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2. Simulating human interactions in supermarkets to measure the risk of COVID-19 contagion at scale

Author

Plata, Serge, Sarma, Sumanas, Lancelot, Melvin, Bagrova, Kristine, and Romano-Critchley, David

Subjects
Computer Science - Distributed, Parallel, and Cluster Computing, Computer Science - Multiagent Systems, 00A69
Abstract

Taking the context of simulating a retail environment using agent based modelling, a theoretical model is presented that describes the probability distribution of customer "collisions" using a novel space transformation to the Torus $Tor^2$. A method for generating the distribution of customer paths based on historical basket data is developed. Finally a calculation of the number of simulations required for statistical significance is developed. An implementation of this modelling approach to run simulations on multiple store geometries at industrial scale is being developed with current progress detailed in the technical appendix., Comment: 23 pages, 11 figures

Published
2020

3. Loss of mouse cardiomyocyte talin-1 and talin-2 leads to β-1 integrin reduction, costameric instability, and dilated cardiomyopathy

Author

Manso, Ana Maria, Okada, Hideshi, Sakamoto, Francesca M, Moreno, Emily, Monkley, Susan J, Li, Ruixia, Critchley, David R, and Ross, Robert S

Subjects
Biochemistry and Cell Biology, Medical Physiology, Biomedical and Clinical Sciences, Biological Sciences, Heart Disease, Cardiovascular, Aetiology, 2.1 Biological and endogenous factors, Animals, Cardiomyopathy, Dilated, Integrin beta1, Mice, Myocardium, Myocytes, Cardiac, Talin, talin, costameres, cardiomyopathy, heart, integrins
Abstract

Continuous contraction-relaxation cycles of the heart require strong and stable connections of cardiac myocytes (CMs) with the extracellular matrix (ECM) to preserve sarcolemmal integrity. CM attachment to the ECM is mediated by integrin complexes localized at the muscle adhesion sites termed costameres. The ubiquitously expressed cytoskeletal protein talin (Tln) is a component of muscle costameres that links integrins ultimately to the sarcomere. There are two talin genes, Tln1 and Tln2. Here, we tested the function of these two Tln forms in myocardium where Tln2 is the dominant isoform in postnatal CMs. Surprisingly, global deletion of Tln2 in mice caused no structural or functional changes in heart, presumably because CM Tln1 became up-regulated. Tln2 loss increased integrin activation, although levels of the muscle-specific β1D-integrin isoform were reduced by 50%. With this result, we produced mice that had simultaneous loss of both CM Tln1 and Tln2 and found that cardiac dysfunction occurred by 4 wk with 100% mortality by 6 mo. β1D integrin and other costameric proteins were lost from the CMs, and membrane integrity was compromised. Given that integrin protein reduction occurred with Tln loss, rescue of the phenotype was attempted through transgenic integrin overexpression, but this could not restore WT CM integrin levels nor improve heart function. Our results show that CM Tln2 is essential for proper β1D-integrin expression and that Tln1 can substitute for Tln2 in preserving heart function, but that loss of all Tln forms from the heart-muscle cell leads to myocyte instability and a dilated cardiomyopathy.

Published
2017

9. Extending the Kohonen self-organising map by use of adaptive parameters and temporal neurons

Author

Critchley, David A.

Subjects
006.3
Abstract

This work extends the Kohonen self-organising map in two primary ways: o A dynamic extension to the model which allows the neighbourhood size and learning rate timecourse to be deduced during learning. o Inclusion of temporal features, both in single layer and hierarchical networks. The dynamic learning parameter model is developed as a consequence of how the self-organising map forms 'stable states' under fixed values of the learning parameters whilst exposed to a driving probability distribution. Such stable states can be used to deduce an appropriate stage to make a transition to a new set of learning parameters. This leads to a sequence of states that ultimately result in convergence. Temporal features are developed in the light of the Temporal Kohonen Map model of Chappell and Taylor. It is shown that application of the standard Kohonen learning law to such a network can lead to instability in the weightspace. This problem is shown to be soluble by moving the integrating characteristics from the cell body (where it is a scalar quantity) to the synapses (where it is a vector quantity). Multilayer temporal topographic mappings are discussed in terms of coding strategies between layers. The codings examined include complete feed-forward, feed-forward with enforced output spectrum and 'triangular coding', a binary coding of topology.

