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2. Nuclear Focal Adhesion Kinase Controls Vascular Smooth Muscle Cell Proliferation and Neointimal Hyperplasia Through GATA4-Mediated Cyclin D1 Transcription

Author

Jeong, Kyuho, Kim, Jung-Hyun, Murphy, James M, Park, Hyeonsoo, Kim, Su-Jeong, Rodriguez, Yelitza AR, Kong, Hyunkyung, Choi, Chungsik, Guan, Jun-Lin, Taylor, Joan M, Lincoln, Thomas M, Gerthoffer, William T, Kim, Jun-Sub, Ahn, Eun-Young Erin, Schlaepfer, David D, and Lim, Ssang-Taek Steve

Subjects
Genetics, Cardiovascular, 2.1 Biological and endogenous factors, Aetiology, Active Transport, Cell Nucleus, Animals, Cell Nucleus, Cell Proliferation, Cells, Cultured, Cyclin D1, Focal Adhesion Kinase 1, GATA4 Transcription Factor, Hyperplasia, Mice, Mice, Inbred C57BL, Myocytes, Smooth Muscle, Tunica Intima, atherosclerosis, cyclin D1, FAK, GATA4, hyperplasia, smooth muscle cell, vascular remodeling, Cardiorespiratory Medicine and Haematology, Clinical Sciences, Cardiovascular System & Hematology
Abstract

RationaleNeointimal hyperplasia is characterized by excessive accumulation of vascular smooth muscle cells (SMCs) leading to occlusive disorders, such as atherosclerosis and stenosis. Blood vessel injury increases growth factor secretion and matrix synthesis, which promotes SMC proliferation and neointimal hyperplasia via FAK (focal adhesion kinase).ObjectiveTo understand the mechanism of FAK action in SMC proliferation and neointimal hyperplasia.Methods and resultsUsing combined pharmacological FAK catalytic inhibition (VS-4718) and SMC-specific FAK kinase-dead (Myh11-Cre-ERT2) mouse models, we report that FAK regulates SMC proliferation and neointimal hyperplasia in part by governing GATA4- (GATA-binding protein 4) cyclin D1 signaling. Inhibition of FAK catalytic activity facilitates FAK nuclear localization, which is required for proteasome-mediated GATA4 degradation in the cytoplasm. Chromatin immunoprecipitation identified GATA4 binding to the mouse cyclin D1 promoter, and loss of GATA4-mediated cyclin D1 transcription diminished SMC proliferation. Stimulation with platelet-derived growth factor or serum activated FAK and redistributed FAK from the nucleus to cytoplasm, leading to concomitant increase in GATA4 protein and cyclin D1 expression. In a femoral artery wire injury model, increased neointimal hyperplasia was observed in parallel with elevated FAK activity, GATA4 and cyclin D1 expression following injury in control mice, but not in VS-4718-treated and SMC-specific FAK kinase-dead mice. Finally, lentiviral shGATA4 knockdown in the wire injury significantly reduced cyclin D1 expression, SMC proliferation, and neointimal hyperplasia compared with control mice.ConclusionsNuclear enrichment of FAK by inhibition of FAK catalytic activity during vessel injury blocks SMC proliferation and neointimal hyperplasia through regulation of GATA4-mediated cyclin D1 transcription.

Published
2019

8. From research to practice: experiences engineering a production metadata database for a scale out file system.

Author

Charles Johnson, Kimberly Keeton, Charles B. Morrey III, Craig A. N. Soules, Alistair C. Veitch, Stephen Bacon, Oskar Batuner, Marcelo Condotta, Hamilton Coutinho, Patrick J. Doyle, Rafael Eichelberger, Hugo Kiehl, Guilherme R. Magalhaes, James McEvoy, Padmanabhan Nagarajan, Patrick Osborne, Joaquim Souza, Andy Sparkes, Mike Spitzer, Sébastien Tandel, Lincoln Thomas, and Sebastian Zangaro

Published
2014

30. Massachusetts Justice Community Opioid Innovation Network (MassJCOIN)

Author

Evans, Elizabeth A., primary, Stopka, Thomas J., additional, Pivovarova, Ekaterina, additional, Murphy, Sean M., additional, Taxman, Faye S., additional, Ferguson, Warren J., additional, Bernson, Dana, additional, Santelices, Claudia, additional, McCollister, Kathryn E., additional, Hoskinson, Randall, additional, Lincoln, Thomas, additional, Friedmann, Peter D., additional, Coppinger, Sheriff Kevin F., additional, Faro, Jason, additional, Donelan, Sheriff Christopher J., additional, Hayes, Edmond, additional, Cocchi, Sheriff Nicholas, additional, Lyman, Martha, additional, Cahillane, Sheriff Patrick J., additional, Cady, Melinda, additional, Koutoujian, Sheriff Peter J., additional, Siddiqi, Kashif, additional, Lee, Dan, additional, McDermott, Sheriff Jerome P., additional, Flynn, Tara, additional, Sica, Erika, additional, Tompkins, Sheriff Steven W., additional, Steinberg, Rachelle, additional, and Bernadeau-Alexandre, Marjorie, additional

Published
2021
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32. Glucose downregulation of PKG-I protein mediates increased thrombospondin1-dependent TGF-[beta] activity in vascular smooth muscle cells

Author

Wang, Shuxia, Lincoln, Thomas M., and Murphy-Ullrich, Joanne E.

Subjects
Protein kinases -- Properties, Dextrose -- Health aspects, Glucose -- Health aspects, Membrane proteins -- Properties, Vascular smooth muscle -- Properties, Transforming growth factors -- Health aspects, Cell physiology -- Research, Biological sciences
Abstract

Diabetes is a major predictor of in-stent restenosis, which is associated with fibroproliferative remodeling of the vascular wall due to increased transforming growth factor-[beta] (TGF-[beta]) action. It is well established that thrombospondin1 (TSP1) is a major regulator of TGF-[beta] activation in renal and cardiac complications of diabetes. However, the role of the TSP1-TGF-[beta] pathway in macrovascular diabetic complications, including restenosis, has not been addressed. In mesangial cells, high glucose concentrations depress protein kinase G (PKG) activity, but not PKG-I protein, thereby downregulating transcriptional repression of TSP1. Previously, we showed that high glucose downregulates PKG-I protein expression by vascular smooth muscle cells (VSMCs) through altered NADPH oxidase signaling. In the present study, we investigated whether high glucose regulation of PKG protein and activity in VSMCs similarly regulates TSP1 expression and downstream TGF-[beta] activity. These studies showed that high glucose stimulates both TSP1 expression and TGF-[beta] bioactivity in primary murine aortic smooth muscle cells (VSMCs). TSP1 is responsible for the increased TGF-[beta] bioactivity under high glucose conditions, because treatment with anti-TSP1 antibody, small interfering RNA-TSP1, or an inhibitory peptide blocked glucose-mediated increases in TGF-[beta] activity and extracellular matrix protein (fibronectin) expression. Overexpression of constitutively active PKG, but not the PKG-I protein, inhibited glucose-induced TSP1 expression and TGF-[beta] bioactivity, suggesting that PKG protein expression is insufficient to regulate TSP1 expression. Together, these data establish that glucose-mediated downregulation of PKG levels stimulates TSP1 expression and enhances TGF-[beta] activity and matrix protein expression, which can contribute to vascular remodeling in diabetes. transforming growth factor-[beta]; fibronectin doi: 10.1152/ajpcell.00330.2009.

Published
2010

34. Exogenous NO triggers preconditioning via a cGMP- and mito[K.sub.ATP]-dependent mechanism

Author

Qin, Qining, Yang, Xi-Ming, Cui, Lin, Critz, Stuart D., Cohen, Michael V., Browner, Natasha C., Lincoln, Thomas M., and Downey. James M.

Subjects
Protein kinases -- Research, Nitric oxide -- Research, Biological sciences
Abstract

