University Hospital of Reims

University of Technology of Compiègne, France

University Hospital of Reims

University of Technology of Compiègne, France

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Serradori T.,University of Lorraine | Germain A.,University of Lorraine | Scherrer M.L.,University of Lorraine | Perez M.,University of Lorraine | And 5 more authors.
British Journal of Surgery | Year: 2013

Background Patients with Crohn's disease are increasingly receiving antitumour necrosis factor α (anti-TNF-α) therapy. Whether anti-TNF-α therapy increases the risk of postoperative infectious complications in Crohn's disease is a matter of debate. Methods This was a retrospective study of three referral centres. The charts of patients who underwent ileocaecal or ileocolonic resection for Crohn's disease between 2000 and 2011 were reviewed. The impact of baseline characteristics and Crohn's disease-related medications on the risk of postoperative intra-abdominal infectious complications was investigated by univariable and multivariable analysis. Results A total of 217 patients were included in the study. Median age at the time of surgery was 36·8 (range 15-78) years. A postoperative intra-abdominal infection occurred in 24 (11·1 per cent) of 217 patients. No deaths were reported. On univariable analysis, age less than 25 years (P = 0·023), steroid use (P = 0·017), anti-TNF-α therapy (P = 0·043) and anti-TNF-α treatment in combination with steroids (P = 0·004) were associated with an increased risk of postoperative intra-abdominal infectious complications. On multivariable analysis, only anti-TNF-α therapy in combination with steroids significantly increased this risk (odds ratio 8·03, 95 per cent confidence interval 1·93 to 33·43; P = 0·035). Conclusion Combined use of steroids and anti-TNF-α therapy was associated with an increased risk of postoperative intra-abdominal infectious complications. Steroids and biologics increase risk © 2013 British Journal of Surgery Society Ltd. Published by John Wiley & Sons, Ltd.


Jaisson S.,University Hospital of Reims | Jaisson S.,University of Sfax | Pietrement C.,University Hospital of Reims | Pietrement C.,University of Sfax | And 2 more authors.
Clinical Chemistry | Year: 2011

BACKGROUND: Carbamylation is a posttranslational modification of proteins resulting from the nonenzymatic reaction between isocyanic acid and specific free functional groups. This reaction alters protein structural and functional properties and thus contributes to molecular ageing. Many studies have shown the involvement of carbamylated proteins in diseases, especially in chronic renal failure and atherosclerosis. CONTENT: In this review we describe the biochemical basis of the carbamylation process and its role in protein molecular ageing. We summarize the current evidence of protein carbamylation involvement in disease, identify available biomarkers of the carbamylation process and their related analytical methods, and discuss the practical relevance of these biomarkers. SUMMARY: Carbamylation-induced protein alterations are involved in the progression of various diseases, because carbamylation-derived products (CDPs) are bioactive compounds that trigger specific and inappropriate cellular responses. For instance, carbamylation may promote hormone and enzyme inactivation, and carbamylated proteins, as diverse as collagen or LDLs, induce characteristic biochemical events of atherosclerosis progression. CDPs are potential biomarkers to monitor diseases characterized by an increased rate of carbamylation (e.g., chronic renal failure and atherosclerosis). Different methods (e.g., liquid chromatography-tandem mass spectrometry and immunoassays) to measure specific carbamylated proteins or general markers of carbamylation, such as protein-bound homocitrulline, have been described. Their use in clinical practice must still be validated by appropriate clinical studies. © 2011 American Association for Clinical Chemistry.


