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A genomic signature for endosporulation includes a gene coding for a protease, YabG, which in the model organism Bacillus subtilis is involved in assembly of the spore coat. We show that in the human pathogen Clostridioidesm difficile, YabG is critical for the assembly of the coat and exosporium layers of spores. YabG is produced during sporulation under the control of the mother cell-specific regulators σE and σK and associates with the spore surface layers. YabG shows an N-terminal SH3-like domain and a C-terminal domain that resembles single domain response regulators, such as CheY, yet is atypical in that the conserved phosphoryl-acceptor residue is absent. Instead, the CheY-like domain carries residues required for activity, including Cys207 and His161, the homologues of which form a catalytic diad in the B. subtilis protein, and also Asp162. The substitution of any of these residues by Ala, eliminates an auto-proteolytic activity as well as interdomain processing of CspBA, a reaction that releases the CspB protease, required for proper spore germination. An in-frame deletion of yabG or an allele coding for an inactive protein, yabGC207A, both cause misassemby of the coat and exosporium and the formation of spores that are more permeable to lysozyme and impaired in germination and host colonization. Furthermore, we show that YabG is required for the expression of at least two σK-dependent genes, cotA, coding for a coat protein, and cdeM, coding for a key determinant of exosporium assembly. Thus, YabG also impinges upon the genetic program of the mother cell possibly by eliminating a transcriptional repressor. Although this activity has not been described for the B. subtilis protein and most of the YabG substrates vary among sporeformers, the general role of the protease in the assembly of the spore surface is likely to be conserved across evolutionary distance.
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Clostridioides difficile , Péptido Hidrolasas , Humanos , Péptido Hidrolasas/metabolismo , Clostridioides difficile/genética , Clostridioides difficile/metabolismo , Clostridioides , Esporas Bacterianas/metabolismo , Factores de Transcripción/metabolismo , Endopeptidasas/metabolismo , Proteínas Bacterianas/metabolismo , Bacillus subtilis/metabolismoRESUMEN
PURPOSE: The aim of this multi-institutional retrospective study was to compare osteoarticular graft reconstruction (OA) and wrist arthrodesis (WA) after distal radius resection for giant cell tumor. MATERIAL AND METHODS: Sixty-seven patients affected by giant cell tumor of the distal radius underwent resection and reconstruction with OA (47 patients) or WA (20 patients). The mean age was 40 years (range, 13-74 years). Grafts included fresh-frozen allograft or nonvascularized fibular autograft. Complications requiring surgical revision were recorded. Clinical outcome was assessed with the Musculoskeletal Tumour Society Score (MSTS) and Disabilities of the Arm, Shoulder, and Hand (DASH) score. RESULTS: Fifteen patients developed a local recurrence after a median of 12 months (range, 6-137 months). Sixteen patients required revision surgery for complications. Of these, 10 were graft-related complications (7 in the OA group and 3 in the WA group). Among OA, 2 patients with painful instabilities and 4 with severe arthritis required conversion into WA after a mean of 26 months (range, 13-38 months) At a median follow-up of 105 months (range, 12-395 months), similar functional outcome (MSTS and DASH score) was observed between OA and WA. CONCLUSIONS: Our results did not show any advantage of OA or WA over the other technique. A patient-by-patient decision should be taken both regarding the type of reconstruction (OA or WA) and the type of graft (allograft or autograft). The reconstructive choice should also consider the patient's functional expectations. TYPE OF STUDY/LEVEL OF EVIDENCE: Therapeutic IV.
