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488 results on '"Penn, Raymond B."'

6. The odorant receptor OR2W3 on airway smooth muscle evokes bronchodilation via a cooperative chemosensory tradeoff between TMEM16A and CFTR

Author

Huang, Jessie, Lam, Hong, Koziol-White, Cynthia, Limjunyawong, Nathachit, Kim, Donghwa, Kim, Nicholas, Karmacharya, Nikhil, Rajkumar, Premraj, Firer, Danielle, Dalesio, Nicholas M., Jude, Joseph, Kurten, Richard C., Pluznick, Jennifer L., Deshpande, Deepak A., Penn, Raymond B., Liggett, Stephen B., Panettieri, Reynold A., Dong, Xinzhong, and An, Steven S.

Published
2020

7. Gα12 facilitates shortening in human airway smooth muscle by modulating phosphoinositide 3‐kinase‐mediated activation in a RhoA‐dependent manner

Author

Yoo, Edwin J, Cao, Gaoyuan, Koziol‐White, Cynthia J, Ojiaku, Christie A, Sunder, Krishna, Jude, Joseph A, Michael, James V, Lam, Hong, Pushkarsky, Ivan, Damoiseaux, Robert, Di Carlo, Dino, Ahn, Kwangmi, An, Steven S, Penn, Raymond B, and Panettieri, Reynold A

Subjects
Medical Physiology, Biomedical and Clinical Sciences, Asthma, Lung, Biotechnology, Aetiology, 2.1 Biological and endogenous factors, Respiratory, Airway Obstruction, Carbachol, Cells, Cultured, GTP-Binding Protein alpha Subunits, G12-G13, Gene Knockdown Techniques, Humans, Muscle Contraction, Muscle, Smooth, Myosin Light Chains, Phosphatidylinositol 3-Kinase, Phosphorylation, Receptor, Muscarinic M3, Signal Transduction, rhoA GTP-Binding Protein, Pharmacology and Pharmaceutical Sciences, Pharmacology & Pharmacy, Pharmacology and pharmaceutical sciences
Abstract

Background and purposePI3K-dependent activation of Rho kinase (ROCK) is necessary for agonist-induced human airway smooth muscle cell (HASMC) contraction, and inhibition of PI3K promotes bronchodilation of human small airways. The mechanisms driving agonist-mediated PI3K/ROCK axis activation, however, remain unclear. Given that G12 family proteins activate ROCK pathways in other cell types, their role in M3 muscarinic acetylcholine receptor-stimulated PI3K/ROCK activation and contraction was examined.Experimental approachGα12 coupling was evaluated using co-immunoprecipitation and serum response element (SRE)-luciferase reporter assays. siRNA and pharmacological approaches, as well as overexpression of a regulator of G-protein signaling (RGS) proteins were applied in HASMCs. Phosphorylation levels of Akt, myosin phosphatase targeting subunit-1 (MYPT1), and myosin light chain-20 (MLC) were measured. Contraction and shortening were evaluated using magnetic twisting cytometry (MTC) and micro-pattern deformation, respectively. Human precision-cut lung slices (hPCLS) were utilized to evaluate bronchoconstriction.Key resultsKnockdown of M3 receptors or Gα12 attenuated activation of Akt, MYPT1, and MLC phosphorylation. Gα12 coimmunoprecipitated with M3 receptors, and p115RhoGEF-RGS overexpression inhibited carbachol-mediated induction of SRE-luciferase reporter. p115RhoGEF-RGS overexpression inhibited carbachol-induced activation of Akt, HASMC contraction, and shortening. Moreover, inhibition of RhoA blunted activation of PI3K. Lastly, RhoA inhibitors induced dilation of hPCLS.Conclusions and implicationsGα12 plays a crucial role in HASMC contraction via RhoA-dependent activation of the PI3K/ROCK axis. Inhibition of RhoA activation induces bronchodilation in hPCLS, and targeting Gα12 signaling may elucidate novel therapeutic targets in asthma. These findings provide alternative approaches to the clinical management of airway obstruction in asthma.

