Search

Your search keyword '"Potter, B."' showing total 1,014 results
Start Over Author "Potter, B." Language english
1,014 results on '"Potter, B."'

8. Cell fate following irradiation of MDA-MB-231- and MCF-7 breast cancer cells pre-exposed to a tetrahydroisoquinoline sulfamate microtubule disruptor

Author

Hargrave, SD, Joubert, AM, Potter, B, Dohle, W, Marais, S, and Mercier, AE

Abstract

Atetrahydroisoquinoline (THIQ) core is able to mimic the A and B rings of 2-methoxyestradiol (2ME2), an endogenous estrogen metabolite that demonstrates promising anticancer properties primarily by disrupting microtubule dynamic instability parameters, but has very poor pharmaceutical properties that can be improved by sulfamoylation. The nonsteroidal THIQ-based microtubule disruptor 2-(3-bromo-4,5-dimethoxybenzyl)-7-methoxy-6-sulfamoyloxy-1,2,3,4-tetrahydro isoquinoline (STX3451), with enhanced pharmacokinetic and pharmacodynamic profiles, was explored for the first time in radition biology. We investigated whether 24 h pre-treatment with STX3451 could pre-sensitize MCF-7 and MDA-MB-231 breast cancer cells to radiation. This regimen showed a clear increase in cytotoxicity compared to the individual modalities, results that were contiguous in spectrophotometric analysis, flow cytometric quantification of apoptosis induction, clonogenic studies and microscopy techniques. Drug pre-treatment increased radiation-induced DNA damage, with statistically more double-strand (ds) DNA breaks demonstrated. The latter could be due to the induction of a radiation-sensitive metaphase block or the increased levels of reactive oxygen species, both evident after compound exposure. STX3451 pre -exposure may also delay DNA repair mechanisms, as the DNA damage response element ataxia telangiectasia mutated (ATM) was depressed. These in vitro finding s may translate into in vivo models, with the ultimate aim of reducing both radiation and drug doses for maximal clinical effect with minimal adverse effects.

Published
2022
Full Text
View/download PDF

14. Predictors and impact of postoperative atrial fibrillation following thoracic surgery: a state‐of‐the‐art review.

Author

Diallo, E.‐H., Brouillard, P., Raymond, J.‐M., Liberman, M., Duceppe, E., and Potter, B. J.

Subjects
ATRIAL fibrillation, THORACIC surgery, BRAIN natriuretic factor, CONGESTIVE heart failure, LEFT heart atrium
Abstract

Summary: This review of 19 studies (39,783 patients) of atrial fibrillation after thoracic surgery addresses the pathophysiology, incidence, and consequences of atrial fibrillation in this population, as well as its prevention and management. Interestingly, atrial fibrillation was most often identified in patients not previously known to have the disease. Rhythm control with amiodarone was the most commonly used treatment and nearly all patients were discharged in sinus rhythm. Major predictors were age; male sex; history of atrial fibrillation; congestive heart failure; left atrial enlargement; elevated brain natriuretic peptide level; and the invasiveness of procedures. Overall, patients with atrial fibrillation stayed 3 days longer in hospital. We also discuss the importance of standardising research on this subject and provide recommendations that might mitigate the impact postoperative atrial fibrillation on hospital resources. [ABSTRACT FROM AUTHOR]

Published
2023
Full Text
View/download PDF

26. Inositol pyrophosphates drive sodium-potassium pump degradation by relieving an autoinhibitory domain of PI3K p85α

Author

Chin, A, Gao, Z, Riley, A, and Potter, B

Abstract

Sodium/potassium-transporting adenosine triphosphatase (Na+/K+-ATPase) is one of the most abundant cell membrane proteins and is essential for eukaryotes. Endogenous negative regulators have long been postulated to play an important role in regulating the activity and stability of Na+/K+-ATPase, but characterization of these regulators has been elusive. Mechanisms of regulating Na+/K+-ATPase homeostatic turnover are unknown. Here, we report that 5-diphosphoinositol 1,2,3,4,6-pentakisphosphate (5-InsP7), generated by inositol hexakisphosphate kinase 1 (IP6K1), promotes physiological endocytosis and downstream degradation of Na+/K+-ATPase-α1. Deletion of IP6K1 elicits a twofold enrichment of Na+/K+-ATPase-α1 in plasma membranes of multiple tissues and cell types. Using a suite of synthetic chemical biology tools, we found that 5-InsP7 binds the RhoGAP domain of phosphatidylinositol 3-kinase (PI3K) p85α to disinhibit its interaction with Na+/K+-ATPase-α1. This recruits adaptor protein 2 (AP2) and triggers the clathrin-mediated endocytosis of Na+/K+-ATPase-α1. Our study identifies 5-InsP7 as an endogenous negative regulator of Na+/K+-ATPase-α1.