Exogenous nitric oxide (NO) triggers a preconditioning-like effect in heart via a pathway that is dependent on reactive oxygen species. This study examined the signaling pathway by which the NO donor S-nitroso-N-acetylpeniciilamine (SNAP, 2 [micro]M) triggers its anti-infarct effect. Isolated rabbit hearts experienced 30 min of regional ischemia and 120 min of subsequent reperfusion, infarct size was determined by triphenyltetrazolium chloride staining, infarct size was reduced from 30.5 [+ or -] 3.0% of the risk zone in control hearts to 10.2 [+ or -] 2.0% in SNAP-treated hearts. Bracketing the SNAP infusion with either the guanylyl cyclase blocker 1H-[1,2,4]oxadiazoie[4,3-a]quinoxalin-1-one (2 [micro]M) or the mitochondrial ATP-sensitive [K.sup.+] (mito[K.sub.ATP]) channel blocker 5-hydroxydecanoate (200 [micro]M) completely blocked the infarct-sparing effect of SNAP (34.3 [+ or -] 3.8 and 32.2 [+ or -] 1.6% infarction, respectively). Pretreatment of hearts with 8-(4-chlorophenylthio)-guanosine 3',5'cyclic monophosphate (10 [micro]M), which is a cell-permeable cGMP analog that activates protein kinase G, mimicked the preconditioning effect of SNAP by reducing infarct size to 7.5 [+ or -] 1.1% of the risk zone. This salutary effect was abolished by either the free radical scavenger N-(2-mercaptopropionyl)glyciue (1 mM) or 5-hydroxydecanoate (100 [micro]M; 28.9 [+ or -] 2.7 and 33.6 [+ or -] 5.0% infarction of the risk zone, respectively). To confirm these functional data and the effect of SNAP on the guanylyl cyclase-protein kinase G signaling pathway, cGMP levels were measured. SNAP increased the level from 0.18 [+ or -] 0.04 to 0.61 [+ or -] 0.14 pmol/mg of protein (P < 0.05). These data suggest that exogenous NO triggers the preconditioning effect by initiating a cascade of events including stimulation of guanylyl cyclase to make cGMP, activation of protein kinase G, opening of mito[K.sub.ATV] channels, and, finally, production of reactive oxygen species. mitochondrial ATP-sensitive potassium channel; protein kinase G; S-nitroso-N-acetylpenicillamine; guanylyl cyclase

Published
2004

35. Downregulation of cGMP-dependent protein kinase expression by inflammatory cytokines in vascular smooth muscle cells

Author

Browner, Natasha C., Sellak, Hassan, and Lincoln, Thomas M.

Subjects
Cytokines -- Research, Cyclic guanylic acid -- Influence, Biological sciences
Abstract

NO and cGMP have antigrowth and anti-inflammatory effects on the vessel wall in response to injury. It is well established that after vascular injury proinflammatory cytokines are involved in vascular wall remodeling. The purpose of this study was to ascertain the signaling mechanisms involved in cGMP-dependent protein kinase (PKG) suppression by inflammatory cytokines in primary bovine aortic vascular smooth muscle cells (VSMC). Interleukin (IL)-I[beta], tumor necrosis factor (TNF)-[alpha], and LPS decreased the mRNA and protein levels of PKG in VSMC. IL-I[beta], TNF-[alpha], and LPS increased inducible nitric oxide synthase (iNOS) expression and cGMP production. Treatment of cells with selective inhibitors of iNOS or soluble guanylate cyclase (sGC) reversed the downregulation of PKG expression induced by cytokines and LPS. The NO donor (Z)-1-[2-(2-aminoethyl)-N-(2-ammonioethyl)amino]diazen-1-ium-1,2-diolate (DETA NONOate) and 3-(5-hydroxymethyl-2-furyl)-1-benzylindazole (YC-1), a NO-independent sGC activator, decreased PKG mRNA and protein expression in bovine aortic VSMC. Cyclic nucleotide analogs [8-(4-chlorophenylthio)guanosine 3',5'-cyclic monophosphate (CPT-cGMP) and 8-(4-chlorophenylthio)adenosine 3,5'-cyclic monophosphate (CPT-cAMP)] also suppressed PKG mRNA and protein expression. However, CPT-cAMP was more effective than CPT-cGMP in decreasing PKG mRNA levels. Selective inhibition of PKA with the Rp isomer of 8-(4-chlorophenylthio)adenosine 3',5'-cyclic monophosphorothioate (Rp-8p-CPT cAMPS) prevented the downregulation of PKG by LPS. In contrast, the Rp isomer of 8-(4-chlorophenylthio)guanosine 3,5'-cyclic monophosphorothioate (Rp-8p-CPT cGMPS; inhibitor of PKG) had no effect on LPS-induced inhibition of PKG mRNA and protein expression. These studies suggest that cross-activation of PKA in response to iNOS expression by inflammatory mediators downregulates PKG expression in bovine aortic VSMC. vascular injury; nitric oxide; inflammation