Published
2017

12. Allosteric ligands for the pharmacologically dark receptors GPR68 and GPR65

Author

Huang, Xi-Ping, Karpiak, Joel, Kroeze, Wesley K, Zhu, Hu, Chen, Xin, Moy, Sheryl S, Saddoris, Kara A, Nikolova, Viktoriya D, Farrell, Martilias S, Wang, Sheng, Mangano, Thomas J, Deshpande, Deepak A, Jiang, Alice, Penn, Raymond B, Jin, Jian, Koller, Beverly H, Kenakin, Terry, Shoichet, Brian K, and Roth, Bryan L

Subjects
Pharmacology and Pharmaceutical Sciences, Biomedical and Clinical Sciences, Medicinal and Biomolecular Chemistry, Chemical Sciences, 5.1 Pharmaceuticals, 1.1 Normal biological development and functioning, Inflammatory and immune system, Generic health relevance, Allosteric Regulation, Allosteric Site, Animals, Anti-Anxiety Agents, Benzyl Alcohols, Conditioning, Classical, Drug Discovery, Fear, Female, HEK293 Cells, Humans, Ligands, Lorazepam, Male, Memory, Mice, Mice, Knockout, Models, Molecular, Receptors, G-Protein-Coupled, Signal Transduction, Triazines, General Science & Technology
Abstract

At least 120 non-olfactory G-protein-coupled receptors in the human genome are 'orphans' for which endogenous ligands are unknown, and many have no selective ligands, hindering the determination of their biological functions and clinical relevance. Among these is GPR68, a proton receptor that lacks small molecule modulators for probing its biology. Using yeast-based screens against GPR68, here we identify the benzodiazepine drug lorazepam as a non-selective GPR68 positive allosteric modulator. More than 3,000 GPR68 homology models were refined to recognize lorazepam in a putative allosteric site. Docking 3.1 million molecules predicted new GPR68 modulators, many of which were confirmed in functional assays. One potent GPR68 modulator, ogerin, suppressed recall in fear conditioning in wild-type but not in GPR68-knockout mice. The same approach led to the discovery of allosteric agonists and negative allosteric modulators for GPR65. Combining physical and structure-based screening may be broadly useful for ligand discovery for understudied and orphan GPCRs.

Published
2015

18. β2 Agonists

Author

Billington, Charlotte K., Penn, Raymond B., Hall, Ian P., Barrett, James E., Editor-in-chief, Flockerzi, Veit, Series editor, Frohman, Michael A., Series editor, Geppetti, Pierangelo, Series editor, Hofmann, Franz B., Series editor, Michel, Martin C., Series editor, Page, Clive P., Series editor, Rosenthal, Walter, Series editor, Wang, KeWei, Series editor, and Barnes, Peter J., editor

Published
2017
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21. Pro-Relaxant EP Receptors Functionally Partition to Different Pro-Contractile Receptors in Airway Smooth Muscle

Author

Nayak, Ajay P, primary, Javed, Elham, additional, Villalba, Dominic R, additional, Wang, Yinna, additional, Morelli, Henry P, additional, Shah, Sushrut D., additional, Kim, Nicholas, additional, Ostrom, Rennolds S, additional, Panettieri, Reynold A, additional, An, Steven S, additional, Tang, Dale D, additional, and Penn, Raymond B, additional

Published
2023
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22. Identification of a β-arrestin-biased negative allosteric modulator for the β 2 -adrenergic receptor

Author

Ippolito, Michael, primary, De Pascali, Francesco, additional, Hopfinger, Nathan, additional, Komolov, Konstantin E., additional, Laurinavichyute, Daniela, additional, Reddy, Poli Adi Narayana, additional, Sakkal, Leon A., additional, Rajkowski, Kyle Z., additional, Nayak, Ajay P., additional, Lee, Justin, additional, Lee, Jordan, additional, Cao, Gaoyuan, additional, Donover, Preston S., additional, Reichman, Melvin, additional, An, Steven S., additional, Salvino, Joseph M., additional, Penn, Raymond B., additional, Armen, Roger S., additional, Scott, Charles P., additional, and Benovic, Jeffrey L., additional

