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Journal of Clinical Periodontology Jul 2020The recently introduced 2017 World Workshop on the classification of periodontitis, incorporating stages and grades of disease, aims to link disease classification with...
BACKGROUND
The recently introduced 2017 World Workshop on the classification of periodontitis, incorporating stages and grades of disease, aims to link disease classification with approaches to prevention and treatment, as it describes not only disease severity and extent but also the degree of complexity and an individual's risk. There is, therefore, a need for evidence-based clinical guidelines providing recommendations to treat periodontitis.
AIM
The objective of the current project was to develop a S3 Level Clinical Practice Guideline (CPG) for the treatment of Stage I-III periodontitis.
MATERIAL AND METHODS
This S3 CPG was developed under the auspices of the European Federation of Periodontology (EFP), following the methodological guidance of the Association of Scientific Medical Societies in Germany and the Grading of Recommendations Assessment, Development and Evaluation (GRADE). The rigorous and transparent process included synthesis of relevant research in 15 specifically commissioned systematic reviews, evaluation of the quality and strength of evidence, the formulation of specific recommendations and consensus, on those recommendations, by leading experts and a broad base of stakeholders.
RESULTS
The S3 CPG approaches the treatment of periodontitis (stages I, II and III) using a pre-established stepwise approach to therapy that, depending on the disease stage, should be incremental, each including different interventions. Consensus was achieved on recommendations covering different interventions, aimed at (a) behavioural changes, supragingival biofilm, gingival inflammation and risk factor control; (b) supra- and sub-gingival instrumentation, with and without adjunctive therapies; (c) different types of periodontal surgical interventions; and (d) the necessary supportive periodontal care to extend benefits over time.
CONCLUSION
This S3 guideline informs clinical practice, health systems, policymakers and, indirectly, the public on the available and most effective modalities to treat periodontitis and to maintain a healthy dentition for a lifetime, according to the available evidence at the time of publication.
Topics: Germany; Gingivitis; Health Behavior; Humans; Periodontics; Periodontitis
PubMed: 32383274
DOI: 10.1111/jcpe.13290 -
Annual Review of Pathology Jan 2019Prion diseases are rapidly progressive, incurable neurodegenerative disorders caused by misfolded, aggregated proteins known as prions, which are uniquely infectious.... (Review)
Review
Prion diseases are rapidly progressive, incurable neurodegenerative disorders caused by misfolded, aggregated proteins known as prions, which are uniquely infectious. Remarkably, these infectious proteins have been responsible for widespread disease epidemics, including kuru in humans, bovine spongiform encephalopathy in cattle, and chronic wasting disease in cervids, the latter of which has spread across North America and recently appeared in Norway and Finland. The hallmark histopathological features include widespread spongiform encephalopathy, neuronal loss, gliosis, and deposits of variably sized aggregated prion protein, ranging from small, soluble oligomers to long, thin, unbranched fibrils, depending on the disease. Here, we explore recent advances in prion disease research, from the function of the cellular prion protein to the dysfunction triggering neurotoxicity, as well as mechanisms underlying prion spread between cells. We also highlight key findings that have revealed new therapeutic targets and consider unanswered questions for future research.
Topics: Amyloid; Animals; Cattle; Deer; Humans; Neurodegenerative Diseases; Prion Diseases; Prion Proteins
PubMed: 30355150
DOI: 10.1146/annurev-pathmechdis-012418-013109 -
Continuum (Minneapolis, Minn.) Dec 2015This article presents an update on the clinical aspects of human prion disease, including the wide spectrum of their presentations. (Review)
Review
PURPOSE OF REVIEW
This article presents an update on the clinical aspects of human prion disease, including the wide spectrum of their presentations.
RECENT FINDINGS
Prion diseases, a group of disorders caused by abnormally shaped proteins called prions, occur in sporadic (Jakob-Creutzfeldt disease), genetic (genetic Jakob-Creutzfeldt disease, Gerstmann-Sträussler-Scheinker syndrome, and fatal familial insomnia), and acquired (kuru, variant Jakob-Creutzfeldt disease, and iatrogenic Jakob-Creutzfeldt disease) forms. This article presents updated information on the clinical features and diagnostic methods for human prion diseases. New antemortem potential diagnostic tests based on amplifying prions in order to detect them are showing very high specificity. Understanding of the diversity of possible presentations of human prion diseases continues to evolve, with some genetic forms progressing slowly over decades, beginning with dysautonomia and neuropathy and progressing to a frontal-executive dementia with pathology of combined prionopathy and tauopathy. Unfortunately, to date, all human prion disease clinical trials have failed to show survival benefit. A very rare polymorphism in the prion protein gene recently has been identified that appears to protect against prion disease; this finding, in addition to providing greater understanding of the prionlike mechanisms of neurodegenerative disorders, might lead to potential treatments.