Deslee G.,University Hospital of Reims | Klooster K.,University of Groningen | Hetzel M.,Krankenhaus Vom Roten Kreuz | Stanzel F.,Lungenklinik | And 9 more authors.
Thorax | Year: 2014

Background: The lung volume reduction (LVR) coil is a minimally invasive bronchoscopic nitinol device designed to reduce hyperinflation and improve elastic recoil in severe emphysema. We investigated the feasibility, safety and efficacy of LVR coil treatment in a prospective multicentre cohort trial in patients with severe emphysema. Methods: Patients were treated in 11 centres. Safety was evaluated by recording all adverse events, efficacy by the St George's Respiratory Questionnaire (SGRQ) as primary endpoint, and pulmonary function testing, modified Medical Research Council dyspnoea score (mMRC) and 6-min walk distance (6MWD) up to 12 months after the final treatment. Results: Sixty patients (60.9 ± 7.5 years, forced expiratory volume in 1 s (FEV1) 30.2 ± 6.3% pred) were bronchoscopically treated with coils (55 bilateral, 5 unilateral), with a median of 10 (range 5-15) coils per lobe. Within 30 days post-treatment, seven chronic obstructive pulmonary disease exacerbations (6.1%), six pneumonias (5.2%), four pneumothoraces (3.5%) and one haemoptysis (0.9%) occurred as serious adverse events. At 6 and 12 months, respectively, ΔSGRQ was -12.1±12.9 and -11.1±13.3 points, Δ6MWD was +29.7±74.1 m and +51.4±76 m, ΔFEV1was +0.11 ±0.20 L and +0.11±0.30 L, and ΔRV (residual volume) was -0.65±0.90 L and -0.71±0.81 L (all p<0.01). Post hoc analyses showed significant responses for SGRQ, 6MWD and RV in patients with both heterogeneous and homogeneous emphysema. Conclusions: LVR coil treatment results in significant clinical improvements in patients with severe emphysema, with a good safety profile and sustained results for up to 1 year. Trial registration number: NCT01328899. © 2014, BMJ Publishing Group. All rights reserved.


Fauvet R.,University of Picardie Jules Verne | Brzakowski M.,University of Picardie Jules Verne | Morice P.,University Paris - Sud | Resch B.,University of Rouen | And 3 more authors.
Annals of Oncology | Year: 2012

Background: The purpose of the current study was to evaluate the characteristics of borderline ovarian tumors (BOTs) diagnosed during pregnancy. Patients and methods: We conducted a retrospective multicenter study of 40 patients with BOTs diagnosed during pregnancy between 1997 and 2009 at five tertiary universitary departments of Gynecology and Obstetrics and one French cancer center. The medical records were reviewed to determine surgical procedure, histology, restaging surgery and recurrence. Results: Mean patient age was 30.2 ± 5.4 years. Most BOTs were diagnosed during the first trimester of pregnancy (62%). Salpingo-oophorectomy (N = 24) was more frequently performed than cystectomy (N = 11) during pregnancy (P = 0.01). Only two patients had an initial complete staging. BOTs were mucinous, serous and mixed in 48%, 42% and 10% of patients, respectively. Twenty-one percent of mucinous BOTs exhibited intraepithelial carcinoma or microinvasion. Forty-seven percent of serous BOTs exhibited micropapillary features, noninvasive implants or microinvasion. Restaging surgery performed in 52% patients resulted in upstaging in 24% of cases. Recurrence rate in patients with serous BOT with micropapillary features or peritoneal implants was 7.5%. Conclusions: BOTsdiagnosedduringpregnancy exhibit a highincidence of aggressive featuresand are rarely completely staged initially. Given this setting, up-front salpingo-oophorectomy should be considered and restaging planned. © The Author 2011. Published by Oxford University Press on behalf of the European Society for Medical Oncology. All rights reserved.


Gillery P.,University Hospital of Reims | Gillery P.,French National Center for Scientific Research | Jaisson S.,University Hospital of Reims | Jaisson S.,French National Center for Scientific Research
Journal of Proteomics | Year: 2013

Molecular aging of proteins results from the complex association of different reactions that lead to the progressive alteration of their structural and functional properties. These reactions, which include oxidation, glycoxidation, carbonylation and carbamylation, occur during aging and are amplified in various chronic diseases such as diabetes or chronic renal failure. Specific compounds generated throughout this process called post-translational modification derived products (PTMDPs) have been suggested to be promising biomarkers for the management of chronic diseases. During the last decades, the emergence of mass spectrometry and proteomics has largely contributed to the development of sensitive and specific analytical methods devoted to PTMDP quantification in biological fluids. This review aimed at providing evidences for the clinical relevance of PTMDPs as biomarkers in chronic diseases, and at emphasizing on the contribution of mass spectrometric and proteomic methods in this field. Different issues that should be addressed in order to ensure the implementation of these biomarkers in clinical practice have been highlighted.This article is part of a Special Issue entitled: Posttranslational Protein modifications in biology and Medicine. © 2013 Elsevier B.V.