Published
2023
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23. Identification and pharmacological characterization of a novel β-arrestin-biased negative allosteric modulator of the β

Author

Pascali, Francesco F. De, primary, Ippolito, Michael, additional, Hopfinger, Nathan, additional, Komolov, Konstantin E., additional, Laurinavichyute, Daniela K., additional, Sakkal, Leon A., additional, Nayak, Ajay P., additional, Reddy, Poli AN., additional, Donover, Preston S., additional, Reichman, Melvin, additional, Salvino, Joseph M., additional, Penn, Raymond B., additional, Armen, Roger S., additional, Scott, Charles P., additional, and Benovic, Jeffrey L., additional

Published
2023
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27. Prorelaxant E-type Prostanoid Receptors Functionally Partition to Different Procontractile Receptors in Airway Smooth Muscle.

Author

Nayak, Ajay P., Javed, Elham, Villalba, Dominic R., Yinna Wang, Morelli, Henry P., Shah, Sushrut D., Kim, Nicholas, Ostrom, Rennolds S., Panettieri Jr., Reynold A., An, Steven S., Tang, Dale D., and Penn, Raymond B.

Subjects
SMOOTH muscle, MUSCARINIC receptors, CONTRACTILE proteins, MYOSIN, PROTEIN kinases, CYTOSKELETON, AIRWAY (Anatomy), HISTAMINE
Abstract

Prostaglandin E2 imparts diverse physiological effects on multiple airway cells through its actions on four distinct E-type prostanoid (EP) receptor subtypes (EP1-EP4). Gs-coupled EP2 and EP4 receptors are expressed on airway smooth muscle (ASM), yet their capacity to regulate the ASM contractile state remains subject to debate. We used EP2 and EP4 subtype-specific agonists (ONO-259 and ONO-329, respectively) in cell- and tissue-based models of human ASM contraction--magnetic twisting cytometry (MTC), and precision-cut lung slices (PCLSs), respectively--to study the EP2 and EP4 regulation of ASM contraction and signaling under conditions of histamine or methacholine (MCh) stimulation. ONO-329 was superior (<0.05) to ONO-259 in relaxing MCh-contracted PCLSs (log half maximal effective concentration [logEC50]: 4.9 x 10-7 vs. 2.2 x 10-6; maximal bronchodilation ± SE, 35 ± 2% vs. 15 ± 2%). However, ONO-259 and ONO-329 were similarly efficacious in relaxing histamine-contracted PCLSs. Similar differential effects were observed in MTC studies. Signaling analyses revealed only modest differences in ONO-329- and ONO-259-induced phosphorylation of the protein kinase A substrates VASP and HSP20, with concomitant stimulation with MCh or histamine. Conversely, ONO-259 failed to inhibit MCh-induced phosphorylation of the regulatory myosin light chain (pMLC20) and the F-actin/G-actin ratio (F/G-actin ratio) while effectively inhibiting their induction by histamine. ONO-329 was effective in reversing induced pMLC20 and the F/G-actin ratio with both MCh and histamine. Thus, the contractile-agonist-dependent differential effects are not explained by changes in the global levels of phosphorylated protein kinase A substrates but are reflected in the regulation of pMLC20 (cross-bridge cycling) and F/G-actin ratio (actin cytoskeleton integrity, force transmission), implicating a role for compartmentalized signaling involving muscarinic, histamine, and EP receptor subtypes. [ABSTRACT FROM AUTHOR]

Published
2023
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28. GPCRs and Arrestins in Airways: Implications for Asthma

Author

Penn, Raymond B., Bond, Richard A., Walker, Julia K. L., Rosenthal, Walter, Series editor, Barrett, James E., Series editor, Hofmann, Franz B., Editor-in-chief, Buckingham, Julia, Series editor, Flockerzi, Veit, Series editor, Geppetti, Pierangelo, Series editor, Michel, Martin C., Series editor, Moore, Philip, Series editor, Page, Clive P., Series editor, and Gurevich, Vsevolod V., editor

Published
2014
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35. Nestin drives allergen‐induced airway smooth muscle hyperplasia and airway remodeling.