Published
2004

40. Sex and age correlates of chlamydia prevalence in adolescents and adults entering correctional facilities, 2005: implications for screening policy

Author

Joesoef, M. Riduan, Weinstock, Hillard S., Kent, Charlotte K., Chow, Joan M., Boudov, Melina R., Parvez, Farah M., Cox, Tamara, Lincoln, Thomas, Miller, Jamie L., and Sternberg, Maya

Subjects
Chlamydia infections -- Risk factors, Chlamydia infections -- Diagnosis, Chlamydia infections -- Distribution, Chlamydia infections -- Prevention, Correctional institutions -- Services, Prevalence studies (Epidemiology) -- Research, Company distribution practices, Health
Abstract

Objectives: To evaluate sex and age correlates of chlamydia prevalence in incarcerated populations. Methods: Cross-sectional analysis of chlamydia prevalence by demographic characteristics from incarcerated females and males entering selected juvenile and adult correctional facilities (jails) in the United States in 2005. Results: A total of 97,681 and 52,485 incarcerated persons aged [greater than or equal to]12 years were screened for chlamydia in 141 juvenile and 22 adult correctional facilities, respectively. Overall, chlamydia prevalence was high in females (14.3% and 7.5%) in both juvenile and adult facilities when compared with that in males (6.0% and 4.6%). The chlamydia prevalence was higher in incarcerated females than in incarcerated males for persons [less than or equal to] 35 years, and prevalence was highest among females aged [less than or equal to] 25 years (range, 11.3%-15.6%). In juvenile facilities, prevalence did not steadily increase with age in females (12.8% in 12-14 years, 15.1% in 15-17 years, and 14.3% in 18-20 years) whereas in males prevalence steadily increased with age (2.4% in 12-14 years to 8.7% in 18-20 years). In females and males the highest prevalence in juvenile facilities was in incarcerated blacks (18.4% and 9.6%, respectively). In adult facilities, the prevalence was consistently highest in younger detainees: in females it was 15.6% in 18- to 20-year olds compared with 1.5% in those >40 years; in males it was 8.8% in 18- to 20-year olds compared with 1.4% in those >40 years. Conclusions: The consistently high chlamydia prevalence among females in juvenile facilities and females ([less than or equal to] 25 years) in adult facilities supports a screening policy in correctional settings consistent with Centers for Disease Control and Prevention and US Preventive Services Task Force guidelines. Although the prevalence of chlamydia in males is substantial, chlamydia prevalence in females exceeds that of males [less than or equal to]35 years, and thus screening females for chlamydia in these facilities should take priority over screening males.