Published
1994

11. Tensin3 interaction with talin drives the formation of fibronectin-associated fibrillar adhesions

Author

Atherton, Paul, primary, Konstantinou, Rafaella, additional, Neo, Suat Peng, additional, Wang, Emily, additional, Balloi, Eleonora, additional, Ptushkina, Marina, additional, Bennett, Hayley, additional, Clark, Kath, additional, Gunaratne, Jayantha, additional, Critchley, David, additional, Barsukov, Igor, additional, Manser, Edward, additional, and Ballestrem, Christoph, additional

Published
2022
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14. Veteran Adherence to Oral Versus Injectable Alcohol Use Disorder Medication Treatment

Author

Dorflinger, Charles, Carey, Heather, Roche, Jennifer, Burant, Christopher, LeHew, Colleen, Stewart, Hayden, Mitchell, Brian, Ayanga, Daniel, Walder, Annette, Cooler, Jordan, Wu, Shuwen, Frey, Theresa, Wenthur, Cody, Burk, Bradley, Ward, Alex, Clark, Brooke, Leung, Jonathan G, Kutzke, Jade, May, Heather P, Maehler, Colin, Kummer, Bethany, Hamner, Jennifer, Ariefdjohan, Merlin, Stutzman, Danielle L, Kicklighter, Jackson, Musco, Shaina, Singson, Grace Marielle, Pamintuan, Claire, Francisco, Janelle, Phan, Tam, Sevak, Rajkumar J, Rogan, Edward L, Kehoe, William A, Halliwell, Robert F, Kanter, Joel, Ryan, Holly, Patel, Krupa, Moukaddam, Nidal, Saunders, John, Fernandez, Luis, Shah, Asim, Wong, Jerry, Erowele, Goldina, Ruppelt, Sara, Tillery, Erika E, Baker, Joni, Loflin, Bobbi Jo, Gray, Emily, Conley, Giulia, Hembree, Amanda, Sterling, Jacyntha, Buige, Ashley N, Nguyen, Mimi, Harris, Suzanne C, Bhavsar, Nisha, Shah, Niti, Lee, Bona, Jeong, Seoyoung, Maroney, Megan E, Whalen, Eric D, Maloney, Rebecca M, Hagemeier, Nicholas E, Takamura, Kay, Rice, Amanda G, Furbish, Amelia B, Hebbard, Amy M, Ross, Clint, Cumbie, Holly, Hickey, J. Scott, Lalani, Falak, Mucha, Hannah, Saklad, Stephen R, Ma, Connie, Lee, Kelly, O’Donnell, Carolyn, Jackson, Sarah, Albee, Jennifer Nelson, Yapel, Ann, Nash, Cynthia, MacDonald, Danielle, King, Amelia, Schneiderhan, Mark, Hager, Keri, Bell Lynum, Karimah S, Nash, Abigail, Fu, Dong Jing, Ionescu, Dawn F, Sliwa, Jennifer Kern, Turkoz, Ibrahim, Dorson, Peter G, Canuso, Carla, Hsia, Stephanie, Nguyen, Julie, La, Amenda, Gruenberg, Katherine, MacDougall, Conan, Brockbank, Josh, Wong, Kara, Schultz, Erica, Pinchinat, Jessica, Thibeaux, Taylor M, McCants, Tamara, Lam, Jason, Diaz-Luna, Jose, Nguyen, Jennifer, Yokoyama, Melissa, Albiar, Olivia, Bradley, Bridget, Popish, Sarah J, Bounthavong, Mark, Lau, Marcos K, Wells, Daina L, Kay, Chad L, Harvey, Michael A, Himstreet, Julianne E, Christopher, Melissa L.D, Weeda, Erin R, McGraw, Daniel J, Gonzalez, Misty L, Pardo-Pfeiffer, Carlos, Rodeghiero, Abigail, Zhang, Lusi, Brown, Sarah Jane, Shan, Yuting, Lee, Adam M, Allen, Josiah D, Eum, Seenae, Bishop, Jeffrey R, Gonzalez, Rolando, Wahl, Kimberly, Naglich, Andrew, Ayson, Marl, Thomas, Kelan, Renfro, Mandy L, Loera, Lindsey J, Hill, Lucas G, Tirado, Carlos, Delerme, Dante, Dean, Taylor, Cullen, Marissa, Straley, Craig M, Carr, Chelsea N, Sun, Wendy, Alzouby, Hiba, Harris, Suzanne, Banker, Christopher M, Cook, Sarah F, Muir, Justin, Brodie, Daniel, Cremers, Serge, Bies, Robert R, Dzierba, Amy L, Moton, Robert, Saklad, Stephen, Ferris, Ryan E, Noble, Brie N, Hartung, Daniel M, Tjia, Jennifer, Furuno, Jon P, Ibrahim, Hajer, Duong, Dat, Malcolm, Benjamin, Gogineni, Hyma