Author

Liao, Guoning, Wang, Ruping, Wu, Yidi, Maheshwari, Neelam Kumari, Penn, Raymond B., and Tang, Dale D.

Subjects
NESTIN, SMOOTH muscle, SERINE/THREONINE kinases, INTERMEDIATE filament proteins, AIRWAY (Anatomy), HYPERPLASIA
Abstract

This article discusses the role of nestin, a protein, in driving airway smooth muscle (ASM) hyperplasia and airway remodeling in asthma. The study found that nestin expression is upregulated in asthmatic ASM cells and tissues. By using mouse models and in vitro experiments, the researchers demonstrated that nestin plays a crucial role in ASM hyperplasia and airway remodeling. The study also suggests that nestin may interact with other proteins, such as 14-3-3 and mTOR, to induce ASM proliferation. These findings provide insights into the mechanisms underlying asthma and may have implications for future therapeutic approaches. [Extracted from the article]

Published
2024
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36. Identification of a β-arrestin-biased negative allosteric modulator for the β2-adrenergic receptor.

Author

Ippolito, Michael, De Pascali, Francesco, Hopfinger, Nathan, Komolov, Konstantin E., Laurinavichyute, Daniela, Reddy, Poli Adi Narayana, Sakkal, Leon A., Rajkowski, Kyle Z., Nayak, Ajay P., Lee, Justin, Lee, Jordan, Gaoyuan Cao, Donover, Preston S., Reichman, Melvin, An, Steven S., Salvino, Joseph M., Penn, Raymond B., Armen, Roger S., Scott, Charles P., and Benovic, Jeffrey L.

Subjects
TRANSMEMBRANE domains, PHARMACEUTICAL chemistry, SMALL molecules, CELLULAR control mechanisms, G protein coupled receptors, ASTHMATICS
Abstract

Catecholamine-stimulated β2-adrenergic receptor (β2AR) signaling via the canonical Gs-adenylyl cyclase-cAMP-PKA pathway regulates numerous physiological functions, including the therapeutic effects of exogenous β-agonists in the treatment of airway disease. β2AR signaling is tightly regulated by GRKs and β-arrestins, which together promote β2AR desensitization and internalization as well as downstream signaling, often antithetical to the canonical pathway. Thus, the ability to bias β2AR signaling toward the Gs pathway while avoiding β-arrestin-mediated effects may provide a strategy to improve the functional consequences of β2AR activation. Since attempts to develop Gs-biased agonists and allosteric modulators for the β2AR have been largely unsuccessful, here we screened small molecule libraries for allosteric modulators that selectively inhibit β-arrestin recruitment to the receptor. This screen identified several compounds that met this profile, and, of these, a difluorophenyl quinazoline (DFPQ) derivative was found to be a selective negative allosteric modulator of β-arrestin recruitment to the β2AR while having no effect on β2AR coupling to Gs. DFPQ effectively inhibits agonist-promoted phosphorylation and internalization of the β2AR and protects against the functional desensitization of β-agonist mediated regulation in cell and tissue models. The effects of DFPQ were also specific to the β2AR with minimal effects on the β1AR. Modeling, mutagenesis, and medicinal chemistry studies support DFPQ derivatives binding to an intracellular membrane-facing region of the β2AR, including residues within transmembrane domains 3 and 4 and intracellular loop 2. DFPQ thus represents a class of biased allosteric modulators that targets an allosteric site of the β2AR. [ABSTRACT FROM AUTHOR]

Published
2023
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39. Contributors

