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1.
Ann R Coll Surg Engl ; 2024 Apr 05.
Artículo en Inglés | MEDLINE | ID: mdl-38578035

RESUMEN

INTRODUCTION: Acute right iliac fossa (RIF) pain is a common presenting symptom in surgical patients, with a wide range of differentials, particularly in premenopausal females. This study explores ultrasound usage in the management of women aged 16-55 years presenting with RIF pain. METHODS: A total of 1,082 patients who presented to a tertiary hospital over 12 months were included. Data were collected from patients' electronic records, including initial clinical impression, imaging, management, operative findings, histology and subsequent hospital attendances within 6 weeks and within 6 months. RESULTS: Following clinical assessment, 607 (56%) of patients underwent an ultrasound. Of these, 280 (25.9%) patients received no radiological imaging on initial presentation, and 252 (42%) had pathology identified on ultrasound. The most common finding was an ovarian cyst, closely followed by unexplained free pelvic fluid. Of the 607 patients scanned, 29 (4.8%) had an ultrasound diagnosis of appendicitis; 254 of 1,082 (23.5%) patients underwent operative management. Of the 254 patients who had surgery, 179 (70.5%) had preoperative imaging. Of the 29 (11.4%) cases where the intraoperative finding was gynaecological, 15 (51.7%) cases had not had any preoperative imaging. The negative appendicectomy rate was 21.3% (45/211). Of the 45 patients who had a histologically normal appendix, 22 (48.9%) had not had any previous imaging. Ultrasound had a specificity of 78% for diagnosing appendicitis. CONCLUSIONS: In patients who underwent operative management, a negative finding or finding not requiring surgical management was associated with no preoperative imaging. This supports the use of ultrasound scans as an adjunct in a multimodal approach to the assessment of women presenting with RIF pain.

2.
Insect Mol Biol ; 11(5): 431-42, 2002 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-12230542

RESUMEN

We have identified a homologue of the Drosophila inhibitor of apoptosis protein 1 in Aedes triseriatus mosquitoes (designated AtIAP1). The AtIAP1 gene maps to a single locus on chromosome 2. The translation product is a 403 amino acid protein that contains two baculovirus IAP repeat (BIR) domains and a RING finger motif. AtIAP1 mRNA was detectable by RT-PCR amplification in all the mosquito developmental stages (embryos, first-fourth instar larvae, early and late pupae, adults) and adult tissues (midguts, ovaries) examined. In contrast, immunoblots with AtIAP1-specific antibodies revealed that the protein was detectable only in certain developmental stages (first instar larvae, early pupae, adults) and tissues (ovaries). AtIAP1-specific serum also recognized proteins in Ae. aegypti, Ae. albopictus and Culex tritaeniorhynchus. Immunoblot analysis revealed that similar amounts of IAP1 were expressed in LaCrosse virus infected and uninfected Ae. albopictus cell cultures.


Asunto(s)
Aedes/genética , Proteínas Portadoras/genética , Expresión Génica , Proteínas de Insectos/genética , Aedes/crecimiento & desarrollo , Aedes/metabolismo , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Proteínas Portadoras/metabolismo , Línea Celular , Mapeo Cromosómico , Cricetinae , ADN Complementario , Drosophila melanogaster , Proteínas Inhibidoras de la Apoptosis , Proteínas de Insectos/metabolismo , Virus La Crosse/fisiología , Datos de Secuencia Molecular , ARN Mensajero , Análisis de Secuencia de ADN , Distribución Tisular
3.
J Virol ; 75(8): 3766-70, 2001 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-11264365

RESUMEN

Influenza A viruses possess two virion surface proteins, hemagglutinin (HA) and neuraminidase (NA). The HA binds to sialyloligosaccharide viral receptors, while the NA removes sialic acids from the host cell and viral sialyloligosaccarides. Alterations of the HA occur during adaptation of influenza viruses to new host species, as in the 1957 and 1968 influenza pandemics. To gain a better understanding of the contributions of the HA and possibly the NA to this process, we generated cell lines expressing reduced levels of the influenza virus receptor determinant, sialic acid, by selecting Madin-Darby canine kidney cells resistant to a lectin specific for sialic acid linked to galactose by alpha(2-3) or alpha(2-6) linkages. One of these cell lines had less than 1/10 as much N-acetylneuraminic acid as its parent cell line. When serially passaged in this cell line, human H3N2 viruses lost sialidase activity due to a large internal deletion in the NA gene, without alteration of the HA gene. These findings indicate that NA mutations can contribute to the adaptation of influenza A virus to new host environments and hence may play a role in the transmission of virus across species.