P, Zahn, Amy L, Alibeckoff, Chloe C, Connor, Sharon, Buranosky, Raquel, Livezey, Sabrina N, Daniell, Jessica, DeClercq, Josh, Choi, Leena, Zuckerman, Autumn, Shah, Nisha B, Kang, Ashley, Anksorus, Heidi, Troglin, Courtney G, Bouldin, J. Brooke, Schreiner, Shannon, McKinney, Mariah, Brown, Stacy D, Pond, Brooks B, Nguyen, Thu, Chin, Hyun Ji, Dambly, Nicolle, Augsten, Alberto, Themas, Samantha, Vicencio, Claudia, Horner, Caroline, Covert, Kelly, Lewis, Paul, Tharp, Jen, Sommi, Roger W, Bidollari, Ilda, Still, Daniel, Du, Yangchun, Yagoda, Sergey, Weiden, Peter J, Long, Katelyn, Vandiver, Emily, Johnson, Stephanie, Darazs, Brooks, Tillery, Erika, Silvia, Richard J, Lee, Kelly C, Bien, Ivy, Farahmand, Khodayar, Goldsmith, Hannah, Farrar, Mallory, Le, Hadley, Huynh, Quynh, Kim, Jane, McCausland, Kristen, Haider, Batool, White, Michelle K, O’Sullivan, Amy K, Rychlec, Kaitlin, Akerman, Sarah, Fratantonio, James, Saxon, Andrew, Thase, Michael E, Parikh, Sagar V, Maheshwari, Priya, Rothschild, Anthony J, Dunlop, Boadie W, DeBattista, Charles, Conway, Charles R, Forester, Brent P, Shelton, Richard C, Macaluso, Matthew, Brown, Krystal, Li, James, Jablonski, Michael R, Greden, John F, Gidal, Barry, Patsalos, Philip, Szaflarski, Jerzy, VanLandingham, Kevan, Critchley, David, Morrison, Gilmour, Weiss, Catherine, Meehan, Stine Rasmussen, Ouyang, John, Hobart, Mary, Rowe, William, Vanover, Kimberly E, Kane, John M, Satlin, Andrew, Durgam, Suresh, Davis, Robert E, Mates, Sharon, Correll, Christoph U, Tamminga, Carol, Rabon, Hannah, Smith, Jordan, Squires, Karrie, VanDaele, Madeline, Logan, Linda D, Zhang, Feng, DeSousa, Norberto J, Sallee, F. Randy, Lickrish, David, Incledon, Bev, Smith, Joseph L, Candon, Molly, Fadeyibi, Oluwatoyin, Connolly, K. Ryan, Lim, Suet, Neimark, Geoffrey, Mandell, David, Newcomer, John W, Silverman, Bernard, DiPetrillo, Lauren, Graham, Christine, Jiang, Ying, Simmons, Adam, Hopkinson, Craig, McDonnell, David, Kahn, Rene, King, Thomas R, Kando, Judith C, Pardo, Antonio, King, Thomas, Edwards, John B, Chen, Richard, Huo, Jason, Cutler, Andrew J, Fawver, Jay, Flanagan, Mindy, Smith, Thomas, Drouin, Michelle, Mirro, Michael, Yatham, Lakshmi N, Vieta, Eduard, McIntyre, Roger S, Jain, Rakesh, Earley, Willie R, Patel, Mehul, Brown, Lisa, Sehgal, Rahul, Yu, Ken, Al Habbab, Talal, Johnson, Holly, Dechairo, Bryan, Chen, Jack J, Singer, Carlos, Marder, Stephen R, Comella, Cynthia L, Shah, Chirag, Jimenez, Roland, Goodwin, Heather, Morrow, Gina, Tewksbury, Ashley, Waters, Kristin, Eggert, Robyn, Tallian, Kimberly, Sepulveda, Joe A, Rojas, Sarah, Sikand, Harminder, Sutera, Nathan, Iuppa, Courtney A, Nelson, Leigh Anne, Kriz, Carrie R, Burns, Nicole A, Lang, Shelby E, Elliott, Ellie S.R, Luong, Uyen, Elsobky, Teresa, Abelleira, Audrey, Awan, Sundus, Dume, Roberta, Dilich, Adam, Anderson, Mikaela, Park, Priscilla, Moehnke, Austin, Aebi, Cydreese, Feighner, Lydia, Vernon, Martein, Streit, Jessica, Kauer, Jill, Lemons, Amber, Diefenderfer, Lauren A, Moon, Joseph, Smith, Jordan O, Franck, Hugh A, Randle, C. Hope, Hedgepeth Kennedy, M. Lindsey, James, Shannon, Coplan, Benjamin, Ruekert, Laura, Puri, Shilpa, Yeleti, Ramya, Cathright, Sela, Coveart, Stephanie, Regen, Sloan, Stewart, Shannon, Stratton, Miranda, Haight, Robert, Hoeft, Dawn, Bishop, Danielle, De La