Author

Abbasi, Soraya, primary, Abbey, James, additional, Adzick, N. Scott, additional, Ahn, Sun-Young, additional, Albertine, Kurt H., additional, Allegaert, Karel, additional, Alper, Seth L., additional, Altit, Gabriel, additional, Altschuler, Steven M., additional, Alvaro, Ruben E., additional, Amorosa, Jennifer M.H., additional, Anbuhl, Kelsey L., additional, Andersen, Claus Yding, additional, Anderson, Richard A., additional, Askenazi, David J., additional, Auten, Richard Lambert, additional, Autmizguine, Julie, additional, Azhibekov, Timur, additional, Back, Stephen A., additional, Badaut, Jérôme, additional, Baker, Peter Russell, additional, Ballard, Philip L., additional, Bancalari, Eduardo H., additional, Barichello, Tatiana, additional, Battaglia, Frederick, additional, Baum, Michel, additional, Beggs, Simon, additional, Bell, Edward F., additional, Benchimol, Corinne, additional, Benders, Manon J.N.L., additional, Bennet, Laura, additional, Bennett, Phillip R., additional, Berger, Melvin, additional, Bernhard, Wolfgang, additional, Bertram, John F., additional, Bhosle, Vikrant K., additional, Bhutani, Vinod K., additional, Black, M. Jane, additional, Bliss, Joseph M., additional, Bolender, David L., additional, Brandenburg, Joline E., additional, Broussard, Delma L., additional, Brown, Laura Davidson, additional, Burrin, Douglas G., additional, Cannon, Barbara, additional, Caplan, Michael, additional, Carlson, Susan E., additional, Carlton, David P., additional, Caruana, Georgina, additional, Cashore, William J., additional, Chaemsaithong, Piya, additional, Chaiyasit, Noppadol, additional, Charlton, Jennifer R., additional, Cheatham, Carol L., additional, Chemtob, Sylvain, additional, Chen, Yi-Yung, additional, Chevalier, Robert L., additional, Chheda, Sadhana, additional, Childs, Andrew J., additional, Christensen, Robert D., additional, Chu, Alison, additional, Chu, David H., additional, Cilio, Maria Roberta, additional, Clark, David A., additional, Cleary-Goldman, Jane, additional, Clemente, Ethel G., additional, Clements, John A., additional, Clyman, Ronald I., additional, Cohen, Susan S., additional, Colombo, John, additional, Cowett, Richard M., additional, Crawford, Peter A., additional, Crowe, James E., additional, Cullen-McEwen, Luise A., additional, Cutfield, Wayne S., additional, D'Alton, Mary E., additional, Danzer, Enrico, additional, Delacourt, Christophe, additional, Devaskar, Sherin U., additional, Diacovo, Thomas G., additional, Docheva, Nikolina, additional, Dormans, John P., additional, Dysart, Kevin, additional, El-Khuffash, Afif, additional, Ellis, Peter James, additional, Empey, Kerry McGarr, additional, Ercal, Baris, additional, Erdős, Melinda, additional, Erickson, Robert P., additional, Fahim, Mohamed A., additional, Faksh, Arij, additional, Frank, Hans-Georg, additional, Friedlich, Philippe S., additional, Friedman, Jed, additional, Gao, Yuansheng, additional, Garland, Marianne, additional, Geddes, Donna, additional, Georgieff, Michael K., additional, Gien, Jason, additional, Giussani, Dino A., additional, Goldman, Armond S., additional, González, Efrén, additional, Good, Misty, additional, Grant, Denis M., additional, Green, Lucy R., additional, Grigoriou, Emmanouil, additional, Grimberg, Adda, additional, Gross, Ian, additional, Grunau, Ruth E., additional, Guignard, Jean-Pierre, additional, Gunn, Alistair Jan, additional, Gurtunca, Nursen, additional, Hadchouel, Alice, additional, Haddad, Gabriel G., additional, Hagberg, Henrik, additional, Hale, Thomas, additional, Hambidge, K. Michael, additional, Hammerman, Cathy, additional, Hansen, Thor Willy Ruud, additional, Hanson, Mark A., additional, Harding, Richard, additional, Harris, Mary Catherine, additional, Hartmann, Peter, additional, Hassiotou, Foteini, additional, Haugen, Guttorm, additional, Hawkes, Colin