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Neoplasias Óseas , Tumor Óseo de Células Gigantes , Adolescente , Adulto , Anciano , Artrodesis , Neoplasias Óseas/cirugía , Trasplante Óseo , Tumor Óseo de Células Gigantes/diagnóstico por imagen , Tumor Óseo de Células Gigantes/cirugía , Humanos , Persona de Mediana Edad , Recurrencia Local de Neoplasia , Radio (Anatomía)/cirugía , Rango del Movimiento Articular , Estudios Retrospectivos , Resultado del Tratamiento , Muñeca , Adulto JovenRESUMEN
During sporulation in Bacillus subtilis, a group of mother cell-specific proteins guides the assembly of the coat, a multiprotein structure that protects the spore and influences many of its environmental interactions. SafA and CotE behave as party hubs, governing assembly of the inner and outer coat layers. Targeting of coat proteins to the developing spore is followed by encasement. Encasement by SafA and CotE requires E, a region of 11 amino acids in the encasement protein SpoVID, with which CotE interacts directly. Here, we identified two single alanine substitutions in E that prevent binding of SafA, but not of CotE, to SpoVID, and block encasement. The substitutions result in the accumulation of SafA, CotE and their dependent proteins at the mother cell proximal spore pole, phenocopying a spoVID null mutant and suggesting that mislocalized SafA acts as an attractor for the rest of the coat. The requirement for E in SafA binding is bypassed by a peptide with the sequence of E provided in trans. We suggest that E allows binding of SafA to a second region in SpoVID, enabling CotE to interact with E and SpoVID to function as a non-competitive hub during spore encasement.
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Bacillus subtilis/metabolismo , Proteínas Bacterianas/metabolismo , Proteínas de la Membrana/metabolismo , Esporas Bacterianas/crecimiento & desarrollo , Sustitución de Aminoácidos/genética , Proteínas Bacterianas/genética , Proteínas de la Membrana/genética , Dominios Proteicos/genéticaRESUMEN
INTRODUCTION: Calcaneal tumors being a rare occurrence, surgical options and outcomes are not well-known. Extensive defects following wide resection, especially in weight-bearing areas, still remain a challenge and different reconstructive techniques have been proposed. The aim of this report was to analyze the clinical and functional long-term outcomes of heel reconstruction using an iliac crest free flap. PATIENTS AND METHODS: Four patients who underwent calcaneal reconstruction between 1999 and 2012 were included. Two were females and mean age was 27 years, ranging 18-42 years. Each patient underwent total calcanectomy, for two osteoblastomas, one osteosarcoma, and one Ewing's sarcoma. An iliac crest flap was harvested and shaped to fit the residual space. After the articular cartilage at recipient site was debrided, the flap was fixed to the talus and the cuboid. RESULTS: The average size of the flaps was 2 x 7 x 5 cm. Postoperatively wound dehiscence, screw breaking, and graft fracture healed conservatively. All the arthrodesis healed successfully and no donor site complication occurred. At an average follow-up of 13 years (range 6-19 years) any patient claimed pain, evident limp or limitation of daily activities. Computerized pedobarographic examination and gait analysis revealed a satisfactory result and an acceptable weight-bearing area in the reconstructed limb in each patient. CONCLUSIONS: Calcaneal reconstruction with iliac crest free flap is likely to provide good chances of a long-lasting result, especially in young patients. Particularly, it provides the possibility to adequately shape the graft to fit the bone loss while using the crest as the weight-bearing surface.
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Neoplasias Óseas/cirugía , Calcáneo/cirugía , Colgajos Tisulares Libres , Ilion/trasplante , Procedimientos Ortopédicos/métodos , Adolescente , Adulto , Femenino , Humanos , Masculino , Estudios Retrospectivos , Resultado del Tratamiento , Adulto JovenRESUMEN
The food enzyme glucan 1,4-α-maltohydrolase (4-α-d-glucan α-maltohydrolase; EC 3.2.1.133) is produced with the genetically modified Saccharomyces cerevisiae strain LALL-MA+ by Danstar Ferment AG. The genetic modifications do not give rise to safety concerns. The food enzyme is free from viable cells of the production organism and its DNA. It is intended to be used in the processing of cereals and other grains for production of baked products. Dietary exposure was estimated to be up to 0.014 mg TOS/kg body weight per day in European populations. Given the QPS status of the production strain and the absence of concerns resulting from the food enzyme manufacturing process, toxicity tests were considered unnecessary by the Panel. A search for the identity of the amino acid sequence of the food enzyme to known allergens was made and four matches were found, three with respiratory allergens and one with an allergen from mosquito (injected). The Panel considered that the risk of allergic reactions upon dietary exposure cannot be excluded, but the likelihood is low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns, under the intended conditions of use.
