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1.
J Arthroplasty ; 29(9): 1717-22, 2014 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-24814806

RESUMEN

There is currently wide variation in the use and cost of post acute care following total joint arthroplasty. Additionally the optimum setting to which patients should be discharged after surgery is controversial. Discharge patterns following joint replacement vary widely between physicians at our institution, however, only weak correlations were found between the cost of discharge and length of stay or readmission rates. The inter-physician variance in discharge cost did not correlate to a difference in quality, as measured by length of stay and readmission rates, but does imply there is significant opportunity to modify physician discharge practices without impacting patient outcomes and the quality of care.


Asunto(s)
Artroplastia de Reemplazo de Cadera/economía , Artroplastia de Reemplazo de Rodilla/economía , Tiempo de Internación/economía , Medicare/economía , Alta del Paciente/economía , Readmisión del Paciente/economía , Anciano , Anciano de 80 o más Años , Comorbilidad , Femenino , Humanos , Incidencia , Seguro de Salud/economía , Masculino , Persona de Mediana Edad , Evaluación de Resultado en la Atención de Salud/economía , Médicos/economía , Estudios Retrospectivos , Estados Unidos
2.
J Phys Chem Lett ; 13(26): 6236-6243, 2022 Jul 07.
Artículo en Inglés | MEDLINE | ID: mdl-35770969

RESUMEN

We formulate the maximum driving force (MDF) parameter as a descriptor to capture the thermodynamic stability of aqueous surface scale creation over a range of environmental conditions. We use free energies of formation, ΔfG's, sourced from high-throughput density functional theory (DFT) calculations and experimental databases to compute the maximum driving force for a range of materials, including oxides and hydroxides of varying compositions. We show how to use the MDF to describe trends in the aqueous corrosion of nickel thin films determined from experimental linear sweep voltammetry data. We also show how to account for subsurface oxidation behavior using depth-dependent effective chemical potentials. We anticipate this approach will increase the overall understanding of oxide formation on chemically complex multielement alloys, where competing oxide phases can form during transient aqueous corrosion.

3.
J Pediatr Rehabil Med ; 14(3): 553-557, 2021.
Artículo en Inglés | MEDLINE | ID: mdl-34057105

RESUMEN

This case report details the complex rehabilitation of an adolescent patient with congenital heart disease with anomalous origin of the left coronary artery from the pulmonary artery (ALCAPA) who presented with a sudden cardiac arrest. The International Classification of Functioning, Disability and Health for Children and Youth, World Health Organization (ICF-CY WHO) principles were used to guide the course of the patient's acute inpatient rehabilitation.


Asunto(s)
Síndrome de Bland White Garland , Actividades Cotidianas , Adolescente , Niño , Muerte Súbita Cardíaca , Evaluación de la Discapacidad , Humanos , Organización Mundial de la Salud
4.
Skelet Muscle ; 7(1): 11, 2017 06 06.
Artículo en Inglés | MEDLINE | ID: mdl-28587652

RESUMEN

BACKGROUND: Sarcospan (SSPN) is a transmembrane protein that interacts with the sarcoglycans (SGs) to form a tight subcomplex within the dystrophin-glycoprotein complex that spans the sarcolemma and interacts with laminin in the extracellular matrix. Overexpression of SSPN ameliorates Duchenne muscular dystrophy in murine models. METHODS: Standard cloning approaches were used to identify nanospan, and nanospan-specific polyclonal antibodies were generated and validated. Biochemical isolation of skeletal muscle membranes and two-photon laser scanning microscopy were used to analyze nanospan localization in muscle from multiple murine models. Duchenne muscular dystrophy biopsies were analyzed by immunoblot analysis of protein lysates as well as indirect immunofluorescence analysis of muscle cryosections. RESULTS: Nanospan is an alternatively spliced isoform of sarcospan. While SSPN has four transmembrane domains and is a core component of the sarcolemmal dystrophin-glycoprotein complex, nanospan is a type II transmembrane protein that does not associate with the dystrophin-glycoprotein complex. We demonstrate that nanospan is enriched in the sarcoplasmic reticulum (SR) fractions and is not present in the T-tubules. SR fractions contain membranes from three distinct structural regions: a region flanking the T-tubules (triadic SR), a SR region across the Z-line (ZSR), and a longitudinal SR region across the M-line (LSR). Analysis of isolated murine muscles reveals that nanospan is mostly associated with the ZSR and triadic SR, and only minimally with the LSR. Furthermore, nanospan is absent from the SR of δ-SG-null (Sgcd-/-) skeletal muscle, a murine model for limb girdle muscular dystrophy 2F. Analysis of skeletal muscle biopsies from Duchenne muscular dystrophy patients reveals that nanospan is preferentially expressed in type I (slow) fibers in both control and Duchenne samples. Furthermore, nanospan is significantly reduced in Duchenne biopsies. CONCLUSIONS: Alternative splicing of proteins from the SG-SSPN complex produces δ-SG3, microspan, and nanospan that localize to the ZSR and the triadic SR, where they may play a role in regulating resting calcium levels as supported by previous studies (Estrada et al., Biochem Biophys Res Commun 340:865-71, 2006). Thus, alternative splicing of SSPN mRNA generates three protein isoforms (SSPN, microspan, and nanospan) that differ in the number of transmembrane domains affecting subcellular membrane association into distinct protein complexes.