Cruz, Austin, Aurelio, Mariellee, Prestenback, Autumn, Price, Paul L, Makuch, Christian X, Salisbury, Nicole M, Koch, Jessa, Palmer, Melissa C, Chace, Ashley, Price, Cristofer, Putney, Jessica, Khan, Fatima, Huntsman, Amanda, Hutcheson, Brooklyn, Hightower, Sharae, Ott, Carol A, Scott, Catherine, Balser, Amanda, Karas, Andrew, Hsu, Michael, Malin, Maureen, Robert, Sophie, Leung, Edwina, Mierzwa, Mark, Kay, Lehua, Bowling, Dalia, Allen, Sabrina, Weingartner, Melissa, Ventricelli, Daniel, Santa, Heather, Nowalk, Alexandra, Downs, George, Le, N, Mospan, C, Burton, Caitlin, Mathys, Monica, Gutierrez, Erika, Ali, Sarah, Chang, Joni, Holzum, Dorothy N, Griffith, June A, Morgan, Katherine T, Laguado, S. Andrea, Steavenson, Rosana, Mehvar, Mina, Bechtold, Carson L, Kim, Heesoo, Dopheide, Julie Ann, Anderson, Lindsey, Kleyn, Thomas, DiRenzo, Baely, Walroth, Todd, Adamczyk, Raechel, Kendrick, Jenna, Thomas, Christopher, Mailloux, Lindsay M, Haas, Matthew T, Larew, Janel M, Stohs, Matthew E, DeJongh, Beth M, Satow, Britney A, Titus-Lay, Erika, Clark, Suzanne, Dike, Dozie, Pinsonnault, John, Gamber, Joy, Roseberry, Samantha, Mitchell, Brian G, Nguyen, Mai, Willborn, Robert, Roche-Desilets, Jennifer, Dailey, Alison, Ignatowski, Michael, Routhieaux, Melanie, Kawsky, Jaclyn, Stratman, Jennifer, Corboy, Alexander, Norberte, Cherisse, Gross, Tonya, Daniel, Jeremy, Tran, Aaron N, Wary, Megan, Kostric, Anna, Schaller, Samantha, Shin, Yunjung, Maroney, Megan, Hampton, Chanese, Krieger, Kelly, Hartwig, Rachel, Thamawatanakul, Rani, Wilbur, Eileen, Shofner, Steven, Butler, Justin, Moody, Breanna, Davis, Elizabeth, Hofammann, Elizabeth, Liveoak, Katie, Mitchell, McKinley, Lebrecht, Morgan, Hawley, Joanne, Smigiel, Joe, Radtke, Michelle, Walkerly, Autumn, King, Morgan, Wakefield, Andrew, Downs, Mona, Hudson, Nancy, Burghart, Steven, Reynoldson, Jill, Booth, Macey, Ishino, Risa, Lee, Tammie, Wright, Melissa, Boggs, Angela, Kaur, Rajandeep, Patel, Parth, Smith, Thomas R, Theriault, Sarah, Okusaga, Olaoluwa, Reinstatler, Kristina, Hawk, David, Rush, Stephen, Vachuska, Michaela, Powell, Elizabeth, Lacro, Jonathan, Chehovich, Charisse, Demler, Tammie Lee, deRosas, Andrea, Trigoboff, Eileen, Taylor, Aminah, Singh, Divita, Burdge, Gary, Reynolds, Jamie, Kriz, Carrie, Burns, Nicole, Sommi, Roger, Yabs, Melanie, Sarpal, Deepak, Fabian, Tanya, Bartos, Lindsey, Tallman, Kristin, Johnson, Dara, Taylor, Daniel, Hogan, Brendon, Kwan, Peter, Bast, Aubree, Sanchez, Apolinar, Maglalang, Patricia D, Scheible, Mahli M, Skurat, McKenzie K, Jackson, Sarah K, Belknap, Jazmin N, Ostfeld, Larissa, Fahy, Megan, Nguyen, Tuyen, Bui, Hoa, Little, Meg M, Seifert, Randall, Maister, Ashley, McCarthy, Caitlin, Burger, Emily, Mullen, Sandy, Cusimano, Joseph, VandenBerg, Amy, Duquette, Meghan, Guttenberg, Viktoria, Matsunaga, Candace, White, Shelby, Richard, Andrea, Jones, Jessica, Morgan, Kaitlyn, Kelsey, Taylor, Sartin, Carrie J, Rickert, Leah, Ferrill, Laine, Vallabh, Anuja, Jhawar, Archana, Barrett, Monica, Ward, Sarah, Colvard, Michelle, Phan, Joann, Preinitz, Jennifer, Ellis, Marcus, Gibu, Matthew, Kivlehan, Audrey, Chiulli, Dana, Rhodes, Kirby, Brewer, T. Amber, Richard, Michelle, Kirwan, Brigit, Flowers, Gary, Albritton, Melinda, Sutton, Caroline M, McEachern, Sydney, Miskle, Benjamin, Barr, Rachel, Thomas, Chris, Yang, Waverly, Vogt, Caitlin, Charles, Amanda, Mathews, Alisha, Bhandari, Deepali, Olsen, Emily, Garling, Ashley, Liszka, Jessica, Goodman, Courtney