P., additional, Hay, William W., additional, Hayward, Christina E., additional, Heine, Vivi M., additional, Hellström, Ann, additional, Helmrath, Michael A., additional, Hendricks-Muñoz, Karen D., additional, Herrera, Emilio, additional, Hiatt, Michael J., additional, Hoath, Steven B., additional, Hooper, Stuart B., additional, Huang, Stephen A., additional, Iacobellli, Silvia, additional, Inder, Terrie E., additional, Iruela-Arispe, M. Luisa, additional, Jadcherla, Sudarshan R., additional, Jain, Deepak, additional, Jansson, Thomas, additional, Jefferies, John Lynn, additional, Jetton, Jennifer G., additional, Jobe, Alan H., additional, Johnson, Lois H., additional, Johnston, Richard B., additional, Jones, Rebecca Lee, additional, Jose, Pedro A., additional, Kalhan, Satish C., additional, Kallapur, Suhas G., additional, Kaplan, Michael, additional, Kaplan, Stanley, additional, Karpen, Heidi Eigenrauch, additional, Karpen, Saul J., additional, Karumanchi, S. Ananth, additional, Kaskel, Frederick J., additional, Katheria, Anup C., additional, Katz, Lorraine E. Levitt, additional, Keeney, Susan E., additional, Kern, Steven E., additional, Khanjani, Shirin, additional, Kilpatrick, Laurie E., additional, Kim, Chang-Ryul, additional, Kinsella, John P., additional, Kiserud, Torvid, additional, Koenig, Joyce M., additional, Kollmann, Tobias R., additional, Kolls, Jay K., additional, Krebs, Nancy F., additional, Kulik, Thomas J., additional, Kutikov, Jessica Katz, additional, Lakshminrusimha, Satyan, additional, Lamola, Angelo A., additional, Lasunción, Miguel Angel, additional, Lavoie, Pascal M., additional, LeBien, Tucker W., additional, Lee, Mary M., additional, Lee, Matthew K., additional, Lee, Yvonne K., additional, Leibel, Sandra, additional, Levine, Fred, additional, Levy, Ofer, additional, Liu, Yang, additional, Lobritto, Steven, additional, Loomis, Cynthia A., additional, Lopez, Colleen A., additional, MacIntyre, David A., additional, Mahe, Maxime M., additional, Maheshwari, Akhil, additional, Mankouski, Anastasiya, additional, Mantilla, Carlos B., additional, Marchant, Arnaud, additional, Margolis, Kara Gross, additional, Mariscalco, M. Michele, additional, Maródi, László, additional, Maršál, Karel, additional, Martin, Richard J., additional, Matsell, Douglas G., additional, Matthews, Dwight E., additional, McArdle, Harry J., additional, McManaman, James L., additional, McNamara, Patrick J., additional, McQuillen, Patrick S., additional, McQuinn, Tim C., additional, Mercer, Judith S., additional, Meschia, Giacomo, additional, Miller, Steven P., additional, Minoo, Parviz, additional, Monagle, Paul, additional, Mortola, Jacopo P., additional, Muglia, Louis J., additional, Munshi, Upender K., additional, Namgung, Ran, additional, Narasimhan, Sumana, additional, Nedergaard, Jan, additional, Neu, Josef, additional, Nigam, Sanjay K., additional, Nogee, Lawrence M., additional, Noori, Shahab, additional, O'Brien, Barbara M., additional, Ohls, Robin K., additional, Ortega-Senovilla, Henar, additional, O'Sullivan, Justin M., additional, Owusu, Sarah A., additional, Pal, Abhijeet, additional, Panitch, Howard B., additional, Penn, Anna A., additional, Penn, Raymond B., additional, Pernia, Cameron, additional, Philipps, Anthony F., additional, Picoraro, Joseph A., additional, Pisani, Francesco, additional, Pleasure, David, additional, Pleasure, Jeanette R., additional, Pleasure, Samuel J., additional, Pomeroy, Scott L., additional, Post, Martin, additional, Prakash, Y.S., additional, Prozialeck, Joshua D., additional, Pysher, Theodore J., additional, Quigley, Raymond, additional, Rabinovitch, Marlene, additional, Raffay, Thomas M., additional, Raj, J. Usha, additional, Ramsey, Haley, additional, Rana, Sarosh, additional, Randis, Tara