Published
2020

35. Irish Association for Cancer Research: Proceedings of annual scientific meeting held at Kinsale on April 15–16th, 1994

Author

Lawler, M., Locasciulli, A., Bacigalupo, A., Humphries, P., Ljungman, P., McCann, S. R., Nolan, N., McDermott, E. W., Reynolds, J. R., McCann, A., Rafferty, R., Sweeney, P., Carney, D., O’Higgins, N. J., Duffy, M. J., Gardiner, C., Reen, D. J., O’Connell, M. A., Kelleher, D., Hall, N., O’Neill, L. A. J., Long, A., McCarthy, J. V., Fernandes, R. S., Cotter, T. G., Ryan, E., Kitching, A., MacMathuna, P., Mulligan, E., Merriman, R., Dervan, P., Kelly, P., Gorey, T. F., Lennon, J. R., Crowe, J., Bennett, M. A., Kay, E. W., Curran, B., O’Donoghue, D. P., Leader, M., Croke, D. T., O’Connor, J. M., McKelvey-Martin, V. J., McKenna, P. G., O’Riordan, J. M., Tobin, A., O’Mahoney, M., Keogh, F. M., O’Riordan, J., McNamara, C., McEneaney, P., Daly, P. A., Farrell, M., Young, S., Gibbons, D., McCarthy, P., Mulcahy, H., Parfrey, N. A., Sheahan, K., Lambkin, H., Mothersill, C., Chin, D., Sheehan, K., Kelehan, P., Parfrey, N., Morrin, M., Khan, F., Delaney, P., Rowan, D. M., Orminston, W. J., Donnellan, P. P., Khalid, A., Kerin, M., O’Hanlon, D. M., Kent, P., Given, H. F., Kennedy, S. M., McGeoch, G., Spurr, N. K., Barrett, J., O’Sullivan, G., Collins, J. K., Willcocks, T., Kennedy, S., Dolan, J., Gallagher, W., McDermott, E., O’Higgins, N., Hagan, R., McManus, R., Ormiston, W., Daly, P., Sheils, O., McDermott, M., O’Briain, D. S., Maher, D., Costello, P., Flanagan, F., Stack, J., Ennis, J., Grimes, H., Yanni, A., Harrison, M., Lowry, W. S., Russell, S. E. H., Atkinson, R. J., White, P., Hickey, I., Bell, D. W., Biggart, D., Doyle, J., Staunton, M. J., Gaffney, E. F., Dervan, P. A., McCabe, M. M., Fennelly, J. J., Carney, D. N., O’Reilly, M., McMahon, J. N., Moriarty, M., Hurson, B., O’Neill, A. J., Magee, H., O’Loughlin, J., Dervan, P. A., Cremin, P., Orminston, W., McCarthy, J., Redmond, P., Duggan, S., Rea, S., Bouchier-Hayes, D., O’Donnell, J., Duggan, C., Crown, J., Bermingham, D., Nugent, A., Fleming, C., Crosby, P., Wolff, S., McCarthy, D., Walsh, C. Barry, Cassidy, M., Husain, S., Kay, E., Thornhilll, M., Whelan, D., Barry, D., Turner, M., Prenderville, W., Murphy, F., Prendiville, W., Gibson, G., O’Grady, T., Carmody, M., Donohoe, J., Walshe, J., Murphy, G. M., O’Donoghue, J., Kerin, K., Ahern, S., Molloy, K., Goulden, N., Pamphilon, D. H., O’Connell, M., Power, C., Leroux, A., Perricaudet, M., Walls, D., Britton, F., Brennan, L., Barnett, Y. A., Madden, B., Wakelin, L. P. G., Loughrey, H. C., Corley, P., Redmond, H. P., Watson, R. W. G., Keogh, I., O’Hanlon, D., Walsh, S., Callaghan, J., McNamara, M., Benedict-Smith, A., Barnes, C., Neylon, D., Fenton, M., Searcey, M., Topham, C. M., Wakelin, L. G., Howarth, N. M., Purohit, A., Reed, M. J., Potter, B. V. L., Hatton, W. J., McKerr, G., Harvey, D., Carson, J., Hannigan, B. M., McCarthy, P. J., McClean, S., Hill, B. T., Costelloe, C., Denny, W. A., Fingleton, B., McDonnell, S., Butler, M., Corbally, N., Dervan, P. A., Stephens, J. F., Martin, G., McGirl, A., Lawlor, E., Gardiner, N., Lynch, S., Arce, M. de, O’Brien, F., Duggan, A., O’Herlihy, S., Shanahan, F., O’Keeffe, G., McCann, S., Sweeney, K., Neill, A. O., Pamphilon, D., Sheridan, M., Reid, I., Seymour, C. B., Walshe, T., Hennessy, T. P., O’Mahony, A., O’Connell’, J., Lawlor, C., Nolan, S., Morrisey, D., Pedlow, P. J., Walsh, M., Lowry, S. W., McAleer, J. J. A., McKeown, S. R., Afrasiabi, M., Lappin, T. R. J., Joiner, B., Hirst, K. V., Hirst, D. G., Sweeney, E., VanderSpek, J., Murphy, J., and Foss, F.