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The European Union (EU) is committed to transitioning toward a circular economy model, with food waste being one of the areas to be targeted. To close the loop of food waste generated during food processing and discarded at the retail or consumption phases, research and innovation parties proposed to valorize agro-food by-products to produce novel foods and food improvement agents (food additives, food enzymes, and food flavorings). In the EU, the authorization of such novel foods and food improvement agents is governed by different regulatory frameworks. A centralized safety assessment by the European Food Safety Authority (EFSA) is the prerequisite for their authorization through the so-called Union Lists. Up to December 2023, EFSA published 45 scientific opinions on the safety of novel foods, food enzymes, and food additives derived from by-products of plant and animal origin. The current study illustrates examples of these by-products for the production of novel foods or food improvement agents and the data requirements behind their respective safety assessments conducted by EFSA. In this review, applications on novel foods, food enzymes, and food additives received by EFSA were screened and analyzed to find the common scientific requirements and differences in terms of the safety evaluation of such products. Various by-products (i.e., corncobs, coffee husks, spent grains of barley and rice, grape pomace, pumpkin peels, bovine whey, eggshells, shrimp heads, and animal organs or tissues) were described in the applications as being processed (extraction, physical treatments, and chemical and enzymatic reactions) to obtain novel foods and food improvement agents. The heterogeneity and complexity of these products emphasize the challenge of their safety assessment, depending on the characteristics of each product. However, as this study shows, the scientific requirements underpinning their safety do not differ substantially in the different regulated product areas considered, with similar information needed to assess their safety in terms of identity, production process, compositional characterization, proposed/intended uses and exposure assessment, toxicological information, and allergenicity data. Additional nutritional information and data on the history of use are required in the case of novel foods.
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The food enzyme triacylglycerol lipase (triacylglycerol acylhydrolase, EC 3.1.1.3) is produced with the non-genetically modified Mucor circinelloides strain AE-LMH by Amano Enzyme Inc. A safety evaluation of this food enzyme was made previously, in which EFSA concluded that this food enzyme did not give rise to safety concerns when used in three food manufacturing processes. Subsequently, the applicant requested to extend its use to include two additional processes. In this assessment, EFSA updated the safety evaluation of this food enzyme when used in a total of five food manufacturing processes. The dietary exposure to the food enzyme-total organic solids (TOS) was estimated to be up to 0.845 mg TOS/kg body weight (bw) per day in European populations. When combined with the no observed adverse effect level previously reported (784 mg TOS/kg bw per day, the highest dose tested), the Panel derived a margin of exposure of at least 928. Based on the data provided for the previous evaluation and the revised margin of exposure, the Panel concluded that this food enzyme does not give rise to safety concerns under the revised intended conditions of use.
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The food enzyme peroxidase (phenolic donor: hydrogen-peroxide oxidoreductase, EC 1.11.1.7) is produced with the genetically modified Aspergillus niger strain MOX by DSM Food Specialties B.V. A safety evaluation of this food enzyme was made previously, in which EFSA concluded that this food enzyme did not give rise to safety concerns when used in one food manufacturing process. Subsequently, the applicant requested to extend its use to include an additional process. In this assessment, EFSA updated the safety evaluation of this food enzyme when used in a total of two food manufacturing processes: processing of dairy products for the production of modified milk proteins and the production of plant-based analogues of milk and milk products. The dietary exposure to the food enzyme-total organic solids (TOS) was estimated to be up to 0.091 mg TOS/kg body weight (bw) per day in European populations. Using the no observed adverse effect level previously reported (2162 mg TOS/kg bw per day), the Panel derived a margin of exposure (MoE) of at least 23,758. Based on the data provided for the previous evaluation and the revised MoE, the Panel concluded that this food enzyme does not give rise to safety concerns under the revised intended conditions of use.
