RESUMO
Rehabilitation traumatology has developed within the field of physical medicine and rehabilitation as a specialized area of knowledge in which the physiatrist works with the traumatology team to enhance the functional outcome of trauma patients. Based on the definition of traumatology in the American Heritage Dictionary, the authors propose rehabilitation traumatology be "the branch of medicine that deals with the treatment of serious wounds, injuries, and disabilities," "to restore [the patient] to good health or useful life." This article reviews the history of traumatology, special considerations of the traumatology patient through the continuum of care, and concepts toward the creation of a rehabilitation traumatology program. LEVEL OF EVIDENCE: V.
Assuntos
Pessoas com Deficiência/reabilitação , Medicina Física e Reabilitação/normas , Centros de Traumatologia/organização & administração , Traumatologia/normas , Ferimentos e Lesões/reabilitação , Medicina Baseada em Evidências , Feminino , Previsões , Humanos , Masculino , Narração , Medicina Física e Reabilitação/tendências , Traumatologia/tendências , Estados UnidosRESUMO
Monitoring fetal wellbeing is key in modern obstetrics. While fetal movement is routinely used as a proxy to fetal wellbeing, accurate, noninvasive, long-term monitoring of fetal movement is challenging. A few accelerometer-based systems have been developed in the past few years, to tackle common issues in ultrasound measurement and enable remote, self-administrated monitoring of fetal movement during pregnancy. However, many questions remain unanswered to date on the optimal setup in terms of body-worn accelerometers as well as signal processing and machine learning techniques used to detect fetal movement. In this paper, we systematically analyze the trade-offs between sensor number and positioning, the presence of reference accelerometers outside of the abdominal area and provide guidelines on dealing with class imbalance. Using a dataset of 15 measurements collected employing 6 three-axial accelerometers we show that including a reference accelerometer on the back of the participant consistently improves fetal movement detection performance regardless of the number of sensors utilized. We also show that two accelerometers plus a reference accelerometer are sufficient for optimal results.
Assuntos
Acelerometria/instrumentação , Monitorização Fetal/métodos , Movimento Fetal , Processamento de Sinais Assistido por Computador , Acelerometria/métodos , Feminino , Monitorização Fetal/instrumentação , Humanos , GravidezRESUMO
Photoplethysmography (PPG) is a non-invasive, inexpensive and unobtrusive method to achieve heart rate monitoring during physical exercises. Motion artifacts during exercise challenge the heart rate estimation from wrist-type PPG signals. This paper presents a methodology to overcome these limitation by incorporating acceleration information. The proposed algorithm consisted of four stages: (1) A wavelet based denoising, (2) an acceleration based denoising, (3) a frequency based approach to estimate the heart rate followed by (4) a postprocessing step. Experiments with different movement types such as running and rehabilitation exercises were used for algorithm design and development. Evaluation of our heart rate estimation showed that a mean absolute error 1.96 bpm (beats per minute) with standard deviation of 2.86 bpm and a correlation of 0.98 was achieved with our method. These findings suggest that the proposed methodology is robust to motion artifacts and is therefore applicable for heart rate monitoring during sports and rehabilitation.
Assuntos
Exercício Físico , Frequência Cardíaca/fisiologia , Algoritmos , Artefatos , Humanos , Fotopletismografia , Corrida/fisiologia , Processamento de Sinais Assistido por Computador , Análise de OndaletasRESUMO
BACKGROUND: During clotting, a thrombin cleaves fibrinogen releasing fibrinopeptide A (FPA). FPA is easily identified in serum using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry (MS). Using MALDI-TOF MS, we observed multiple, progressively shorter fragments of serum FPA. Following ambient incubation of serum, variations in the content of FPA fragments occur over time. Denaturation of a thrombin by heating the serum sample appears to minimize this variation. These observations suggest that intrinsic proteolytic and peptidolytic activity is elevated in serum and perhaps originates from the coagulation cascade enzymes themselves, especially a thrombin. METHODS: Extrinsic addition of a thrombin to a subset (3-30 kDa) of plasma proteins was carried out to induce proteolysis and to examine the resultant peptides to reveal a thrombin susceptible parent proteins. One of these identified proteins, hemopexin, was directly digested by a thrombin and the peptides examined to confirm the observations from the initial plasma protein digestion. RESULTS: Extrinsic addition of a thrombin to a subset (3-30 kDa) of plasma proteins results in wide-spread digestion of proteins unrelated to coagulation, revealing a substrate range encompassing more than fibrinogen. Direct digestion of one of these proteins, hemopexin, by a thrombin confirms these observations. CONCLUSIONS: The resulting peptides indicate broad tolerance beyond the consensus R-G cleavage site of fibrinogen; in fact, there appears to be no bias for the amino acid following the R/K residue. These data support our hypothesis that the enzymatic activities inherent to coagulation, or at least to thrombin, contribute to destabilization of the protein and peptide content of serum.