S, Smith, Tammy, Barron, Ana, Williams, Andrew, Zuloaga, Andrea, Parra, Brianne, Miller, Joy, Blake, Jennifer, Toney, Gregory, Galeano, Kathleen, Morabito, Brianna, Smith, Sydney, Miller, Lindsey, Fleisch, Sheryl, Kim, Erika, Kurz, Troy, Peterson, Angela M, Gruca, Justin, McGuire, Michael, Stummer, Lauren, Yip, Agustin, Rodriguez-Villa, Fernando, Wilson, Jennifer, Sutton, Caroline, Owings, R. Laney, Herbst, Claire, Hosmer, Kane, Wulff-Burchfield, Elizabeth, Ramion, Shelby, Brown, Lauren, Shishko, Ilona, Allen, Sarah, Nichols, Taylor, Fawcett, Janet, Trent, Kelley N, Eatmon, Courtney V, Hershberger, Allie, Roads, Mary, Pittenger, Amy L, Dadebo, Victoria, Tomko, John R, Simeone, Danielle, Sherwood, Devon A, Morgan, Katherine, White, C. Whitney, Holzum, Dorothy, Adetunji, Oluwaseyi, Blalock, Meredith, Snyder, Sabrina Domicoli, Kneebusch, Jamie, Mitchell, Melissa, Butala, Niyati, McHugh, Trisha, McGuire, J Michael, Moller, Karen, Melton, Brittany, Mitchell, Melissa M, Chaplin, Kyrsten, Canto, Samantha, Hang Vu, Thi Thuy, Rey, Jose A, Elmaoued, Amre Adel, Hopper, Jessica, Do, Annette, Leckband, Susan G, Abraham, Dana L, Haught, Emma J, Kobulinsky, Lawrence R, Fabian, Tanya J, Greenwood, Jessica, Rey, Jose, Chen, Emily, Farhadian, Sanaz, Smith, Austin M, Hopkins, Tiffany M, Deardorff, O. Greg, Jenne, Victoria, Wood, Joshua, Trout, Megan, Beck, Niels C, Pals, Hale, Frazier, Erica, Cavaliere, Vincent S, DiPaula, Bethany A, Glassman, Matthew, Wehring, Heidi J, Mackowick, Marie, Park, Jaeboon, Love, Raymond C, Kelly, Deanna L, Newbold, Mervan, Fioravanti, Nicole, Brown, Matthew J, Casey, Emily R, Nadkarni, Neha, Oh, Sarah, Patel, Romi, Riedley, Taylor, Mathis, Erin, Fadden, Patrick, Madden, Cristina, Schneiderhan, Mark E, Hintsala, Madelynn, Stenehjem, David, Rufus, Krystal M, Elhakim, Athar, Zolezzi, Monica, Elamin, Waad M, Homs, Shorouk, Qubaiah, Iman K, Mahmoud, Doaa A, Tawfik, Enge M, Fritz, Merideth, Alman, Brianne, Wartman, Carolanne, Clark, Megan, Ott, Carol, Rainey, Carly A, Mann, Elise, Modany, Madison, Schoettmer, Amanda, Buckley, Tiffany, Patwardhan, Vidisha, Boyle, Cynthia J, Gardner, Kristen N, Hamby, Kerri, Ngo, Nichol, Kim, Lila Q, Chen, Steven W, Mosley, Scott, Dadiomov, David, Goldstone, Lisa W, DellaVecchia, Matthew J, Cauffield, Jacintha, Grim, Hannah, Eschler, Anna, Aladeen, Traci, Blondell, Richard, Capote, Horacio, Rainka, Michelle, Lee, Ashley, Shelley, Maria, Stoncius, Kristina, Berry, Jonathan, Doroudgar, Shadi, Johnson, Kayla, Pouliot, Jonathon, Rarrick, Christine, Hebbard, Amy, Shikwana, Sara, Koller, Katherine, Reed, Ellen, Hoefling, Austin D, Miles, Talia M, Ansara, Elayne D, Titova, Viktoriya, Kandela, Dalea, Douglass, Amber R, Ehrhard, Kimberly, Stanley, Madison, Ganihong, Carissa, Liu, Mei T, Bohnenberger, Kristin, Zuber, Nicole, Plunkett, McKenzie, Axelrod, Chelsey, Lightfoot, Myaa, Moore, Miranda, Crouse, Ericka, Olazo, Muriel, Taormina, Stephanie, Reiss, Rebecca, Denno, Nora, Johnson, Braniesha, Wilkening, Gwendolyn Lucy, Andrews, Haley, Neumeister, Kristen, Murad, Muhammad Ubaidullah, Reid, Bailey, Franco, Ashley, Stutzman, Danielle, Jorgensen, Jennifer, Basit, Saadia, Jensen, Aimee, Nadal, Celeste N, Truong, Quynh-Nhu, Jameson, Melanie, Knox, Erin D, Bota, Robert G, Wieruszewski, Patrick M, and Leung, Sarah B