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The food enzyme α-glucosidase (α-d-glucoside glucohydrolase; EC 3.2.1.20) is produced with the non-genetically modified Aspergillus niger strain AE-TGU by Amano Enzyme Inc. A safety evaluation of this food enzyme was made previously, in which EFSA concluded that this food enzyme did not give rise to safety concerns when used in four food manufacturing processes. Subsequently, the applicant requested to extend its use to include three additional processes. In this assessment, EFSA updated the safety evaluation of this food enzyme when used in a total of seven food manufacturing processes. The dietary exposure to the food enzyme-total organic solids (TOS) was estimated to be up to 0.693 mg TOS/kg body weight (bw) per day in European populations. When combined with the no observed adverse effect level previously reported (1062 mg TOS/kg bw per day, the highest dose tested), the Panel derived a margin of exposure of at least 1532. Based on the data provided for the previous evaluation and the revised margin of exposure, the Panel concluded that this food enzyme does not give rise to safety concerns under the revised intended conditions of use.
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The food enzyme with phospholipase A1 (phosphatidycholine 1-acylhydrolase, EC 3.1.1.32) and lysophospholipase (2-lysophosphatidylcholine acylhydrolase, EC 3.1.1.5) activities is produced with the genetically modified Aspergillus niger strain PLN by DSM. The genetic modifications do not give rise to safety concerns. The food enzyme is free from viable cells of the production organism and its DNA. It is intended to be used for the production of refined edible fats and oils by degumming. Since residual amounts of total organic solids are removed during this process, dietary exposure was not calculated and toxicological studies were considered unnecessary for the assessment of this food enzyme. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and no matches were found. The Panel considered that the risk of allergic reactions upon dietary exposure cannot be excluded, but the likelihood is low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns, under the intended conditions of use.
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Bacillus paralicheniformis, a species known to produce the antimicrobial bacitracin, could be misidentified as Bacillus licheniformis, depending on the identification method used. For this reason, the European Commission requested EFSA to review the taxonomic identification of formerly assessed B. licheniformis production strains. Following this request, EFSA retrieved the raw data from 27 technical dossiers submitted and found that the taxonomic identification was established by 16S rRNA gene analyses for 15 strains and by whole genome sequence analysis for 12 strains. As a conclusion, only these 12 strains could be unambiguously identified as B. licheniformis.
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The food enzyme bacillolysin (EC 3.4.24.28) is produced with the non-genetically modified Bacillus amyloliquefaciens strain NZYM-NB by Novozymes A/S. The production strain meets the requirements for qualified presumption of safety (QPS) approach to safety assessment. The food enzyme is intended to be used in eleven food manufacturing processes. Since residual amounts of total organic solids (TOS) are removed during two processes, dietary exposure was estimated only for the remaining nine food manufacturing processes. Exposure was estimated to be up to 1.327 mg TOS/kg body weight per day in European populations. As the production strain qualifies for the QPS approach and no issue of concern arising from the production process of the food enzyme was identified, the Panel considered that no toxicological studies other than the assessment of allergenicity were necessary. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that the risk of allergic reactions by dietary exposure cannot be excluded (except for distilled alcohol production), but the likelihood is low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.
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The food enzyme α-galactosidase (α-d-galactoside galactohydrolase; EC 3.2.1.22) is produced with the genetically modified Saccharomyces cerevisiae strain CBS 615.94 by Kerry Ingredients & Flavours Ltd. The production strain of the food enzyme contains multiple copies of a known antimicrobial resistance gene. However, based on the absence of viable cells and DNA from the production organism in the food enzyme, this is not considered to be a risk. As no other concerns arising from the genetically modified microbial source or from the manufacturing process have been identified, the Panel considered that toxicological tests were not needed for the assessment of this food enzyme. The food enzyme is intended to be used in guar gum processing. The dietary exposure was estimated to be up to 0.828 mg TOS/kg body weight per day in European populations. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that a risk of allergic reactions by dietary exposure cannot be excluded, but the likelihood is low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.
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The food enzyme ß-fructofuranosidase (ß-d-fructofuranoside fructohydrolase; EC 3.2.1.26) is produced with the non-genetically modified Saccharomyces cerevisiae strain NCYC R693 by Kerry Ingredients & Flavours Ltd. The production strain meets the requirements for the qualified presumption of safety (QPS) approach. The food enzyme is intended to be used in four food manufacturing processes. The dietary exposure to the food enzyme-total organic solids (TOS) was estimated to be up to 2.485 mg TOS/kg body weight per day in European populations. As the production strain qualifies for the QPS approach of safety assessment and no issue of concern arising from the production process of the food enzyme were identified, the Panel considered that no toxicological studies other than the assessment of allergenicity were necessary. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and one match with a tomato allergen was found. The Panel considered that the risk of allergic reactions upon dietary exposure to this food enzyme, particularly in individuals sensitised to tomato, cannot be excluded. However, the likelihood of allergic reactions is expected not to exceed the likelihood of allergic reactions to tomato. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.