Assuntos
Fibrinopeptídeo A/análise , Hemopexina/análise , Fragmentos de Peptídeos/sangue , Peptídeo Hidrolases/metabolismo , Proteômica/métodos , Trombina/fisiologia , Sequência de Aminoácidos , Coagulação Sanguínea/fisiologia , Fibrinogênio/metabolismo , Fibrinopeptídeo A/química , Fibrinopeptídeo A/metabolismo , Hemopexina/química , Hemopexina/metabolismo , Temperatura Alta , Humanos , Técnicas In Vitro , Dados de Sequência Molecular , Fragmentos de Peptídeos/química , Fragmentos de Peptídeos/metabolismo , Plasma , Inibidores de Proteases/farmacologia , Estabilidade Proteica , Soro , Manejo de Espécimes , Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz/métodos , Trombina/metabolismoRESUMO
High-efficiency prefractionation of complex protein mixtures is critical for top-down proteomics, i.e., the analysis of intact proteins by MS. Free-flow electrophoresis (FFE) can be used for IEF to separate proteins within a pH gradient according to their pIs. In an FFE system, this separation is performed entirely in the liquid phase, without the need for particulate chromatographic media, gels, or membranes. Herein, we demonstrated the compatibility of IEF-FFE with ESI-Fourier transform ICR MS (ESI-FTICR-MS) for top-down experiments. We demonstrated that IEF-FFE of intact proteins were highly reproducible between FFE instruments, between laboratories, and between analyses. Applying native (0.2% hydroxypropylmethyl cellulose) IEF-FFE to an enzyme resulted in no decrease in enzyme activity; applying either native or denaturing (8 M urea) IEF-FFE to a four-protein mixture with different pIs resulted in isolation of each protein into separate fractions in a 96-well plate. After desalting, each protein was sequenced by top-down MS/MS. As an application of this technique, chicken erythrocyte histone H2A-IV and its major modified forms were enriched by IEF-FFE. Top-down analysis revealed Lys-5 to be a major acetylation site, in addition to N-terminal acetylation.
Assuntos
Ciclotrons , Análise de Fourier , Focalização Isoelétrica/métodos , Proteômica/métodos , Espectrometria de Massas por Ionização por Electrospray , Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz , Sequência de Aminoácidos , Animais , Bovinos , Galinhas , Cavalos , Concentração de Íons de Hidrogênio , Dados de Sequência Molecular , Proteômica/instrumentação , Espectrometria de Massas por Ionização por Electrospray/métodos , Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz/métodosRESUMO
Human plasma and serum samples, including protein and peptide biomarkers, are subjected to preanalytical variations and instability caused by intrinsic proteases. In this study, we directly investigated the stability of peptide biomarkers by spiking an isotopically labeled peptide into human plasma and serum samples and then monitoring its time-dependent change. Fibrinogen peptide A (FPA) was used as a model substrate, and its degradation in a conventional serum and plasma either with citrate, heparin, or EDTA as the anticoagulant, or EDTA plus protease inhibitors (inhibited plasma), was measured using time-course MALDI-TOF MS analysis. The FPA and other peptides tested in this study vary in these samples. However, the peptides are most stable in the inhibited plasma followed by, in general order, EDTA plasma, citrate plasma, heparin plasma and serum, demonstrating the benefit of plasma versus serum, and protease inhibitors for biomarker stabilization. Kinetic analysis indicates that intrinsic peptidases cause an observed first-order Sequential Multiple-Step Reaction (SMSR) in digestion of the peptide. Modeling analysis of the SMSR demonstrates that step reactions differ in their kinetic rate constants, suggesting a significant contribution of the truncated end residue on the substrate specificity of the intrinsic peptidase(s). Our observations further show that synthetic peptides introduced into plasma as internal controls can also be degraded, and thus, their (in)stability as a preanalytical variable should not be overlooked.