Asunto(s)
Empalme Alternativo , Proteínas Portadoras/genética , Proteínas de la Membrana/genética , Proteínas de Neoplasias/genética , Sarcoglicanopatías/metabolismo , Retículo Sarcoplasmático/metabolismo , Animales , Proteínas Portadoras/metabolismo , Humanos , Proteínas de la Membrana/metabolismo , Ratones , Ratones Endogámicos C57BL , Proteínas de Neoplasias/metabolismo , Isoformas de Proteínas/genética , Isoformas de Proteínas/metabolismo , Transporte de Proteínas , Sarcoglicanopatías/genética , Sarcoglicanopatías/patología , Sarcoglicanos/genética , Retículo Sarcoplasmático/ultraestructura
5.
Int J Shoulder Surg ; 6(4): 112-5, 2012 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-23493640

RESUMEN

AIMS: To assess whether patients above 50 years of age, particularly female, would benefit from repair of their SLAP tears. SETTINGS AND DESIGN: Review of patients' records followed by telephone interview at a minimum of two years after surgery. MATERIALS AND METHODS: Seventy-two consecutive patients who had their SLAP repaired were retrospective reviewed by an independent examiner. Follow up was by telephone interview with pain and functional results measured according to the Oxford Shoulder Questionnaire. The patients were asked whether they would undergo the same operation if they had a similar injury. STATISTICAL ANALYSIS USED: OKS - One way ANOVA, followed by Tukey HSD multiple comparisons were used to assess the Oxford Shoulder score. Kruskal-Wallis Test was used to assess the final VAS Pain Score. Student's T tests for Oxford scores before and after surgery. RESULTS: Between 2007-2008, 38 male patients and 34 female patients with an average age of 53 (19-75) years had their SLAP repair. Good to excellent results in Oxford shoulder scores were reported in 94%. 68 0f 72 patients would undergo the same if they had a similar injury. No statistical correlation was found between the patient's age, gender and outcome scores. CONCLUSIONS: Neither the patients' gender nor their age above 50 affected the outcome after surgery.

6.
Exp Cell Res ; 313(4): 639-51, 2007 Feb 15.
Artículo en Inglés | MEDLINE | ID: mdl-17223103

RESUMEN

Sarcospan is a component of the dystrophin-glycoprotein complex that forms a tight subcomplex with the sarcoglycans. The sarcoglycan-sarcospan subcomplex functions to stabilize alpha-dystroglycan at the plasma membrane and perturbations of this subcomplex are associated with autosomal recessive limb-girdle muscular dystrophy. In order to characterize protein interactions within this subcomplex, we first demonstrate that sarcospan forms homo-oligomers within the membrane. Experiments with a panel of site-directed mutants reveal that proper structure of the large extracellular loop is an important determinant of oligo formation. Furthermore, the intracellular N- and C-termini contribute to stability of sarcospan-mediated webs. Point mutation of each cysteine residue reveals that Cys 162 and Cys 164 within the large extracellular loop form disulfide bridges, which are critical for proper sarcospan structure. The extracellular domain of sarcospan also forms the main binding site for the sarcoglycans. We propose a model whereby sarcospan forms homo-oligomers that cluster the components of the dystrophin-glycoprotein complex within the membrane.


Asunto(s)
Proteínas Portadoras/química , Complejo de Proteínas Asociado a la Distrofina/química , Complejo de Proteínas Asociado a la Distrofina/fisiología , Proteínas de la Membrana/química , Proteínas de Neoplasias/química , Sarcoglicanos/química , Animales , Sitios de Unión , Células CHO , Proteínas Portadoras/metabolismo , Células Cultivadas , Cricetinae , Cricetulus , Proteínas de la Membrana/metabolismo , Ratones , Ratones Transgénicos , Modelos Biológicos , Músculo Esquelético/química , Proteínas de Neoplasias/metabolismo , Estructura Cuaternaria de Proteína , Proteínas Recombinantes/química , Sarcoglicanos/metabolismo
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