SUMMARY
Sporadic Jakob-Creutzfeldt disease is the most common form of human prion disease. Genetic prion diseases, resulting from mutations in the prion-related protein gene (PRNP), are classified based on the mutation, clinical phenotype, and neuropathologic features and can be difficult to diagnose because of their varied presentations. Perhaps most relevant to this Continuum issue on neuroinfectious diseases, acquired prion diseases are caused by accidental transmission to humans, but fortunately, they are the least common form and are becoming rarer as awareness of transmission risk has led to implementation of measures to prevent such occurrences.
Topics: Humans; Prion Diseases
PubMed: 26633779
DOI: 10.1212/CON.0000000000000251 -
Viruses Mar 2019Kuru, the first human prion disease was transmitted to chimpanzees by D. Carleton Gajdusek (1923⁻2008). In this review, we summarize the history of this seminal... (Review)
Review
Kuru, the first human prion disease was transmitted to chimpanzees by D. Carleton Gajdusek (1923⁻2008). In this review, we summarize the history of this seminal discovery, its anthropological background, epidemiology, clinical picture, neuropathology, and molecular genetics. We provide descriptions of electron microscopy and confocal microscopy of kuru amyloid plaques retrieved from a paraffin-embedded block of an old kuru case, named Kupenota. The discovery of kuru opened new vistas of human medicine and was pivotal in the subsequent transmission of Creutzfeldt⁻Jakob disease, as well as the relevance that bovine spongiform encephalopathy had for transmission to humans. The transmission of kuru was one of the greatest contributions to biomedical sciences of the 20th century.
Topics: Animals; Cannibalism; History, 20th Century; Humans; Kuru; Pan troglodytes; Papua New Guinea; Prions
PubMed: 30866511
DOI: 10.3390/v11030232 -
Revista Espanola de Enfermedades... Nov 2018Meckel's diverticulum is the most common anomalous development of the gastrointestinal system that results from an incomplete vitelline canal. A diagnosis is usually... (Review)
Review
Meckel's diverticulum is the most common anomalous development of the gastrointestinal system that results from an incomplete vitelline canal. A diagnosis is usually made during the clinical examination of presentations such as unexplained gastrointestinal bleeding, obstruction, inflammation or perforation. The purpose of this review is to provide an adequate level of knowledge of the clinical and diagnostic features as well as the management of Meckel's diverticulum. Diagnosis of Meckel's diverticulum may be challenging as the condition remains asymptomatic or may mimic various diseases and obscure the clinical picture. Life-threatening complications include bleeding, obstruction, inflammation and perforation. Therefore, it is essential that anatomical and pathophysiological characteristics are known in detail in order to prevent complications which will result in morbidity and mortality.
Topics: Humans; Meckel Diverticulum
PubMed: 30032625
DOI: 10.17235/reed.2018.5628/2018 -
Journal of Internal Medicine Aug 2016There are around 30 human diseases associated with protein misfolding and amyloid formation, each one caused by a certain protein or peptide. Many of these diseases are... (Review)
Review
There are around 30 human diseases associated with protein misfolding and amyloid formation, each one caused by a certain protein or peptide. Many of these diseases are lethal and together they pose an enormous burden to society. The prion protein has attracted particular interest as being shown to be the pathogenic agent in transmissible diseases such as kuru, Creutzfeldt-Jakob disease and bovine spongiform encephalopathy. Whether similar transmission could occur also in other amyloidoses such as Alzheimer's disease, Parkinson's disease and serum amyloid A amyloidosis is a matter of intense research and debate. Furthermore, it has been suggested that novel biomaterials such as artificial spider silk are potentially amyloidogenic. Here, we provide a brief introduction to amyloid, prions and other proteins involved in amyloid disease and review recent evidence for their potential transmission. We discuss the similarities and differences between amyloid and silk, as well as the potential hazards associated with protein-based biomaterials.
Topics: Amyloid; Animals; Humans; Protein Folding; Proteostasis Deficiencies; Silk
PubMed: 27002185
DOI: 10.1111/joim.12499 -
Turkish Journal of Medical Sciences Feb 2020Hip fractures in older adults are associated with high morbidity, mortality, and subsequent hospital costs and decreased quality of life. The objective of this study was...
