PTM are key to the physiologic functions of the proteins involved, ... ...

Title translation	Post-translational modifications modulate estrogen receptor alpha activity in breast tumors.
Abstract	Regulation of the proteome by post-translational modifications (PTM) emerges as a major contributing factor to the functional diversity in biology regulating cellular processes. Because PTM are key to the physiologic functions of the proteins involved, it is imperative that we understand the << coding >> that these modifications impart to regulate diverse activities. As estrogen signalling mediates a plethora of PTM not only on the receptors themselves but also on their coregulators, we investigate to << crack >> the ER code. Besides the long-known phosphorylation, other covalent additions such as acetylation, ubiquitination, sumoylation and methylation have been described for estrogen receptors in recent years. These modifications affect receptor stability and activity, and provide potential mechanisms for cell- or-gene-specific regulation. A better understanding of the impact of these PTMs on estrogen receptor should help in the identification of new drugs for breast cancer treatments.
MeSH term(s)	Breast Neoplasms/enzymology ; Breast Neoplasms/metabolism ; Enzyme Activation ; Estrogen Receptor alpha/genetics ; Estrogen Receptor alpha/metabolism ; Female ; Histone Acetyltransferases/metabolism ; Humans ; Phosphorylation ; Protein Kinases/metabolism ; Protein Processing, Post-Translational
Chemical Substances	Estrogen Receptor alpha ; Histone Acetyltransferases (EC 2.3.1.48) ; Protein Kinases (EC 2.7.-)
Language	French
Publishing date	2010-06
Publishing country	France
Document type	English Abstract ; Journal Article ; Review
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/2010266-7636
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Article ; Online: Protein arginine methylation in estrogen signaling and estrogen-related cancers.

Teyssier, Catherine / Le Romancer, Muriel / Sentis, Stéphanie / Jalaguier, Stéphan / Corbo, Laura / Cavaillès, Vincent

Trends in endocrinology and metabolism: TEM

2010 Volume 21, Issue 3, Page(s) 181–189

Abstract: Estrogen signaling pathways regulate multiple cellular processes including proliferation and differentiation, and dysregulation of these pathways underlies several human pathologies. Post-translational modifications (PTMs) play an important role in ... ...

Abstract	Estrogen signaling pathways regulate multiple cellular processes including proliferation and differentiation, and dysregulation of these pathways underlies several human pathologies. Post-translational modifications (PTMs) play an important role in estrogen signaling. This review focuses on recent findings pertinent to arginine methylation of non-histone proteins and their implications in estrogen signaling. We describe protein arginine methyltransferases and demethylases, the role of methylarginine proteins in estrogen action and crosstalk with other PTMs such as phosphorylation and lysine methylation. The relationships between various PTMs form a specific code that is likely to play an important role in hormone signaling. In addition, dysregulation of arginine methylation or of enzymes responsible for these modifications could be key events in estrogen-dependent cancers such as breast cancer.
MeSH term(s)	Animals ; Arginine/metabolism ; Breast Neoplasms/metabolism ; Estrogens/metabolism ; Female ; Humans ; Male ; Methylation ; Models, Biological ; Neoplasms/metabolism ; Protein-Arginine N-Methyltransferases/metabolism ; Receptors, Estrogen/metabolism ; Signal Transduction/physiology
Chemical Substances	Estrogens ; Receptors, Estrogen ; Arginine (94ZLA3W45F) ; Protein-Arginine N-Methyltransferases (EC 2.1.1.319)
Language	English
Publishing date	2010-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1042384-9
ISSN	1879-3061 ; 1043-2760
ISSN (online)	1879-3061
ISSN	1043-2760
DOI	10.1016/j.tem.2009.11.002
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Article ; Online: Transcriptional repression of estrogen receptor α signaling by SENP2 in breast cancer cells.

Nait Achour, Thiziri / Sentis, Stéphanie / Teyssier, Catherine / Philippat, Amandine / Lucas, Annick / Corbo, Laura / Cavaillès, Vincent / Jalaguier, Stéphan

Molecular endocrinology (Baltimore, Md.)

2013 Volume 28, Issue 2, Page(s) 183–196

Abstract: Estrogen receptors (ERs) are ligand-activated transcription factors involved in many physiological and pathological processes, including breast cancer. Their activity is fine-tuned by posttranslational modifications, notably sumoylation. In the present ... ...

