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198 results on '"Kempson, S. A."'

3. COVID-19: Rapid antigen detection for SARS-CoV-2 by lateral flow assay: A national systematic evaluation of sensitivity and specificity for mass-testing

Author

Peto, T., Affron, D., Afrough, B., Agasu, A., Ainsworth, M., Allanson, A., Allen, K., Allen, C., Archer, L., Ashbridge, N., Aurfan, I., Avery, M., Badenoch, E., Bagga, P., Balaji, R., Baldwin, E., Barraclough, S., Beane, C., Bell, J., Benford, T., Bird, S., Bishop, M., Bloss, A., Body, R., Boulton, R., Bown, A., Bratten, C., Bridgeman, C., Britton, D., Brooks, T., Broughton-Smith, M., Brown, P., Buck, B., Butcher, E., Byrne, W., Calderon, G., Campbell, S., Carr, O., Carter, P., Carter, D., Cathrall, M., Catton, M., Chadwick, J., Chapman, D., Chau, K.K., Chaudary, T., Chidavaenzi, S., Chilcott, S., Choi, B., Claasen, H., Clark, S., Clarke, R., Clarke, D., Clayton, R., Collins, K., Colston, R., Connolly, J., Cook, E., Corcoran, M., Corley, B., Costello, L., Coulson, C., Crook, A., Crook, D.W., D'Arcangelo, S., Darby, M-A, Davis, J., de Koning, R., Derbyshire, P., Devall, P., Dolman, M., Draper, N., Driver, M., Dyas, S., Eaton, E., Edwards, J., Elderfield, R., Ellis, K., Ellis, G., Elwell, S., Evans, R., Evans, B., Evans, M., Eyre, D., Fahey, C., Fenech, V., Field, J., Field, A., Foord, T., Fowler, T., French, M., Fuchs, H., Gan, J., Gernon, J., Ghadiali, G., Ghuman, N., Gibbons, K., Gill, G., Gilmour, K., Goel, A., Gordon, S., Graham, T., Grassam-Rowe, A., Green, D., Gronert, A., Gumsley-Read, T., Hall, C., Hallis, B., Hammond, S., Hammond, P., Hanney, B., Hardy, V., Harker, G., Harris, A., Havinden-Williams, M., Hazell, E., Henry, J., Hicklin, K., Hollier, K., Holloway, B., Hoosdally, S.J., Hopkins, S., Hughes, L., Hurdowar, S., Hurford, S-A, Jackman, J., Jackson, H., Johns, R., Johnston, S., Jones, J., Kanyowa, T., Keating-Fedders, K., Kempson, S., Khan, I., Khulusi, B., Knight, T., Krishna, A., Lahert, P., Lampshire, Z., Lasserson, D., Lee, K., Lee, L.Y.W., Legard, A., Leggio, C., Liu, J., Lockett, T., Logue, C., Lucas, V., Lumley, S.F., Maripuri, V., Markham, D., Marshall, E., Matthews, P.C., Mckee, S., McKee, D.F., McLeod, N., McNulty, A., Mellor, F., Michel, R., Mighiu, A., Miller, J., Mirza, Z., Mistry, H., Mitchell, J., Moeser, M.E., Moore, S., Muthuswamy, A., Myers, D., Nanson, G., Newbury, M., Nicol, S., Nuttall, H., Nwanaforo, J.J., Oliver, L., Osbourne, W., Osbourne, J., Otter, A., Owen, J., Panchalingam, S., Papoulidis, D., Pavon, J.D., Peace, A., Pearson, K., Peck, L., Pegg, A., Pegler, S., Permain, H., Perumal, P., Peto, L., Peto, T.E.A., Pham, T., Pickford, H.L., Pinkerton, M., Platton, M., Price, A., Protheroe, E., Purnell, H., Rawden, L., Read, S., Reynard, C., Ridge, S., Ritter, T.G., Robinson, J., Robinson, P., Rodger, G., Rowe, C., Rowell, B., Rowlands, A., Sampson, S., Saunders, K., Sayers, R., Sears, J., Sedgewick, R., Seeney, L., Selassie, A., Shail, L., Shallcross, J., Sheppard, L., Sherkat, A., Siddiqui, S., Sienkiewicz, A., Sinha, L., Smith, J., Smith, E., Stanton, E., Starkey, T., Stawiarski, A., Sterry, A., Stevens, J., Stockbridge, M., Stoesser, N., Sukumaran, A., Sweed, A., Tatar, S., Thomas, H., Tibbins, C., Tiley, S., Timmins, J., Tomas-Smith, C., Topping, O., Turek, E., Neibler, T., Trigg-Hogarth, K., Truelove, E., Turnbull, C., Tyrrell, D., Vaughan, A., Vertannes, J., Vipond, R., Wagstaff, L., Waldron, J., Walker, P., Walker, A.S., Walters, M., Wang, J.Y., Watson, E., Webberley, K., Webster, K., Westland, G., Wickens, I., Willcocks, J., Willis, H., Wilson, S., Wilson, B., Woodhead, L., Wright, D., Xavier, B., Yelnoorkar, F., Zeidan, L., Zinyama, R., Peto, T., Affron, D., Afrough, B., Agasu, A., Ainsworth, M., Allanson, A., Allen, K., Allen, C., Archer, L., Ashbridge, N., Aurfan, I., Avery, M., Badenoch, E., Bagga, P., Balaji, R., Baldwin, E., Barraclough, S., Beane, C., Bell, J., Benford, T., Bird, S., Bishop, M., Bloss, A., Body, R., Boulton, R., Bown, A., Bratten, C., Bridgeman, C., Britton, D., Brooks, T., Broughton-Smith, M., Brown, P., Buck, B., Butcher, E., Byrne, W., Calderon, G., Campbell, S., Carr, O., Carter, P., Carter, D., Cathrall, M., Catton, M., Chadwick, J., Chapman, D., Chau, K.K., Chaudary, T., Chidavaenzi, S., Chilcott, S., Choi, B., Claasen, H., Clark, S., Clarke, R., Clarke, D., Clayton, R., Collins, K., Colston, R., Connolly, J., Cook, E., Corcoran, M., Corley, B., Costello, L., Coulson, C., Crook, A., Crook, D.W., D'Arcangelo, S., Darby, M-A, Davis, J., de Koning, R., Derbyshire, P., Devall, P., Dolman, M., Draper, N., Driver, M., Dyas, S., Eaton, E., Edwards, J., Elderfield, R., Ellis, K., Ellis, G., Elwell, S., Evans, R., Evans, B., Evans, M., Eyre, D., Fahey, C., Fenech, V., Field, J., Field, A., Foord, T., Fowler, T., French, M., Fuchs, H., Gan, J., Gernon, J., Ghadiali, G., Ghuman, N., Gibbons, K., Gill, G., Gilmour, K., Goel, A., Gordon, S., Graham, T., Grassam-Rowe, A., Green, D., Gronert, A., Gumsley-Read, T., Hall, C., Hallis, B., Hammond, S., Hammond, P., Hanney, B., Hardy, V., Harker, G., Harris, A., Havinden-Williams, M., Hazell, E., Henry, J., Hicklin, K., Hollier, K., Holloway, B., Hoosdally, S.J., Hopkins, S., Hughes, L., Hurdowar, S., Hurford, S-A, Jackman, J., Jackson, H., Johns, R., Johnston, S., Jones, J., Kanyowa, T., Keating-Fedders, K., Kempson, S., Khan, I., Khulusi, B., Knight, T., Krishna, A., Lahert, P., Lampshire, Z., Lasserson, D., Lee, K., Lee, L.Y.W., Legard, A., Leggio, C., Liu, J., Lockett, T., Logue, C., Lucas, V., Lumley, S.F., Maripuri, V., Markham, D., Marshall, E., Matthews, P.C., Mckee, S., McKee, D.F., McLeod, N., McNulty, A., Mellor, F., Michel, R., Mighiu, A., Miller, J., Mirza, Z., Mistry, H., Mitchell, J., Moeser, M.E., Moore, S., Muthuswamy, A., Myers, D., Nanson, G., Newbury, M., Nicol, S., Nuttall, H., Nwanaforo, J.J., Oliver, L., Osbourne, W., Osbourne, J., Otter, A., Owen, J., Panchalingam, S., Papoulidis, D., Pavon, J.D., Peace, A., Pearson, K., Peck, L., Pegg, A., Pegler, S., Permain, H., Perumal, P., Peto, L., Peto, T.E.A., Pham, T., Pickford, H.L., Pinkerton, M., Platton, M., Price, A., Protheroe, E., Purnell, H., Rawden, L., Read, S., Reynard, C., Ridge, S., Ritter, T.G., Robinson, J., Robinson, P., Rodger, G., Rowe, C., Rowell, B., Rowlands, A., Sampson, S., Saunders, K., Sayers, R., Sears, J., Sedgewick, R., Seeney, L., Selassie, A., Shail, L., Shallcross, J., Sheppard, L., Sherkat, A., Siddiqui, S., Sienkiewicz, A., Sinha, L., Smith, J., Smith, E., Stanton, E., Starkey, T., Stawiarski, A., Sterry, A., Stevens, J., Stockbridge, M., Stoesser, N., Sukumaran, A., Sweed, A., Tatar, S., Thomas, H., Tibbins, C., Tiley, S., Timmins, J., Tomas-Smith, C., Topping, O., Turek, E., Neibler, T., Trigg-Hogarth, K., Truelove, E., Turnbull, C., Tyrrell, D., Vaughan, A., Vertannes, J., Vipond, R., Wagstaff, L., Waldron, J., Walker, P., Walker, A.S., Walters, M., Wang, J.Y., Watson, E., Webberley, K., Webster, K., Westland, G., Wickens, I., Willcocks, J., Willis, H., Wilson, S., Wilson, B., Woodhead, L., Wright, D., Xavier, B., Yelnoorkar, F., Zeidan, L., and Zinyama, R.

