Entity

Time filter

Source Type


Gautier N.,Center Regional Of Lutte Contre Le Cancer Eugene Marquis | Lalonde L.,Center Hospitalier Of Luniversite Of Montreal Chum | Tran-Thanh D.,Center Hospitalier Of Luniversite Of Montreal Chum | Khoury M.E.,Center Hospitalier Of Luniversite Of Montreal Chum | And 4 more authors.
European Journal of Radiology | Year: 2013

Purpose: The aim of this study is to describe the clinical and radiological presentation of chronic granulomatous mastitis. Material and methods: We retrospectively reviewed the clinical and radiological data of 11 women with histologically proven chronic granulomatous mastitis (CGM) diagnosed between March 2008 and September 2011. Results: The diagnosis of CGM is often a challenging one that can mimic infectious and malignant breast conditions. Clinically, CGM most commonly presents as a mass, occasionally with associated erythema. The most frequent mammographic presentation is an asymmetric density, while ultrasound most commonly reveals a hypoechoic mass with tubular extensions and a striated echotexture. On MRI, the most specific finding is peripherally enhancing fluid or solid masses with fistulous tract to the skin, although the latter is not commonly encountered. Diagnosis can be reliably obtained by needle core or vacuum-assisted biopsy, and is established pathologically by the identification of granulomatous inflammation without caseous necrosis. CGM is a diagnosis of exclusion after infectious and foreign body causes are ruled out. Treatment options include oral steroids or surgery; both options are associated with similar recurrence rates. The disease tends to burn itself out and the option of conservative management with observation is a valid one. Conclusion: CGM is a rare benign disease with no specific features clinically or at imaging. There are no radiologic findings that are specific of CGM, but in the appropriate clinical setting, the diagnosis can be suggested by the radiologist. © 2012 Elsevier Ireland Ltd. All rights reserved. Source


Hetz C.,University of Chile | Hetz C.,Harvard University | Chevet E.,University of Rennes 1 | Chevet E.,Center Regional Of Lutte Contre Le Cancer Eugene Marquis | Oakes S.A.,University of California at San Francisco
Nature Cell Biology | Year: 2015

Stress induced by accumulation of misfolded proteins in the endoplasmic reticulum is observed in many physiological and pathological conditions. To cope with endoplasmic reticulum stress, cells activate the unfolded protein response, a dynamic signalling network that orchestrates the recovery of homeostasis or triggers apoptosis, depending on the level of damage. Here we provide an overview of recent insights into the mechanisms that cells employ to maintain proteostasis and how the unfolded protein response determines cell fate under endoplasmic reticulum stress. © 2015 Macmillan Publishers Limited. Source


Revest M.,Rennes University Hospital Center | Revest M.,University of Rennes 1 | Patrat-Delon S.,Rennes University Hospital Center | Devillers A.,Center Regional Of Lutte Contre Le Cancer Eugene Marquis | And 4 more authors.
Medecine et Maladies Infectieuses | Year: 2014

The diagnosis of some infectious diseases is sometimes difficult to make and new diagnostic tools have been regularly assessed to that end. 18fluoro-deoxyglucose (18FDG) positron-emission tomography (PET) coupled with computed tomography (CT) is one of these new procedures. It has been evaluated for numerous infectious diseases with uneven results. A literature review allowed drawing some conclusions. First, 18FDG-PET/CT is not currently a first-line procedure for infectious diseases. Second, it has proved useful for the evaluation of patients presenting with fever of unknown origin (FUO). Its negative predictive value is 100%: the symptoms of patients experiencing FUO with negative first-line investigations and a negative 18FDG-PET/CT will almost always spontaneously disappear. Third, 18FDG-PET/CT also seems to be contributive for the diagnosis of vascular prosthesis infections or osteomyelitis. Fourth, it has promising results for patients presenting with infective endocarditis, especially for secondary infectious foci, or for patients presenting with suspected infection of pacemakers or implanted defibrillator; but results are still preliminary and must be confirmed. Finally18FDG-PET/CT cannot be recommended yet for other infectious diseases due to lack of published data. © 2014 Elsevier Masson SAS. Source


Manie S.N.,University of Lyon | Lebeau J.,University of Lyon | Chevet E.,French Institute of Health and Medical Research | Chevet E.,Center Regional Of Lutte Contre Le Cancer Eugene Marquis
American Journal of Physiology - Cell Physiology | Year: 2014

The endoplasmic reticulum (ER)-induced unfolded protein response (UPR) is an adaptive mechanism that is activated upon accumulation of misfolded proteins in the ER and aims at restoring ER homeostasis. In the past 10 years, the UPR has emerged as an important actor in the different phases of tumor growth. The UPR is transduced by three major ER resident stress sensors, which are protein kinase RNA-like ER kinase (PERK), activating transcription factor 6 (ATF6), and inositol-requiring enzyme-1 (IRE1). The signaling pathways elicited by those stress sensors have connections with metabolic pathways and with other plasma membrane receptor signaling networks. As such, the ER has an essential position as a signal integrator in the cell and is instrumental in the different phases of tumor progression. Herein, we describe and discuss the characteristics of an integrated signaling network that might condition the UPR biological outputs in a tissue- or stress-dependent manner. We discuss these issues in the context of the pathophysiological roles of UPR signaling in cancers. © 2014 the American Physiological Society. Source


Maurel M.,VIB | Maurel M.,Ghent University | Chevet E.,University of Bordeaux Segalen | Chevet E.,Center Regional Of Lutte Contre Le Cancer Eugene Marquis | And 4 more authors.
Trends in Biochemical Sciences | Year: 2014

Inositol-requiring enzyme 1 (IRE1) is the most conserved transducer of the unfolded protein response (UPR), a homeostatic response that preserves proteostasis. Intriguingly, via its endoribonuclease activity, IRE1 produces either adaptive or death signals. This occurs through both unconventional splicing of XBP1 mRNA and regulated IRE1-dependent decay of mRNA (RIDD). Whereas XBP1 mRNA splicing is cytoprotective in response to endoplasmic reticulum (ER) stress, RIDD has revealed many unexpected features. For instance, RIDD cleaves RNA at an XBP1-like consensus site but with an activity divergent from XBP1 mRNA splicing and can either preserve ER homeostasis or induce cell death. Here we review recent findings on RIDD and propose a model of how IRE1 RNase activity might control cell fate decisions. © 2014 Elsevier Ltd. Source

Discover hidden collaborations