BACKGROUND/AIM
Hip fractures in older adults are associated with high morbidity, mortality, and subsequent hospital costs and decreased quality of life. The objective of this study was to evaluate geriatric patients who underwent partial prosthesis surgery following hip fracture and effects of early mobilization and weight bearing on postoperative walking ability and pain.
MATERIALS AND METHODS
A total of 52 geriatric patients with intertrochanteric and femoral neck fractures were included in the study. Patients’ service files, system records, pre- and postoperative X-rays were retrospectively reviewed.
RESULTS
There were 52 patients in the study group with 36 (69.2%) being female. The mean age of the patients was found as 82.9 ± 6.5 years. The mean length of stay in hospital was found as 6.2 ± 2.6 days. The mean length of stay in hospital was found as 5.3 ± 1.7 days in male and 6.6 ± 2.8 days in female patients, and the difference was statistically significant (P = 0.035). The mean length of stay in hospital was found as 5.4 ± 1.8 days in early mobilization group and 6.9 ± 2.9 days in late mobilization group, and the difference was statistically significant (P = 0.026). There was a significant difference between Harris and pain scores in terms of the time of first weight bearing at the postoperative 1st month follow-up. Harris score was found as 84.0 ± 5.8 (median: 84.0, min–max: 73–94), and the main pain score as 36.8 ± 6.8 in the group with the first weight bearing within the first 24 h, while Harris score was found as 71.10 ± 2.8, and the main pain score as 24.4 ± 6.4 in the group with the first weight bearing after the postoperative 24th hour.
CONCLUSION
The results of our study indicated that early mobilization and full weight bearing in geriatric patients after hip fracture surgery shortened length of stay in hospital, reduced postoperative pain, and increased walking ability.
Topics: Aged; Aged, 80 and over; Early Ambulation; Female; Hip Fractures; Humans; Length of Stay; Male; Pain, Postoperative; Retrospective Studies; Walking; Weight-Bearing
PubMed: 31742370
DOI: 10.3906/sag-1906-57 -
Infectious Diseases of Poverty Jun 2016Human prion diseases are a group of transmissible, progressive, and invariably fatal neurodegenerative disorders, which include Kuru, Creutzfeldt-Jakob disease (CJD),... (Review)
Review
Human prion diseases are a group of transmissible, progressive, and invariably fatal neurodegenerative disorders, which include Kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scheinker syndrome, and fatal familial insomnia. Human prion diseases affect approximately 1-2 persons per million worldwide annually, occurring in sporadic, inherited, and acquired forms. These diseases have attracted both scientific and public attention not only because of their mysterious pathogen, but also due to their considerable threat to public health since the emergence of the variant CJD.There are still no specific therapeutic and prophylactic interventions available for prion diseases, thus active surveillance of human prion diseases is critical for disease control and prevention. Since 1993, CJD surveillance systems have been established in many countries and regions, and several long-term multinational cooperative projects have been conducted.In this paper, the epidemiological characteristics of various human prion diseases and the active surveillance systems pertaining to them in different countries and regions are summarized and reviewed.
Topics: Epidemiological Monitoring; Humans; Prion Diseases; Public Health
PubMed: 27251305
DOI: 10.1186/s40249-016-0143-8 -
Cold Spring Harbor Perspectives in... Jan 2017Prions are proteins that can adopt self-perpetuating conformations and are traditionally regarded as etiological agents of infectious neurodegenerative diseases in... (Review)
Review
Prions are proteins that can adopt self-perpetuating conformations and are traditionally regarded as etiological agents of infectious neurodegenerative diseases in humans, such as Creutzfeldt-Jakob disease, kuru, and transmissible encephalopathies. More recently, a growing consensus has emerged that prion-like, self-templating mechanisms also underlie a variety of neurodegenerative disorders, including amyotrophic lateral sclerosis, Alzheimer's disease, and Huntington's disease. Perhaps most surprising, not all prion-like aggregates are associated with pathological changes. There are now several examples of prion-like proteins in mammals that serve positive biological functions in their aggregated state. In this review, we discuss functional prions in the nervous system, with particular emphasis on the cytoplasmic polyadenylation element-binding protein (CPEB) and the role of its prion-like aggregates in synaptic plasticity and memory. We also mention a more recent example of a functional prion-like protein in the brain, TIA-1, and its role during stress. These studies of functional prion-like proteins have provided a number of generalizable insights on how prion-based protein switches may operate to serve physiological functions in higher eukaryotes.
Topics: Animals; Aplysia; Brain; Drosophila; Humans; Memory; Models, Animal; Prions; Serotonin; Synapses; Transcription Factors; mRNA Cleavage and Polyadenylation Factors
PubMed: 28049644
DOI: 10.1101/cshperspect.a023671