Abstract

Background Lateral flow device (LFD) viral antigen immunoassays have been developed around the world as diagnostic tests for SARS-CoV-2 infection. They have been proposed to deliver an infrastructure-light, cost-economical solution giving results within half an hour. Methods LFDs were initially reviewed by a Department of Health and Social Care team, part of the UK government, from which 64 were selected for further evaluation from 1st August to 15th December 2020. Standardised laboratory evaluations, and for those that met the published criteria, field testing in the Falcon-C19 research study and UK pilots were performed (UK COVID-19 testing centres, hospital, schools, armed forces). Findings 4/64 LFDs so far have desirable performance characteristics (orient Gene, Deepblue, Abbott and Innova SARS-CoV-2 Antigen Rapid Qualitative Test). All these LFDs have a viral antigen detection of >90% at 100,000 RNA copies/ml. 8951 Innova LFD tests were performed with a kit failure rate of 5.6% (502/8951, 95% CI: 5.1–6.1), false positive rate of 0.32% (22/6954, 95% CI: 0.20–0.48). Viral antigen detection/sensitivity across the sampling cohort when performed by laboratory scientists was 78.8% (156/198, 95% CI 72.4–84.3). Interpretation Our results suggest LFDs have promising performance characteristics for mass population testing and can be used to identify infectious positive individuals. The Innova LFD shows good viral antigen detection/sensitivity with excellent specificity, although kit failure rates and the impact of training are potential issues. These results support the expanded evaluation of LFDs, and assessment of greater access to testing on COVID-19 transmission. Funding Department of Health and Social Care. University of Oxford. Public Health England Porton Down, Manchester University NHS Foundation Trust, National Institute of Health Research.

Published
2021

37. The betaine-GABA transporter (BGT1, slc6a12) is predominantly expressed in the liver and at lower levels in the kidneys and at the brain surface.

Author

Zhou, Y., Holmseth, S., Hua, R., Lehre, A. C., Olofsson, A. M., Poblete-Naredo, I., Kempson, S. A., and Danbolt, N. C.

Abstract

The Na+- and Cl+-dependent GABA-betaine transporter (BGT1) has received attention mostly as a protector against osmolarity changes in the kidney and as a potential controller of the neurotransmitter GABA in the brain. Nevertheless, the cellular distribution of BGT1, and its physiological importance, is not fully understood. Here we have quantified mRNA levels using TaqMan real-time PCR, produced a number of BGT1 antibodies, and used these to study BGT1 distribution in mice. BGT1 (protein and mRNA) is predominantly expressed in the liver (sinusoidal hepatocyte plasma membranes) and not in the endothelium. BGT1 is also present in the renal medulla, where it localizes to the basolateral membranes of collecting ducts (particularly at the papilla tip) and the thick ascending limbs of Henle. There is some BGT1 in the leptomeninges, but brain parenchyma, brain blood vessels, ependymal cells, the renal cortex, and the intestine are virtually BGT1 deficient in 1- to 3-mo-old mice. Labeling specificity was assured by processing tissue from BGT1-deficient littermates in parallel as negative controls. Addition of 2.5% sodium chloride to the drinking water for 48 h induced a two- to threefold upregulation of BGT1, tonicity-responsive enhancer binding protein, and sodiummyo- inositol cotransporter 1 (slc5a3) in the renal medulla, but not in the brain and barely in the liver. BGT1-deficient and wild-type mice appeared to tolerate the salt treatment equally well, possibly because betaine is one of several osmolytes. In conclusion, this study suggests that BGT1 plays its main role in the liver, thereby complementing other betaine-transporting carrier proteins (e.g., slc6a20) that are predominantly expressed in the small intestine or kidney rather than the liver. [ABSTRACT FROM AUTHOR]

Published
2012
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44. Structure of Peripheral Cementum of Normal Equine Cheek Teeth.