Gillery P.,University Hospital of Reims
Journal of Medical Biochemistry | Year: 2011

During their biological life, proteins are exposed in a cumulative way to irreversible nonenzymatic post-translational modifications that are responsible for their molecular aging and generate specific by-products called post-translational modification derived products (PTMDPs). PTMDPs are involved in the pathogenesis of various diseases such as diabetes mellitus, renal insufficiency and atherosclerosis, and are potential biomarkers in clinical practice. Nonenzymatic glycation refers to the spontaneous binding of glucose and reducing sugars to free amino groups and is amplified by oxidative processes (referred to as «glycoxidation»). It generates many reactive by-products such as aldehydes and leads to the formation of «advanced glycation end products» (AGEs). AGEs accumulate in vivo, alter tissue organization and activate membrane receptors such as RAGE, which triggers inflammatory responses. Carbamylation is due to the binding of isocyanic acid, formed in vivo either by spontaneous dissociation of urea or by action of myeloperoxidase on thiocyanate, and generates homocitrulline from lysine groups. Carbamylation leads to alteration of the structural and biological properties of proteins, and favors inflammation and atherosclerosis. PTMDPs may be assayed by different methods, among others LC-MS/MS or immuno assays, constitute a promising field of investigation in basic research and are potential major biomarkers in laboratory medicine.


Jaisson S.,University Hospital of Reims | Desmons A.,University Hospital of Reims | Renard B.,University Hospital of Reims | Chevelle B.,University Hospital of Reims | And 2 more authors.
Clinica Chimica Acta | Year: 2014

Background: HbA1c is considered the gold standard for the follow-up of diabetic patients and a new diagnostic tool for diabetes mellitus, which implies the availability of reliable assay methods. We have evaluated a new assay developed by Abbott Laboratories, based on the enzymatic quantification of HbA1c by a fructosyl dipeptide oxidase using Architect analyzers. Methods: Precision, linearity, correlation with a HPLC method, accuracy and potential impact interferences on HbA1c measurement have been evaluated. Results: Intra-day and between-day CVs were lower than 1.2% and linearity was excellent from 19mmol/mol (3.9%) to 163mmol/mol (17.1%). The results were well correlated with those obtained by the HPLC (Variant II device, kit NU - BioRad): HbA1c [Architect, mmol/mol]=0.986×HbA1c [Variant II, mmol/mol]+0.713 (r=0.998, n=109). This method provided consistent results with IFCC titrated quality control samples. Classical interferences in HbA1c assays (i.e. labile HbA1c, carbamylated hemoglobin, triglycerides or bilirubin) did not have an impact on HbA1c quantification by this method. Conclusion: This new enzymatic assay proved to be a robust and reliable method for HbA1c measurement suitable for routine practice in clinical chemistry laboratories. © 2014 Elsevier B.V.


Jaisson S.,University Hospital of Reims | Gillery P.,University Hospital of Reims
Clinical Chemistry | Year: 2010