Abstract	Estrogen receptors (ERs) are ligand-activated transcription factors involved in many physiological and pathological processes, including breast cancer. Their activity is fine-tuned by posttranslational modifications, notably sumoylation. In the present study, we investigated the role of the small ubiquitin-related modifier (SUMO) protease, SUMO1/sentrin/suppressor of Mif 2-specific peptidase 2 (SENP2), in the regulation of ERα activity. We first found SENP2 to significantly repress estradiol-induced transcriptional activity in breast cancer cells (MCF7 and T47D). This effect was observed with a reporter plasmid and on endogenous genes such as TFF1 and CTSD, which were shown to recruit SENP2 in chromatin immunoprecipitation experiments. Using glutathione S-transferase pull-down, coimmunoprecipitation and proximity ligation assays, SENP2 was found to interact with ERα and this interaction to be mediated by the amino-terminal region of the protease and the hinge region of the receptor. Interestingly, we demonstrated that ERα repression by SENP2 is independent of its SUMO protease activity and requires a transcriptional repressive domain located in the amino-terminal end of the protease. Using small interfering RNA assays, we evidenced that this domain recruits the histone deacetylase 3 (HDAC3), to be fully active. Furthermore, using both overexpression and knockdown strategies, we showed that SENP2 robustly represses estrogen-dependent and independent proliferation of MCF7 cells. We provided evidence that this effect requires both the proteolytic and transcriptional activities of SENP2. Altogether, our study unravels a new property for a SUMO protease and identifies SENP2 as a classical transcription coregulator.
MeSH term(s)	Breast Neoplasms ; Cell Proliferation ; Cysteine Endopeptidases/physiology ; Estradiol/physiology ; Estrogen Receptor alpha/physiology ; Female ; Gene Expression Regulation, Neoplastic ; Gene Silencing ; Histone Deacetylases/metabolism ; Humans ; MCF-7 Cells ; Promoter Regions, Genetic ; Protein Binding ; Protein Structure, Tertiary ; Transcription, Genetic
Chemical Substances	ESR1 protein, human ; Estrogen Receptor alpha ; Estradiol (4TI98Z838E) ; Cysteine Endopeptidases (EC 3.4.22.-) ; SENP2 protein, human (EC 3.4.22.-) ; Histone Deacetylases (EC 3.5.1.98) ; histone deacetylase 3 (EC 3.5.1.98)
Language	English
Publishing date	2013-01-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	639167-9
ISSN	1944-9917 ; 0888-8809
ISSN (online)	1944-9917
ISSN	0888-8809
DOI	10.1210/me.2013-1376
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Article ; Online: hCAF1/CNOT7 regulates interferon signalling by targeting STAT1.

Chapat, Clément / Kolytcheff, Chloé / Le Romancer, Muriel / Auboeuf, Didier / De La Grange, Pierre / Chettab, Kamel / Sentis, Stéphanie / Corbo, Laura

The EMBO journal

2013 Volume 32, Issue 5, Page(s) 688–700

Abstract: Stringent regulation of the interferon (IFN) signalling pathway is essential for maintaining the immune response to pathogens and tumours. The transcription factor STAT1 is a crucial mediator of this response. Here, we show that hCAF1/CNOT7 regulates ... ...

