Myriam Polette

ORCID: 0000-0001-8173-3246
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About
Contact & Profiles
Research Areas
  • Protease and Inhibitor Mechanisms
  • Cancer Cells and Metastasis
  • Peptidase Inhibition and Analysis
  • Neonatal Respiratory Health Research
  • Cell Adhesion Molecules Research
  • Wnt/β-catenin signaling in development and cancer
  • Blood Coagulation and Thrombosis Mechanisms
  • Cancer-related gene regulation
  • Nicotinic Acetylcholine Receptors Study
  • S100 Proteins and Annexins
  • Asthma and respiratory diseases
  • Cystic Fibrosis Research Advances
  • Tracheal and airway disorders
  • Chronic Obstructive Pulmonary Disease (COPD) Research
  • Cervical Cancer and HPV Research
  • Genetic and Kidney Cyst Diseases
  • Cancer Genomics and Diagnostics
  • Bone and Dental Protein Studies
  • Fibroblast Growth Factor Research
  • Signaling Pathways in Disease
  • Barrier Structure and Function Studies
  • RNA modifications and cancer
  • Epigenetics and DNA Methylation
  • Hedgehog Signaling Pathway Studies
  • Genetics and Neurodevelopmental Disorders

Université de Reims Champagne-Ardenne
2016-2025

Inserm
2016-2025

Centre Hospitalier Universitaire de Reims
2016-2025

Hôpital Maison Blanche
2010-2024

Pathologies Pulmonaires et Plasticité Cellulaire
2019-2024

Hôpital Robert-Debré
2019-2022

University of Liège
1996-2016

Centre National de la Recherche Scientifique
2014

Institute of Molecular and Cell Biology
2011

Laboratoire Excell
1999-2011

ABSTRACT Vimentin expression in human mammary epithelial MCF10A cells was examined as a function of their migratory status using an vitro wound-healing model. Analysis the trajectories and speeds by time lapse-video microscopy revealed that vimentin mRNA protein were exclusively induced at wound’s edge which actively migrating towards center lesion. Actin labeling showed reorganization actin filaments confirmed phenotype this cell subpopulation. Moreover, disappeared when became stationary...

10.1242/jcs.112.24.4615 article EN Journal of Cell Science 1999-12-15

The cytoplasmic and nuclear redistribution of β-catenin the de novo expression vimentin are frequently involved in epithelial-to-mesenchymal transition associated with increased invasive/migratory properties epithelial cells. Because can act as a coactivator transcription through its binding to T-cell factor (TCF)/lymphoid enhancer 1 family, we have explored possibility that β-catenin/TCF could directly transactivate vimentin. We first compared relation localization eight breast cancer cell...

10.1136/ijgc-00009577-200303001-00219 article EN cc-by-nc-nd International Journal of Gynecological Cancer 2003-03-01

Cell spreading and migration associated with the expression of 92-kD gelatinase (matrix metalloproteinase 9 or MMP-9) are important mechanisms involved in repair respiratory epithelium. We investigated location MMP-9 its potential role migrating human bronchial epithelial cells (HBEC). In vivo vitro, accumulated HBEC located at leading edge a wound paralleled cell speed. through an actin-dependent pathway advancing lamellipodia was subsequently found active extracellular matrix (ECM)....

10.1083/jcb.146.2.517 article EN The Journal of Cell Biology 1999-07-26

In chronic obstructive pulmonary disease (COPD), epithelial changes and subepithelial fibrosis are salient features in conducting airways. Epithelial-to-mesenchymal transition (EMT) has been recently suggested COPD, but the mechanisms relationship to peribronchial remain unclear. We hypothesised that de-differentiation of COPD respiratory epithelium through EMT could participate airway thereby, obstruction. Surgical lung tissue primary broncho-epithelial cultures (in air-liquid interface...

10.1183/09031936.00135814 article EN European Respiratory Journal 2015-03-05

Epithelial-mesenchymal transition (EMT) is prominent in circulating tumor cells (CTC), but how it influences metastatic spread this setting obscure. Insofar as blood provides a specific microenvironment for cells, we explored potential link between EMT and coagulation that may provide EMT-positive CTCs with enhanced colonizing properties. Here report induces tissue factor (TF), major cell-associated initiator of related procoagulant properties the blood. TF blockade by antibody or shRNA...