Author

Mitchell, S. R., Kempson, S. A., and Dixon, P. M.

Subjects
EQUINE dentistry, TEETH, TRANSMISSION electron microscopy, DENTAL caries, PALATE, MICROSCOPY
Abstract

The structure of peripheral cementum of mandibular and maxillary cheek teeth was studied by gross observation, light microscopy, and scanning and transmission electron microscopy. Teeth from four horses aged 4. 8, 17. and 30- years-old were examined. The cementum of the occlusal surface was thicker on the buccal aspect when compared with the lingual aspect of mandibular teeth. The cementum of the occlusal surface was thicker on the palatal aspect when compared with the buccal aspect of maxillary teeth. There was no peripheral cementum on the interdental aspects of either mandibular or maxillary cheek teeth. In the adult tooth, cementum covered the crown and root surfaces. The peripheral cementum of the gingival region showed a dramatic increase In thickness compared with cementum covering the alveolar portion of the embedded tooth. At a microscopic level, three layers (primary, secondary, and tertiary) were identified within cementum. The increase in cementum in the gingival region was of tertiary cementum. All three layers contained vital cementocytes. There was a well-developed vascular system within the cementum. Nerve bundles were also present Th-ee cementoblast profiles were identified at the junction of the cementum with the periodontal ligament The results reported in this paper show that cementum is a dynamic vital tissue. These findings should contribute to a greater understanding of the etiology and pathogenesis of cemental caries and periodontal disease in the horse. [ABSTRACT FROM AUTHOR]

Published
2003
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47. NAD+-dependent ADP-ribosyltransferase in renal brush-border membranes

Author

Kempson, S. A. and Curthoys, N. P.

Abstract

Oxidized nicotinamide adenine dinucleotide (NAD+) in cytosol may interact with renal brush-border membranes (BBM) and inhibit BBM phosphate transport. The possible mechanism of interaction was investigated in the present study. Incubation of BBM with [adenine-3H]NAD+ led to acid-stable binding of 3H to the BBM, in contrast there was no binding of 14C when [carbonyl-14C]NAD+ was used. The data are consistent with an ADP-ribosylation mechanism involving transfer of ADP-ribose from NAD+ to BBM. This was confirmed by using [adenylate-32P]NAD+ and by the release of bound 32P in the form of 5'-[32P]AMP when the BBM were treated with snake venom phosphodiesterase. After gradient centrifugation of BBM the ADP-ribosyltransferase was recovered at the same density as known BBM enzymes, indicating that ADP-ribosyltransferase is an intrinsic BBM component and not a contaminant. These findings indicate that cytosolic NAD+ may be used for ADP-ribosylation of BBM proteins and that this may be a mechanism for regulating the BBM phosphate transport system.

Published
1983
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48. Specific inhibition of rat renal Na+/phosphate cotransport by picolinamide.

Author

Campbell, P I, al-Mahrouq, H A, Abraham, M I, and Kempson, S A

Abstract

Nicotinamide is both a precursor for NAD synthesis and an inhibitor of intracellular NAD hydrolysing enzymes. Overnight treatment of rats with nicotinamide causes dose-dependent inhibition of the Na+/phosphate cotransporter in the renal brush border membrane. Picolinamide is an isomer of nicotinamide that cannot be used for NAD synthesis. Picolinamide was used in the present study to explore the possibility that inhibition of Na+/phosphate cotransport may be related to inhibition of NAD hydrolyzing enzymes. Overnight treatment of rats with picolinamide, administered as a single injection (4 mmol/kg), inhibited Na+/phosphate cotransport by isolated renal brush border membrane vesicles. Like nicotinamide, the inhibition by picolinamide occurred in thyroparathyroidectomized rats, was specific for Na+/phosphate cotransport and was accompanied by a decrease in the apparent Vmax. In contrast to nicotinamide, there was only a small increase (1.5-fold) in renal cortical NAD content after picolinamide treatment. Direct incubation of isolated proximal tubules with thymidine, a potent inhibitor of NAD hydrolysis by intracellular enzymes, produced no change in Na+/phosphate cotransport. Thus, specific inhibition of renal Na+/phosphate cotrasport by picolinamide in vivo is unlikely due to inhibition of NAD hydrolyzing enzymes. It is suggested, based on data from in vitro studies, that a cyclic AMP-dependent mechanism may be involved.

Published
1989

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