Abstract	Stringent regulation of the interferon (IFN) signalling pathway is essential for maintaining the immune response to pathogens and tumours. The transcription factor STAT1 is a crucial mediator of this response. Here, we show that hCAF1/CNOT7 regulates class I and II IFN pathways at different crucial steps. In resting cells, hCAF1 can control STAT1 trafficking by interacting with the latent form of STAT1 in the cytoplasm. IFN treatment induces STAT1 release, suggesting that hCAF1 may shield cytoplasmic STAT1 from undesirable stimulation. Consistently, hCAF1 silencing enhances STAT1 basal promoter occupancy associated with increased expression of a subset of STAT1-regulated genes. Consequently, hCAF1 knockdown cells exhibit an increased protection against viral infection and reduced viral replication. Furthermore, hCAF1 participates in the extinction of the IFN signal, through its deadenylase activity, by speeding up the degradation of some STAT1-regulated mRNAs. Since abnormal and unbalanced JAK/STAT activation is associated with immune disorders and cancer, hCAF1 could play a major role in innate immunity and oncogenesis, contributing to tumour escape.
MeSH term(s)	Apoptosis/drug effects ; Biomarkers, Tumor/genetics ; Biomarkers, Tumor/metabolism ; Blotting, Western ; Breast Neoplasms/genetics ; Breast Neoplasms/metabolism ; Breast Neoplasms/pathology ; Cell Proliferation/drug effects ; Chromatin Immunoprecipitation ; Cytoplasm/drug effects ; Cytoplasm/metabolism ; Exoribonucleases ; Female ; Fluorescent Antibody Technique ; Gene Expression Profiling ; Gene Expression Regulation, Neoplastic ; Humans ; Immunity, Innate ; Immunoprecipitation ; Interferons/pharmacology ; MicroRNAs/genetics ; Oligonucleotide Array Sequence Analysis ; Phosphorylation ; Promoter Regions, Genetic/genetics ; RNA, Messenger/genetics ; RNA, Small Interfering/genetics ; Real-Time Polymerase Chain Reaction ; Repressor Proteins ; Reverse Transcriptase Polymerase Chain Reaction ; STAT1 Transcription Factor/antagonists & inhibitors ; STAT1 Transcription Factor/genetics ; STAT1 Transcription Factor/metabolism ; Signal Transduction/drug effects ; Transcription Factors/antagonists & inhibitors ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Virus Replication/drug effects
Chemical Substances	Biomarkers, Tumor ; CNOT8 protein, human ; MicroRNAs ; RNA, Messenger ; RNA, Small Interfering ; Repressor Proteins ; STAT1 Transcription Factor ; STAT1 protein, human ; Transcription Factors ; Interferons (9008-11-1) ; CNOT7 protein, human (EC 3.1.-) ; Exoribonucleases (EC 3.1.-)
Language	English
Publishing date	2013-02-05
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.1038/emboj.2013.11
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Article ; Online: Schwann cells support oncogenic potential of pancreatic cancer cells through TGFβ signaling.

Cassier, Philippe A / Tomasini, Richard / Sentis, Stéphanie / Bartholin, Laurent

Cell death & disease

2019 Volume 10, Issue 12, Page(s) 886

Abstract: Pancreatic ductal adenocarcinoma (PDAC) is one of the solid tumors with the poorest prognosis. The stroma of this tumor is abundant and composed of extracellular matrix and stromal cells (including cancer-associated fibroblasts and immune cells). Nerve ... ...

Abstract	Pancreatic ductal adenocarcinoma (PDAC) is one of the solid tumors with the poorest prognosis. The stroma of this tumor is abundant and composed of extracellular matrix and stromal cells (including cancer-associated fibroblasts and immune cells). Nerve fibers invading this stroma represent a hallmark of PDAC, involved in neural remodeling, which participates in neuropathic pain, cancer cell dissemination and tumor relapse after surgery. Pancreatic cancer-associated neural remodeling is regulated through functional interplays mediated by physical and molecular interactions between cancer cells, nerve cells and surrounding Schwann cells, and other stromal cells. In the present study, we show that Schwann cells (glial cells supporting peripheral neurons) can enhance aggressiveness (migration, invasion, tumorigenicity) of pancreatic cancer cells in a transforming growth factor beta (TGFβ)-dependent manner. Indeed, we reveal that conditioned medium from Schwann cells contains high amounts of TGFβ able to activate the TGFβ-SMAD signaling pathway in cancer cells. We also observed in human PDAC samples that high levels of TGFβ signaling activation were positively correlated with perineural invasion. Secretome analyses by mass spectrometry of Schwann cells and pancreatic cancer cells cultured alone or in combination highlighted the central role of TGFβ in neuro-epithelial interactions, as illustrated by proteomic signatures related to cell adhesion and motility. Altogether, these results demonstrate that Schwann cells are a meaningful source of TGFβ in PDAC, which plays a crucial role in the acquisition of aggressive properties by pancreatic cancer cells.
Language	English
Publishing date	2019-11-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2541626-1
ISSN	2041-4889 ; 2041-4889
ISSN (online)	2041-4889
ISSN	2041-4889
DOI	10.1038/s41419-019-2116-x
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