Subjects
CPNP Foundation Strategic Goals Award Finalists, Therapeutic Case Report Abstracts, Original Research Abstracts, Therapeutic Case Report Award Finalists, Article, Encore Presentation Abstracts, Work in Progress Abstracts, Neuropsychology and Physiological Psychology, Original Research Award Finalists, Research Trainee Award Finalists, Pharmacology (medical), Neurology (clinical), General Pharmacology, Toxicology and Pharmaceutics, Innovative Practices Abstracts, Innovative Practices Award Finalists, Scientific Posters
Published
2020

15. QoS-based multi-domain routing in public broadband networks

Author

Karali, Dora, Karayannis, Fotis, Berdekas, Klearchos, Reilly, James, Romano-Critchley, David, Goos, G., editor, Hartmanis, J., editor, van Leeuwen, J., editor, Trigila, Sebastiano, editor, Mullery, Al, editor, Campolargo, Mario, editor, Vanderstraeten, Hans, editor, and Mampaey, Marcel, editor

Published
1998
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17. Podocyte-associated talin1 is critical for glomerular filtration barrier maintenance

Author

Tian, Xuefei, Kim, Jin Ju, Monkley, Susan M., Gotoh, Nanami, Nandez, Ramiro, Soda, Keita, Inoue, Kazunori, Balkin, Daniel M., Hassan, Hossam, Son, Sung Hyun, Lee, Yashang, Moeckel, Gilbert, Calderwood, David A., Holzman, Lawrence B., Critchley, David R., Zent, Roy, Reiser, Jochen, and Ishibe, Shuta

Subjects
Cytoskeletal proteins -- Identification and classification -- Properties, Physiological research, Glomerular filtration rate -- Research, Health care industry
Abstract