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HYPOTHESIS: The Constant-Murley score (CMS) is one of the most used scales for shoulder dysfunction. The aim of this study is to determine whether the reliability of the CMS can be improved by enhancing the standardization of the items. METHODS: Two consecutive series of 55 patients with shoulder dysfunction were enrolled in a test-retest study and examined by 2 orthopedic surgeons with different levels of expertise. The following scores were measured: CMS, individual relative CMS, relative CMS, and standardized CMS. For each variable, the intraobserver and interobserver reliability was calculated. RESULTS: The less experienced observer had worse intraobserver reliability using the CMS (error, 4 points; 95% limit of agreement, 22) than the expert observer (error, 2.4 points; 95% limit of agreement, 16). The standardized CMS showed better intraobserver reliability, with an error of 0.4 points and 95% limits of agreement of 9 for the expert observer and 13 for the less experienced observer. The correction against the contralateral unaffected side and the reference population determined a worsening of reliability in both observers. Interobserver reliability showed an improvement similar to that of intraobserver reliability (systematic error, 4; 95% limit of agreement, 24) by use of the CMS and improved to 1 point when the standardized CMS was adopted (95% limit of agreement, 12). CONCLUSIONS: This study showed that the standardization of the items significantly improved both the intraobserver reliability and interobserver reliability of the CMS. The level of expertise of the observer has less of an effect on reliability when the score is applied with a higher level of standardization.
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Rango del Movimiento Articular/fisiología , Articulación del Hombro/fisiopatología , Dolor de Hombro/diagnóstico , Adulto , Anciano , Anciano de 80 o más Años , Femenino , Estudios de Seguimiento , Humanos , Masculino , Persona de Mediana Edad , Variaciones Dependientes del Observador , Reproducibilidad de los Resultados , Índice de Severidad de la Enfermedad , Dolor de Hombro/fisiopatologíaRESUMEN
Antimicrobial resistance (AMR) is a quickly advancing threat for human health worldwide and almost 5 million deaths are already attributable to this phenomenon every year. Since antibiotics are failing to treat AMR-bacteria, new tools are needed, and human monoclonal antibodies (mAbs) can fill this role. In almost 50 years since the introduction of the first technology that led to mAb discovery, enormous leaps forward have been made to identify and develop extremely potent human mAbs. While their usefulness has been extensively proved against viral pathogens, human mAbs have yet to find their space in treating and preventing infections from AMR-bacteria and fully conquer the field of infectious diseases. The novel and most innovative technologies herein reviewed can support this goal and add powerful tools in the arsenal of weapons against AMR.
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In the last two decades bisphosphonates (BP) has become the mainstream therapy for osteoporosis and the benefit in reducing the incidence of fractures has been well demonstrated in several studies, together with the drug long term (5-10 years) efficacy and safety. A complication of the long-term use of bisphosphonates is a low-energy stress fractures located in the sub-trochanteric region and the femoral shaft called atypical femur fracture (AFF). These stress fractures can be seen on plain radiographs as simple transverse patterns, with unicortical beaking and hypertrophy of the diaphyseal lateral cortex. Usually a localized thigh pain in the prodromal phase may precede the fracture by months. The current surgical treatment of choice for AFFs is intramedullary nailing (IMN). However, the treatment of AFFs is associated with a higher rate of intra-operative and post-surgical complications. This is related to anatomical e biomechanical reasons. Iatrogenic fractures, deformities, medial gap opening, eccentric position of the distal nail tip with anterior cortex perforation, delayed or non-union are frequent complications of this procedure and healing rate of AFFs. The average healing time of almost 8 months for AFFs appeared to be longer than that for typical femoral fractures, which heal at an average of 3-6 months. The purpose of this study is to analyze the different surgical devices and techniques and to advance some considerations that can be useful to diminish the rate of failure and/or complications in the treatment of AFFs in both oncologic and osteoporotic patients.