Published
2009

42. Contributors

Author

Abrams, John M., primary, Adelman, John P., additional, Alcorn, Joseph L., additional, Alessi, Dario R., additional, Alexov, Emil, additional, Alford, Simon, additional, Alitalo, Kari, additional, Allison, James P., additional, Almo, Steven C., additional, Alory, Christelle, additional, Al-Shamkhani, Aymen, additional, Amundson, Sally A., additional, Anderson, Carl W., additional, Andersen, Jannik N., additional, Angel, Peter, additional, Appella, Ettore, additional, Arendshorst, William J., additional, Arkinstall, Steve, additional, Audhya, Anjon, additional, Avruch, Joseph, additional, Bader, Gary D., additional, Bagala, Cinzia, additional, Balch, William E., additional, Balsinde, Jesus, additional, Banerjee, Utpal, additional, Barford, David, additional, Bar-Sagi, Dafna, additional, Bartlett, Perry F., additional, Bastiaens, Philippe I.H., additional, Battelli, Chiara, additional, Baudhuin, Linnea M., additional, Beavil, Andrew J., additional, Beavil, Rebecca L., additional, Beavo, Joseph A., additional, Bello-Reuss, Elsa, additional, Bellum, Stephen, additional, Belmonte, Juan Carlos Izpisúa, additional, Bennett, Craig B., additional, Benovic, Jeffrey L., additional, Berridge, Michael J., additional, Beuning, Penny J., additional, Bhandari, Rashna, additional, Bhattacharya, Ananya, additional, Biel, Martin, additional, Bielinski, Vincent A., additional, Bilak, Hana, additional, Birnbaumer, Lutz, additional, Birrell, Geoff, additional, Bishop, Gail A., additional, Blackmer, Trillium, additional, Blackshear, Perry J., additional, Blattner, Christine, additional, Blaustein, Mordecai P., additional, Bokoch, Gary M., additional, Bonewald, Lynda F., additional, Bonomi, Marco, additional, Booden, Michelle A., additional, Boone, Charles, additional, Bootman, Martin D., additional, Bos, Johannes L., additional, Bradbury, Jane M., additional, Bradshaw, Ralph A., additional, Bresnick, Anne R., additional, Brevnova, Lena, additional, Brinkworth, Ross I., additional, Brown, Michael S., additional, Brown, Steven A., additional, Brunet, Anne, additional, Bucki, Robert, additional, Burgoyne, Robert D., additional, Buss, Janice E., additional, Butow, Ronald A., additional, Capdevila, Javier, additional, Carafoli, Ernesto, additional, Carlson, Cathrine R., additional, Carpenter, Graham, additional, Carrillo, Juan J., additional, Casey, Patrick J., additional, Catterall, William A., additional, Cerione, Richard A., additional, Cesareni, Gianni, additional, Chan, Andrew C., additional, Chang, Geoffrey, additional, Chao, Moses V., additional, Charbonneau, Harry, additional, Chen, Philip, additional, Cheng, Alan, additional, Chiu, Chris, additional, Chow, Dar-chone, additional, Chrisman, Ted D., additional, Christensen, Anne Elisabeth, additional, Chung, Jee Y., additional, Churchill, Grant C., additional, Ciechanover, Aaron, additional, Cingolani, Gino, additional, Claeysen, Sylvie, additional, Closset, Jean, additional, Cockcroft, Shamshad, additional, Cohen, Patricia T.W., additional, Cohen, Philip, additional, Colbran, Roger J., additional, Comstock, Clay E.S., additional, Conti, Marco, additional, Corbin, Jackie D., additional, Corda, Daniela, additional, Costagliola, Sabine, additional, Cote, Rick H., additional, Coughlin, Shaun R., additional, Cowart, L. Ashley, additional, Cox, Adrienne D., additional, Cragg, Mark S., additional, Crespo, José L., additional, Crosio, Claudia, additional, Daly, Christopher, additional, Damak, Sami, additional, Dasso, Mary, additional, David, Michael, additional, Davis, Anthony J., additional, Davis, Roger J., additional, Day, Richard N., additional, Degerman, Eva, additional, DeLano, Warren L., additional, Dell'Acqua, Mark L., additional, Délot, Emmanuèle, additional, Demple, Bruce, additional, Dennis, Edward A., additional, Denu, John M., additional, DePaoli-Roach, Anna A., additional, Der, Channing J., additional, de Rooij, Johan, additional, de Sauvage, Frederic, additional, Devreotes, Peter N., additional, Dewaste, Valérie, additional, Dickson, Robert B., additional, Diebold, Becky A., additional, Fiori, Pier Paolo Di, additional, Girolamo, Maria Di, additional, Diplexcito, Julie, additional, Dixon, Jack E., additional, Doms, Robert W., additional, Donoghue, Daniel J., additional, Doolittle, Russell F., additional, Døskeland, Stein Ove, additional, Dostmann, Wolfgang R.G., additional, Dreyer, Matthias K., additional, Du, Guo Guang, additional, Du, Keyong, additional, Duchen, Michael R., additional, Dunphy, William G., additional, Durgan, Joanne, additional, Dustin, Michael