10.1158/0008-5472.can-15-2263 article EN Cancer Research 2016-05-25

MMP-2 (gelatinase A) has been associated with the invasive potential of many cancer cells both in vitro and vivo. It is now becoming clear that activation this enzyme might be a key step tumor invasion. This process shown to membrane-associated pathway inducible by various agents such as collagen type I, concanavalin A or TGF-beta, but its physiological regulation still largely unresolved. MT-MMP was recently discovered described gelatinase-A activator. In present study, we investigated...

10.1002/(sici)1097-0215(19960117)65:2<209::aid-ijc14>3.0.co;2-8 article EN International Journal of Cancer 1996-01-17

The expression of various matrix metalloproteinases (MMPs) and their tissue inhibitors (TIMPs) in 88 primary bronchopulmonary cancers 13 neighbouring pulmonary parenchyma samples was quantified by Northern-blot analysis, morphologically examined situ hybridization immunohistochemistry order to evaluate the involvement MMPs pathophysiology these carcinomas look for potential markers aggressivity lung tumours. analysis showed that predominantly expressed were gelatinase A (66%), its activator...

10.1002/(sici)1097-0215(19970807)72:4<556::aid-ijc2>3.0.co;2-p article EN International Journal of Cancer 1997-08-07

Tumor cell-derived collagenase stimulatory factor (TCSF) stimulates in vitro the biosynthesis of various matrix metalloproteinases involved tumor invasion, such as interstitial collagenase, gelatinase A, and stromelysin 1. The expression TCSF mRNAs was studied vivo, using situ hybridization Northern blotting analysis, seven normal tissues 22 squamous cell carcinomas lung, benign proliferations ductal mammary gland. By hybridization, were detected 40 44 carcinomas, pre-invasive invasive...

10.1177/002215549704500508 article EN Journal of Histochemistry & Cytochemistry 1997-05-01

Vimentin is an intermediate filament protein normally expressed in mesenchymal cells, but evidence accumulating the literature which suggests that aberrant expression of vimentin epithelial cancer cells might be related to local invasiveness and metastatic potential. has previously been associated with invasive properties vitro model consisting a set HPV-33-transformed cervical keratinocyte cell lines. In present study, order emphasize those findings, investigated neoplasms different grades,...

10.1002/(sici)1096-9896(199610)180:2<175::aid-path630>3.0.co;2-g article EN The Journal of Pathology 1996-10-01

Chronic rhinosinusitis (CRS) defines a group of disorders characterized by persistent inflammation the sinonasal tract. Epithelial changes and structural remodelling are present, but whether epithelial differentiation is altered remains uncertain.To evaluate state epithelium in CRS, biopsies from patients with CRS nasal polyps (CRSwNP) or without (CRSsNP), allergic rhinitis (AR), as compared to controls, were processed immunohistochemistry RT-qPCR for terminal (E-cadherin, high molecular...

10.1111/all.12503 article EN Allergy 2014-08-07

Abstract Loss of E‐cadherin/catenin mediated cell–cell adhesion and overexpression matrix metalloproteinases (MMPs) are largely involved in tumor invasion. It has been recently shown that high levels a soluble 80 kDa fragment E‐cadherin, resulting from cleavage by MMPs, found serum urine cancer patients. Additionally, this E‐cadherin (sE‐CAD) promotes cell invasion into chick heart collagen type I gels. The aim our study was to examine the mechanism sE‐CAD‐induced Since MMPs play crucial...

10.1002/ijc.11168 article EN International Journal of Cancer 2003-05-15

Tumor cells interact with stromal via soluble or cell-bound factors stimulating the production of matrix metalloproteinases (MMPs), a group enzymes largely involved in extracellular (ECM) remodeling tumor invasion. Among these factors, metalloproteinase inducer (EMMPRIN) has been shown to stimulate vitro fibroblast various MMPs such as interstitial collagenase (MMP-1), stromelysin-1 (MMP-3), and gelatinase A (MMP-2). In this study, EMMPRIN protein was detected by immunohistochemistry...

10.1177/002215549904701209 article EN Journal of Histochemistry & Cytochemistry 1999-12-01
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