Asunto(s)
Adaptación Fisiológica , Virus de la Influenza A/enzimología , Ácido N-Acetilneuramínico/metabolismo , Neuraminidasa/metabolismo , Animales , Secuencia de Bases , Línea Celular , Embrión de Pollo , Cromatografía Líquida de Alta Presión , Perros , Fluorometría , Glicoproteínas Hemaglutininas del Virus de la Influenza/genética , Glicoproteínas Hemaglutininas del Virus de la Influenza/metabolismo , Humanos , Virus de la Influenza A/genética , Virus de la Influenza A/fisiología , Lectinas/metabolismo , Mutación/genética , Neuraminidasa/genética , Replicación Viral
4.
EMBO J ; 19(24): 6751-8, 2000 Dec 15.
Artículo en Inglés | MEDLINE | ID: mdl-11118210

RESUMEN

For nuclear export of proteins, the formation of a ternary export complex composed of the export substrate, a cellular export factor and Ran-GTP is crucial. CRM1 is a cellular export factor for proteins containing leucine-rich nuclear export signals (NESs). Although the NES sequence is crucial for nuclear export, its exact role in the formation of the ternary export complex is controversial. Here we demonstrate an interaction between human CRM1 (hCRM1) and influenza A virus NS2 protein, which contains an NES motif in its N-terminal region. Replacement of the hydrophobic amino acids in the NES motif did not abolish NS2's interaction with hCRM1. Using our recently established systems for the generation of influenza virus or virus-like particles from cloned cDNAs, we found that NS2 is essential for nuclear export of influenza virus ribonucleoprotein (RNP) complexes, and that alteration of the NS2-NES abrogated this event and influenza virus generation. These findings suggest that the NS2-NES is not crucial for the interaction of this protein with hCRM1, but is for the formation of the ternary export complex with Ran-GTP.


Asunto(s)
Proteínas Portadoras/metabolismo , Núcleo Celular/metabolismo , Virus de la Influenza A/fisiología , Carioferinas , Receptores Citoplasmáticos y Nucleares , Proteínas no Estructurales Virales/metabolismo , Replicación Viral/fisiología , Transporte Activo de Núcleo Celular , Secuencia de Aminoácidos , Sitios de Unión , Proteínas Portadoras/química , Línea Celular , Núcleo Celular/virología , Secuencia de Consenso , Humanos , Riñón , Leucina , Estadios del Ciclo de Vida , Mutagénesis Sitio-Dirigida , Proteínas Nucleares/fisiología , ARN Polimerasa I/metabolismo , Proteínas Recombinantes de Fusión/metabolismo , Proteínas Recombinantes/química , Proteínas Recombinantes/metabolismo , Proteínas no Estructurales Virales/química , Proteína Exportina 1
5.
J Virol ; 74(11): 5206-12, 2000 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-10799596

RESUMEN

Influenza A viruses possess both hemagglutinin (HA), which is responsible for binding to the terminal sialic acid of sialyloligosaccharides on the cell surface, and neuraminidase (NA), which contains sialidase activity that removes sialic acid from sialyloligosaccharides. Interplay between HA receptor-binding and NA receptor-destroying sialidase activity appears to be important for replication of the virus. Previous studies by others have shown that influenza A viruses lacking sialidase activity can undergo multiple cycles of replication if sialidase activity is provided exogenously. To investigate the sialidase requirement of influenza viruses further, we generated a series of sialidase-deficient mutants. Although their growth was less efficient than that of the parental NA-dependent virus, these viruses underwent multiple cycles of replication in cell culture, eggs, and mice. To understand the molecular basis of this viral growth adaptation in the absence of sialidase activity, we investigated changes in the HA receptor-binding affinity of the sialidase-deficient mutants. The results show that mutations around the HA receptor-binding pocket reduce the virus's affinity for cellular receptors, compensating for the loss of sialidase. Thus, sialidase activity is not absolutely required in the influenza A virus life cycle but appears to be necessary for efficient virus replication.