Podocytes are specialized actin-rich epithelial cells that line the kidney glomerular filtration barrier. The interface between the podocyte and the glomerular basement membrane requires integrins, and defects in either [α.sub.3] or [β.sub.1] integrin, or the [α.sub.3][β.sub.1] ligand laminin result in nephrotic syndrome in murine models. The large cytoskeletal protein talin1 is not only pivotal for integrin activation, but also directly links integrins to the actin cytoskeleton. Here, we found that mice lacking talin1 specifically in podocytes display severe proteinuria, foot process effacement, and kidney failure. Loss of talin1 in podocytes caused only a modest reduction in [β.sub.1] integrin activation, podocyte cell adhesion, and cell spreading; however, the actin cytoskeleton of podocytes was profoundly altered by the loss of talin1. Evaluation of murine models of glomerular injury and patients with nephrotic syndrome revealed that calpain-induced talin1 cleavage in podocytes might promote pathogenesis of nephrotic syndrome. Furthermore, pharmacologic inhibition of calpain activity following glomerular injury substantially reduced talin1 cleavage, albuminuria, and foot process effacement. Collectively, these findings indicate that podocyte talin1 is critical for maintaining the integrity of the glomerular filtration barrier and provide insight into the pathogenesis of nephrotic syndrome., Introduction The glomerular filtration barrier is composed of podocytes and fenestrated endothelial cells separated by a glomerular basement membrane (GBM), which together function to filter plasma to generate urine devoid [...]

Published
2014
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24. Tensin3 interaction with talin drives formation of fibronectin-associated fibrillar adhesions

Author

Atherton, Paul, primary, Konstantinou, Rafaella, additional, Neo, Suat Peng, additional, Wang, Emily, additional, Balloi, Eleonora, additional, Ptushkina, Marina, additional, Bennett, Hayley, additional, Clark, Kath, additional, Gunaratne, Jayantha, additional, Critchley, David, additional, Barsukov, Igor, additional, Manser, Edward, additional, and Ballestrem, Christoph, additional

Published
2021
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31. Rapid leukocyte migration by integrin-independent flowing and squeezing

Author

Lammermann, Tim, Bader, Bernhard L., Monkley, Susan J., Worbs, Tim, Wedlich-Soldner, Roland, Hirsch, Karin, Keller, Markus, Forster, Reinhold, Critchley, David R., Fassler, Reinhard, and Sixt, Michael

Subjects
Myosin, Muscle proteins, Integrins, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

All metazoan cells carry transmembrane receptors of the integrin family, which couple the contractile force of the actomyosin cytoskeleton to the extracellular environment. In agreement with this principle, rapidly migrating leukocytes use integrin-mediated adhesion when moving over two-dimensional surfaces. As migration on two-dimensional substrates naturally overemphasizes the role of adhesion, the contribution of integrins during three-dimensional movement of leukocytes within tissues has remained controversial. We studied the interplay between adhesive, contractile and protrusive forces during interstitial leukocyte chemotaxis in vivo and in vitro. We ablated all integrin heterodimers from murine leukocytes, and show here that functional integrins do not contribute to migration in three-dimensional environments. Instead, these cells migrate by the sole force of actin-network expansion, which promotes protrusive flowing of the leading edge. Myosin II-dependent contraction is only required on passage through narrow gaps, where a squeezing contraction of the trailing edge propels the rigid nucleus., The current model of metazoan cell migration is frequently described as a multistep cycle: F-actin polymerization at the cell front pushes out a membrane protrusion that subsequently becomes anchored to [...]

Published
2008
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32. Loss of PIP5KI[gamma], unlike other PIP5KI isoforms, impairs the integrity of the membrane cytoskeleton in murine megakaryocytes

Author

Wang, Yanfeng, Litvinov, Rustem I., Chen, Xinsheng, Bach, Tami L., Lian, Lurong, Petrich, Brian G., Monkley, Susan J., Critchley, David R., Sasaki, Takehiko, Birnbaum, Morris J., Weisel, John W., Hartwig, John, and Abrams, Charles S.

Subjects
Bone marrow cells -- Physiological aspects, Bone marrow cells -- Research, Cell membranes -- Physiological aspects, Cell membranes -- Research, Phosphatidylinositol -- Physiological aspects, Phosphatidylinositol -- Health aspects, Phosphatidylinositol -- Research
Abstract