Marie, additional, Ranger, Manon, additional, Ratner, Adam J., additional, Regnault, Timothy R.H., additional, Rigatto, Henrique, additional, Rintoul, Natalie E., additional, Romero, Roberto, additional, Rose, James C., additional, Rosenfeld, Charles R., additional, Ross, A. Catharine, additional, Rozycki, Henry J., additional, Ryan, Thomas D., additional, Sahni, Rakesh, additional, Sajti, Eniko, additional, Sarnat, Harvey B., additional, Satlin, Lisa M., additional, Saugstad, Ola Didrik, additional, Schierding, William, additional, Schmalstieg, Frank C., additional, Schwartz, George J., additional, Schwartz, Jeffrey, additional, Segar, Jeffrey L., additional, Selewski, David T., additional, Seri, Istvan, additional, Shaffer, Thomas H., additional, Shah, Kara N., additional, Shearer, Martin J., additional, Shojaie, Sharareh, additional, Shroyer, Noah F., additional, Sibley, Colin P., additional, Sieck, Gary C., additional, Simmons, Rebecca A., additional, Sivieri, Emidio M., additional, Smith, Francine G., additional, Smith, Lois E.H., additional, Smyth, Ian M., additional, Snarr, Brian S., additional, Snyder, Evan Y., additional, Sola-Visner, Martha, additional, Solhaug, Michael J., additional, Sperling, Mark A., additional, Srinivasan, Lakshmi, additional, Stahl, Andreas, additional, Stanley, Charles A., additional, Steinhorn, Robin H., additional, Stonestreet, Barbara S., additional, Strasburger, Janette F., additional, Styne, Dennis M., additional, Sussel, Lori, additional, Tam, Emily W.Y., additional, Tan, Libo, additional, Thornton, Claire, additional, Tollin, Daniel J., additional, Tóth, Beáta, additional, Towbin, Jeffrey A., additional, Trocle, Ashley, additional, Truog, William E., additional, Tsang, Reginald C., additional, Uhler, Kristin M., additional, Van Den Anker, John N., additional, van Goudoever, Johannes (Hans) B., additional, Vannucci, Susan J., additional, Vickers, Mark H., additional, Virgintino, Daniela, additional, Volpe, Joseph J., additional, Vora, Neeta L., additional, Vyas, Neha V., additional, Wacker-Gussmann, Annette, additional, Wallace, Megan J., additional, Walsh, Brian H., additional, Wang, Alice M., additional, Warburton, David, additional, Ward, Robert M., additional, Watterberg, Kristi L., additional, Werner, Lynne A., additional, Wershil, Barry K., additional, Wert, Susan E., additional, Wessels, Andy, additional, Whitsett, Jeffrey A., additional, Wise, Michael, additional, Wolf, Matthias T., additional, Wolfson, Marla R., additional, Wong, Hector R., additional, Wynn, James L., additional, Yeo, Lami, additional, Yip, Stephen, additional, Yoder, Bradley A, additional, Yoder, Mervin C., additional, Yoshimoto, Momoko, additional, Yuskaitis, Christopher J., additional, Zhou, Dan, additional, and Zovein, Ann, additional

Published
2017
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42. Reactive Oxygen Species Behaving Badly: Oxidized Phosphatidylcholines Corrupt Ca2+ Signaling in Airway Smooth Muscle.

Author

Deshpande, Deepak A. and Penn, Raymond B.

Subjects
REACTIVE oxygen species, SMOOTH muscle, CALCIUM ions, POLLUTANTS, RYANODINE receptors, CD38 antigen
Abstract

An editorial discusses the role of oxidized phosphatidylcholines (OxPCs) in obstructive lung diseases, emphasizing their impact on airway smooth muscle (ASM) and calcium signaling. Topics include the procontractile effects of OxPCs on ASM, the mechanisms of intracellular calcium mobilization, and the potential implications for asthma pathobiology and therapeutic strategies.

Published
2023
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47. β2 Agonists

Author

Billington, Charlotte K., primary, Penn, Raymond B., additional, and Hall, Ian P., additional

Published
2016
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