Asunto(s)
Glicoproteínas Hemaglutininas del Virus de la Influenza/metabolismo , Virus de la Influenza A/enzimología , Neuraminidasa/metabolismo , Receptores de Superficie Celular/metabolismo , Replicación Viral , Animales , Técnicas de Cultivo de Célula , Línea Celular , Embrión de Pollo , Perros , Inhibidores Enzimáticos/farmacología , Femenino , Expresión Génica , Guanidinas , Glicoproteínas Hemaglutininas del Virus de la Influenza/genética , Humanos , Virus de la Influenza A/fisiología , Ratones , Ratones Endogámicos BALB C , Mutagénesis , Neuraminidasa/antagonistas & inhibidores , Neuraminidasa/genética , Piranos , Ácidos Siálicos/farmacología , Zanamivir , alfa-Fetoproteínas/metabolismo
6.
J Learn Disabil ; 31(5): 428-36, 1998.
Artículo en Inglés | MEDLINE | ID: mdl-9763773

RESUMEN

Social outcomes of students who participated in two different educational settings designed to provide special services for students with learning disabilities (LD) placed full-time within the general education classroom were examined. Participants were 185 third-through sixth-grade students: 59 students with LD, 72 low to average achieving, and 54 high achieving. There was an overall educational setting effect, with students on the consultation/collaborative teaching setting demonstrating more positive outcomes than students in the co-teaching setting on friendship quality and peer acceptance. Students with LD in the consultation/collaborative teaching setting also demonstrated moderate increases in the number of reciprocal friendships from fall to spring. Discussion addresses the positive social outcomes for students with LD and high-achieving students in the consultation/collaborative teaching setting, and the importance of monitoring student progress in all settings.


Asunto(s)
Educación , Relaciones Interpersonales , Discapacidades para el Aprendizaje/psicología , Conducta Social , Adolescente , Niño , Niños con Discapacidad/psicología , Femenino , Humanos , Masculino
7.
Surgery ; 119(2): 208-13, 1996 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-8571208

RESUMEN

BACKGROUND: Although secretin has been found within the brain, its central role in pancreatic exocrine function has not been previously addressed. The hypothesis that intracerebroventricular secretin enhances pancreatic volume and bicarbonate output at doses that have no effect when given intravenously was tested. METHODS: Sprague-Dawley rats had a cannula stereotactically placed into the left lateral cerebral ventricle 24 hours before study. At laparotomy the bile and pancreatic ducts were separately cannulated and excluded for tared collections and bicarbonate assay. RESULTS: Increasing doses of intracerebroventricular secretin (0.005, 0.05, and 0.5 microgram/1.0 microliter) induced a significant dose-related increase in bicarbonate output (2.95, 3.32, and 4.02 microEq/30 min, respectively) above basal (2.62 microEq/30 min) compared with control or intracerebroventricular saline treated animals. Pancreatic volume increased to 59.7 microliters at the lowest intracerebroventricular dose and increased (p < 0.025) to 65.8 microliters at the 0.05 intracerebroventricular secretin dose when compared with basal (59.4 microliters). To show that this was not a systemic effect of secretin, intravenous infusion of secretin at 0.005 and 0.05 microgram/kg/hr failed to stimulate either volume or bicarbonate output compared with that observed with intracerebroventricular secretin over the same dose range. CONCLUSIONS: These observations indicate that intracerebroventricular secretin stimulates pancreatic volume and bicarbonate output and suggest that central secretin may play a role in the regulation of exocrine pancreatic secretion.


Asunto(s)
Bicarbonatos/metabolismo , Bilis/metabolismo , Ventrículos Cerebrales/fisiología , Páncreas/efectos de los fármacos , Secretina/farmacología , Animales , Bilis/efectos de los fármacos , Ventrículos Cerebrales/efectos de los fármacos , Relación Dosis-Respuesta a Droga , Inyecciones Intraventriculares , Cinética , Hígado/efectos de los fármacos , Masculino , Páncreas/metabolismo , Páncreas/fisiología , Ratas , Ratas Sprague-Dawley , Valores de Referencia , Técnicas Estereotáxicas , Factores de Tiempo
8.
Am J Optom Physiol Opt ; 63(10): 819-23, 1986 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-3535525

RESUMEN

A double-masked, randomized study was conducted to determine the effects of power and water content on the initial comfort of hydrogel contact lenses in 10 unadapted subjects. Three lens powers (-0.50, -5.00, and -10.00 D) were used in each of three water contents (38, 55, and 70%). A significant negative correlation (p less than 0.05) was found between lens comfort and lens water content; that is, lower water content lenses of lesser bulk were more comfortable than higher water content lenses. These data will allow practitioners to predict patient awareness to various lens types. When fitting hydrogel lenses to an apprehensive patient who has not worn contact lenses previously, it may be advisable to insert a thin, low water content lens initially, thereby maximizing lens comfort.


Asunto(s)
Lentes de Contacto Hidrofílicos/normas , Polietilenglicoles , Sensación , Adulto , Concienciación , Ensayos Clínicos como Asunto , Humanos , Hidrogel de Polietilenoglicol-Dimetacrilato
9.
J Neurosurg Nurs ; 4(1): 83-91, 1972 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-4537754
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