Phosphatidylinositol-4,5-bisphosphate ([PIP.sub.2]) is an abundant phospholipid that contributes to second messenger formation and has also been shown to contribute to the regulation of cytoskeletal dynamics in all eukaryotic cells. Although the [alpha], [beta], and [gamma] isoforms of phosphatidylinositol-4-phosphate-5-kinase I (PIP5KI) all synthesize PIP2, mammalian cells usually contain more than one PIP5KI isoform. This raises the question of whether different isoforms of PIP5KI fulfill different functions. Given the speculated role of [PIP.sub.2] in platelet and megakaryocyte actin dynamics, we analyzed murine megakaryocytes lacking individual PIP5KI isoforms. PIP5KI[gamma]-/- megakaryocytes exhibited plasma membrane blebbing accompanied by a decreased association of the membrane with the cytoskeleton. This membrane defect was rescued by adding back wild-type PIP5KI[gamma], but not by adding a catalytically inactive mutant or a splice variant lacking the talin-binding motif. Notably, both PIP5KI[beta]- and PIP5KI[gamma]-/- cells had impaired [PIP.sub.2] synthesis. However, PIP5KI[beta]-null cells lacked the membrane-cytoskeleton defect. Furthermore, overexpressing PIP5KI[beta] in PIP5KI[gamma]-/- cells failed to revert this defect. Megakaryocytes lacking the PIP5KI[gamma]-binding partner, talin1, mimicked the membrane-cytoskeleton defect phenotype seen in PIP5KI[gamma]-/- cells. These findings demonstrate a unique role for PIP5KI[gamma] in the anchoring of the cell membrane to the cytoskeleton in megakaryocytes, probably through a pathway involving talin. These observations further demonstrate that individual PIP5KI isoforms fulfill distinct functions within cells., Introduction In contrast to the head group of other phospholipids, the head group of phosphatidylinositol can be phosphorylated reversibly at the (3), (4), or (5) position to generate a family [...]

Published
2008

35. Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin

Author

Jiang, Guoying, Giannone, Gregory, Critchley, David R., Fukumoto, Emiko, and Sheetz, Michael P.

Subjects
Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Author(s): Guoying Jiang [1]; Grégory Giannone [1]; David R. Critchley [2]; Emiko Fukumoto [3]; Michael P. Sheetz (corresponding author) [1] Mechanical forces on matrix-integrin-cytoskeleton linkages are crucial for cell viability, [...]

Published
2003
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41. Crystal structure of the vinculin tail suggests a pathway for activation

Author

Bakolitsa, Constantina, Pereda, Jose M.de, Bagshaw, Clive R., Critchley, David R., and Liddington, Robert C.

Subjects
Actin -- Physiological aspects, Cytoskeletal proteins -- Research, X-ray crystallography -- Usage, Enzymes -- Structure-activity relationship, Biological sciences
Abstract

Results demonstrate that cytoskeletal protein vinculin plays a role in the assemby of the actin cytoskeleton. Data indicate that C-terminal arm of vinculin binds to the acidic phospholipids and this binding results in conformational changes leading to activation of actin.

Published
1999

47. The heat-labile enterotoxin of Escherichia coli binds to polylactosaminoglycan-containing receptors in CaCo-2 human intestinal epithelial cells

Author

Orlandi, Palmer A., Critchley, David R., and Fishman, Peter H.

Subjects
Enterotoxins -- Research, Epithelial cells -- Research, Escherichia coli -- Research, Biological sciences, Chemistry
Abstract

A functional characterization of Escherichia coli type I heat-labile enterotoxin (LT-I), a class of LT-I receptors, using the human intestinal epithelial cell line CaCo-2 reveals an eight times greater binding of LT-I by CaCo-2 cells than by cholera toxin (CT). The partial inhibition of LT-I activity by CT-B at concentrations that eliminate CT activity completely indicates that some of these additional LT-I receptors are functional. Separation of the solubilized toxin B-receptor complexes formed from (3H)galactose-labeled membranes by sodium dodecyl sulfate-polyacrylamide gel electrophoresis reveals a group of LT-I-recognizable galactoproteins. Neuraminidase treatment improves LT-I activity on intact cells and its association with membranes and the galactoproteins.

Published
1994

48. Analysis of the actin-binding domain of alpha-actinin by mutagenesis and demonstration that dystrophin contains a functionally homologous domain

Author

Hemmings, Lance, Kuhlman, Philip A., and Critchley, David R.

Subjects
Actin -- Research, Muscle proteins -- Research, Proteins -- Crosslinking, Binding sites (Biochemistry) -- Research, Protein binding -- Research, Biological sciences
Abstract

The actin-binding site within the NH(sub 2)-terminal domain (residues 1-245) of chick smooth muscle alpha-actinin (AA) was determined by expressing AA deletion mutants in monkey Cos cells and testing their ability to target actin filaments. The results showed that the binding site was between residues 108 and 189. In addition, the hypothesis thatthe NH(sub 2)-terminal domain of dystrophin is functionally and structurally homologous to that of alpha-actinin was confirmed by the behavior of chimeric proteins containing the NH(sub 2)-terminal region of dystrophin fused to alpha-actinin residues.

Published
1992

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