BACKGROUND: During their biological life, proteins are exposed in a cumulative fashion to irreversible nonenzymatic, late posttranslational modifications that are responsible for their molecular aging. It is now well established that these damaged proteins constitute a molecular substratum for many dysfunctions described in metabolic and age-related diseases, such as diabetes mellitus, renal insufficiency, atherosclerosis, or neurodegenerative diseases. Accordingly, the specific end products derived from these reactions are considered potentially useful biomarkers for these diseases. CONTENT: The aim of this review is to give an overview of nonenzymatic posttranslational modifications of proteins and their influence in vivo, take inventory of the analytical methods available for the measurement of posttranslational modification-derived products, and assess the potential contribution of new technologies for their clinical use as biological markers of protein molecular aging. SUMMARY: Despite their clinical relevance, biomarkers of posttranslational modifications of proteins have been studied only in the context of experimental clinical research, owing to the analytical complexity of their measurement. The recent implementation in clinical chemistry laboratories of mass spectrometry-based methods that provide higher specificity and sensitivity has facilitated the measurement of these compounds. These markers are not used currently by clinicians in routine practice, however, and many challenges, such as standardization, have to be confronted before these markers can be used as efficient tools in the detection and monitoring of long-term complications of metabolic and age-related diseases. © 2010 American Association for Clinical Chemistry.


Jaisson S.,University of Reims Champagne Ardenne | Jaisson S.,Matrix | Jaisson S.,University Hospital of Reims | Gillery P.,University of Reims Champagne Ardenne | And 2 more authors.
Diabetologia | Year: 2014

In living organisms, proteins are regularly exposed to 'molecular ageing', which corresponds to a set of non-enzymatic modifications that progressively cause irreversible damage to proteins. This phenomenon is greatly amplified under pathological conditions, such as diabetes mellitus. For their survival and optimal functioning, cells have to maintain protein homeostasis, also called 'proteostasis'. This process acts to maintain a high proportion of functional and undamaged proteins. Different mechanisms are involved in proteostasis, among them degradation systems (the main intracellular proteolytic systems being proteasome and lysosomes), folding systems (including molecular chaperones), and enzymatic mechanisms of protein repair. There is growing evidence that the disruption of proteostasis may constitute a determining event in pathophysiology. The aim of this review is to demonstrate how such a dysregulation may be involved in the pathogenesis of diabetes mellitus and in the onset of its long-term complications. © 2014 Springer-Verlag.


Gillery P.,Reims University Hospital Center | Gillery P.,University Hospital of Reims | Gillery P.,University of Reims Champagne Ardenne | Jaisson S.,University Hospital of Reims | Jaisson S.,University of Reims Champagne Ardenne
Clinical Chemistry and Laboratory Medicine | Year: 2014

In living organisms, proteins are progressively modified by spontaneous non-enzymatic reactions generating many post-translational modification derived products (PTMDPs) which exert deleterious effects and may be considered endogenous toxins in diabetes mellitus and chronic renal failure. Non-enzymatic glycation, which refers to the spontaneous binding of reducing sugars to free amino groups, is increased in diabetes mellitus because of hyperglycemia and is amplified by oxidative processes ('glycoxidation'). Glycoxidation leads to the formation of 'advanced glycation end products' (AGEs), together with products of other oxidative pathways. AGEs alter tissue organization and cell-protein interactions, mainly in the case of long-lived extracellular matrix proteins, and interact with membrane receptors, among which RAGE (receptor of AGEs), a multiligand receptor which triggers intracellular signaling pathways stimulating inflammatory functions. Another major protein modification, carbamylation, is increased in chronic renal failure, which may occur during the course of diabetes mellitus. Carbamylation is due to the binding of isocyanic acid on the α-NH2 extremity of proteins or amino acids, or on ε-NH2 lysine groups, generating homocitrulline, a potential biomarker in atherosclerosis. Isocyanic acid is formed in vivo either by spontaneous dissociation of urea or by myeloperoxidase action on thiocyanate. Carbamylated proteins exhibit altered properties. For example, carbamylated collagen is unable to stimulate oxidative functions of polymorphonuclear neutrophils but increases matrix metalloproteinase-9 production by monocytes. Lipoprotein functions are altered by carbamylation and may contribute to atherogenesis. Thus, the numerous PTMDPs may be considered both hallmarks of protein damage in chronic diseases and endogenous toxins acting at the molecular and cellular levels. © 2014 by Walter de Gruyter Berlin Boston.

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