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Conservadores de la Densidad Ósea/efectos adversos , Difosfonatos/efectos adversos , Fracturas del Fémur/cirugía , Fijación Intramedular de Fracturas , Curación de Fractura/fisiología , Osteoporosis/tratamiento farmacológico , Fracturas Osteoporóticas/cirugía , Anciano , Conservadores de la Densidad Ósea/uso terapéutico , Difosfonatos/uso terapéutico , Femenino , Fracturas del Fémur/diagnóstico por imagen , Fracturas del Fémur/fisiopatología , Fijación Intramedular de Fracturas/métodos , Guías como Asunto , Humanos , Masculino , Persona de Mediana Edad , Osteoporosis/prevención & control , Fracturas Osteoporóticas/diagnóstico por imagen , Fracturas Osteoporóticas/fisiopatología , RadiografíaRESUMEN
AIM: Lactose and complex carbohydrates maldigestion, common food intolerances due to low gut content of α- and ß-galactosidase, lead to abdominal symptoms including pain, diarrhea, bloating, flatulence, and cramping. Commonly, intolerant patients are advised by physicians to avoid the offending foods (dairy foods, cereals, beans, etc). This food-limiting option, however, has possible nutritional risks. We have therefore evaluated the impact of using pure, enteric-coated α- plus ß-galactosidase on gut symptoms in intolerant subjects instead of avoidance of the offending foods. METHODS: Sixteen subjects intolerant to lactose and/or complex carbohydrates were enrolled and evaluated in terms of gut symptoms with 1) uncontrolled diet, 2) diet devoid of offending foods, and 3) uncontrolled diet along with pure, enteric-coated α- and ß-galactosidase (DDM Galactosidase(®)). RESULTS: Even with the uncontrolled diet, intolerant subjects treated with DDM Galactosidase(®) exhibited reduced gut symptoms (bloating, flatulence, diarrhea, and constipation) significantly better than the control treatment as well as having a diet devoid of offending foods. CONCLUSION: DDM Galactosidase(®) is a valid and safe optional treatment to counteract lactose and complex carbohydrate intolerance in subjects who prefer not to avoid, at least partially, offending foods.
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Fibromyalgia syndrome is mainly characterized by pain, fatigue, and sleep disruption. The etiology of fibromyalgia is still unclear: if central sensitization is considered to be the main mechanism involved, then many other factors, genetic, immunological, and hormonal, may play an important role. The diagnosis is typically clinical (there are no laboratory abnormalities) and the physician must concentrate on pain and on its features. Additional symptoms (e.g., Raynaud's phenomenon, irritable bowel disease, and heat and cold intolerance) can be associated with this condition. A careful differential diagnosis is mandatory: fibromyalgia is not a diagnosis of exclusion. Since 1990, diagnosis has been principally based on the two major diagnostic criteria defined by the ACR. Recently, new criteria have been proposed. The main goals of the treatment are to alleviate pain, increase restorative sleep, and improve physical function. A multidisciplinary approach is optimal. While most nonsteroidal anti-inflammatory drugs and opioids have limited benefit, an important role is played by antidepressants and neuromodulating antiepileptics: currently duloxetine (NNT for a 30% pain reduction 7.2), milnacipran (NNT 19), and pregabalin (NNT 8.6) are the only drugs approved by the US Food and Drug Administration for the treatment of fibromyalgia. In addition, nonpharmacological treatments should be associated with drug therapy.
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Contracture of the elbow represents a disabling condition that can impair a person's quality of life. Regardless of the event that causes an elbow contracture, the conservative or surgical treatment is usually considered technically difficult and associated with complications. When the conservative treatment fails to restore an acceptable range of motion in the elbow, open techniques have been shown to be successful options. More recently the use of arthroscopy has become more popular for several reasons. These reasons include better visualization of intra-articular structures, less tissue trauma from open incisions, and potentially the ability to begin early postoperative motion. The purpose of this paper is to review the indications, complications, and results of arthroscopic management of a stiff elbow.