Published
1995
Full Text
View/download PDF

39. Abstracts of papers clinical pharmacological meeting

Author

van der Klauw, M. M., Stricker, B. H. Ch., Ottervanger, J. P., van der Meché, F. G. A., van Griensven, J. M. T., Lemkes, H. H. P. J., Kroon, J. M., Schoemaker, H. C., Cohen, A. F., Schellens, J. H. M., Loos, W., van Acker, B., de Boer-Dennert, M., Planting, A. S. T., van der Burg, M. E. L., Stoter, G., Krediet, R., Verweij, J., Blaak, E. E., van Baak, M. A., Kemerink, G. J., Pakbiers, M. T. W., Heidendal, G. A. K., Saris, W. H. M., Bouckaert, S., Vakaet, L., Dhont, M., Remon, J. P., van den Broek, S. A. J., de Graeff, P. A., van Gilst, W. H., van Veldhuisen, D. J., Hillige, H. L., Wesseling, H., Lie, K. I., Gaillard, C. A., van Es, P. N., de Leeuw, P. W., Van Bortel, L. M. A. B., Kool, M. J. F., Lustermans, F. A. T., Breed, J. G. S., Hoeks, A. P. G., Boudier, H. A. J. Struijker, Pickkers, R. P., Smits, P., Baadenhuysen, H., van 't Laar, A., Thien, Th., Elseviers, M. M., De Broe, M. E., van der Ven, A. J. A. M., Koopmans, P. P., Peters, W. H. M., Vree, T. B., van der Meer, J. W. M., Snoeck, E., Van Peer, A., Sack, M., Horton, M., Mannens, G., Woestenborghs, R., Heykants, J., Meibach, R., van Witsen, T. B., Valkenburg, H. A., Vander Stichele, R. H., De Potter, B., Vyncke, P., Bogaert, M. G., Burggraaf, J., Wollersheim, H., van Aalen, J., Schoemaker, R. G., Du, X. Y., Bax, W. A., Bos, E., Saxena, P. R., Rongen, G. A., van Heiningen, P. N. M., Schwietert, H. R., Kortboyer, J. M., Sollie, F. A. E., Piraube, C., Desché, P., Jonkman, J. H. G., Blok, W. L., Gyssens, I. C., Hekster, Y. A., Koopmans, P. P., van der Meer, J. W. M., Jansen P. A. F., Sival R. C., van Nieuwkerk J. F., Klaverwiiden B., de Bruijn, E. A., and Driessen, O.

Published
1993
Full Text
View/download PDF

47. Inositol hexakisphosphate increases the size of platelet aggregates

Author

Brehm, M, Klemm, U, Rehbach, C, Erdmann, N, Kolšek, K, Lin, H, Aponte-Santamaría, C, Gräter, F, Rauch, B, Riley, A, Mayr, G, Potter, B, and Windhorst, S

Subjects
Platelets, Blood Platelets, Aggregation, Phytic Acid, Platelet Aggregation, Inositol hexakisphosphate, Fibrinogen, Humans, Article, Protein Structure, Secondary, ComputingMethodologies_COMPUTERGRAPHICS
Abstract

Graphical abstract, The inositol phosphates, InsP5 and InsP6, have recently been identified as binding partners of fibrinogen, which is critically involved in hemostasis by crosslinking activated platelets at sites of vascular injury. Here, we investigated the putative physiological role of this interaction and found that platelets increase their InsP6 concentration upon stimulation with the PLC-activating agonists thrombin, collagen I and ADP and present a fraction of it at the outer plasma membrane. Cone and plate analysis in whole blood revealed that InsP6 specifically increases platelet aggregate size. This effect is fibrinogen-dependent, since it is inhibited by an antibody that blocks fibrinogen binding to platelets. Furthermore, InsP6 has only an effect on aggregate size of washed platelets when fibrinogen is present, while it has no influence in presence of von Willebrand factor or collagen. By employing blind docking studies we predicted the binding site for InsP6 at the bundle between the γ and β helical subunit of fibrinogen. Since InsP6 is unable to directly activate platelets and it did not exhibit an effect on thrombin formation or fibrin structure, our data indicate that InsP6 might be a hemostatic agent that is produced by platelets upon stimulation with PLC-activating agonists to promote platelet aggregation by supporting crosslinking of fibrinogen and activated platelets.

Published
2018

Catalog

Books, media, physical & digital resources
See catalog results