L., additional, Edwards, Peter A., additional, Egen, Jackson G., additional, Eiden, Lee E., additional, Elion, Elaine A., additional, Emr, Scott, additional, Engelhardt, Othmar G., additional, Erneux, Christophe, additional, Espenshade, Peter J., additional, Esplin, Edward D., additional, Evers, B. Mark, additional, Eyles, Joanne L., additional, Fame, Sheelagh, additional, Farquhar, Marilyn, additional, Feil, Robert, additional, Feng, Gui-Jie, additional, Fields, Stanley, additional, Fiordalisi, James J., additional, Firtel, Richard A., additional, Fitzgerald, Garret A., additional, Flint, Andrew, additional, Foiani, Marco, additional, Forman, Barry Marc, additional, Fornace, Albert J., additional, Francis, Sharron H., additional, Fritz, Günter, additional, Fruman, David A., additional, Galione, Antony, additional, Gandhi, Chris S., additional, Garbers, David L., additional, Garcia, K. Christopher, additional, Geiger, Benjamin, additional, Gerace, Larry, additional, Gerstner, Andrea, additional, Giaccia, Amato J., additional, Giannattasio, Michele, additional, Giguère, Vincent, additional, Glass, Christopher K., additional, Glennie, Martin J., additional, Glick, Jennifer L., additional, Goldstein, Joseph L., additional, Gopal, Venkatesh, additional, Gorospe, Myriam, additional, Govaerts, Cedric, additional, Graves, Paul R., additional, Gray, Patrick W., additional, Graziani, Irene, additional, Green, Douglas R., additional, Greenberg, Michael E., additional, Greenwald, Iva, additional, Gu, Haihua, additional, Gueven, Nuri, additional, Gutkind, J. Silvio, additional, Haeggström, Jesper Z., additional, Hall, Alan, additional, Hall, Michael N., additional, Haller, Otto, additional, Hamm, Heidi E., additional, Hannun, Yusef A., additional, Hansen, Carl A., additional, Harden, T. Kendall, additional, Hardie, D. Grahame, additional, Hasegawa, Kiminori, additional, Hawkins, Phillip T., additional, Haystead, Timothy A.J., additional, He, Xiao-lin, additional, Heizmann, Claus W., additional, Heldin, Carl-Henrik, additional, Hermiston, Michelle L., additional, Herrlich, Peter, additional, Hewat, Elizabeth A., additional, Hille, Bertil, additional, Hilton, Douglas J., additional, Hinchliffe, K.A., additional, Ho, Steffan N., additional, Ho, Su-Chin, additional, Hochstrasser, Mark, additional, Hofmann, Franz, additional, Hogue, Christopher W., additional, Hol, Wim G.J., additional, Holash, Jocelyn, additional, Holmgren, Robert A., additional, Honig, Barry, additional, Hostager, Bruce S., additional, Hubbard, Stevan R., additional, Huber, Michael, additional, Hunter, Tony, additional, Huttenlocher, Anna, additional, Hymowitz, Sarah G., additional, Ihle, James N., additional, Imler, Jean-Luc, additional, Irvine, R.F., additional, Isacoff, Ehud Y., additional, Iturrioz, Xavier, additional, Iversen, Lars F., additional, Iyengar, Ravi, additional, Jackson, Stephen P., additional, Jan, Lily Yeh, additional, Janiak-Spens, Fabiola, additional, Janmey, Paul A., additional, Jansen, Peter Gildsig, additional, Jarriault, Sophie, additional, Javitch, Jonathan A., additional, Jensen, Elwood V., additional, Jepsen, Kristen, additional, Jones, E. Yvonne, additional, Jones, Katherine A., additional, Jordan, J. Dedrick, additional, Joseph, Jomon, additional, Justement, Louis B., additional, Kafri, Yariv, additional, Kahn, Richard A., additional, Kang, Shin W., additional, Karlin, Arthur, additional, Kast-Woelbern, Heidi R., additional, Kaufman, Randal J., additional, Kazlauskas, Andrius, additional, Keen, James H., additional, Kemler, Rolf, additional, Kemp, Bruce E., additional, Kennedy, Mary B., additional, Kennedy, Matthew A., additional, Kikkawa, Ushio, additional, Kim, Albert H., additional, Kim, Soo-A, additional, Kim, Sung-Hou, additional, Kim, Youngjoo, additional, King-Jones, Kirst, additional, Kintner, Chris, additional, Kivimäe, Saul, additional, Klee, Claude B., additional, Klein, Rüdiger, additional, Kleppisch, Thomas, additional, Kliewer, Steven A., additional, Klinghoffer, Richard A., additional, Knoblich, Juergen A., additional, Kobe, Bostjan, additional, Kochs, George, additional, Kong-Beltran, Monica, additional, König, Rolf, additional, Koong, Albert C., additional, Korc, Murray, additional, Kornitzer, Daniel, additional, Kossiakoff, Anthony A., additional, Kotera, Jun, additional, Kovalenko, M.V., additional, Kozasa, Tohru, additional, Kozlov, Sergei, additional, Kozminski, Keith G., additional, Krugmann, Sonja, additional, Kuriyan, John, additional, Kurokawa, Riki, additional, Kwong, Peter D., additional, Lai, Wi S., additional, Lamar, Elise, additional, Lambert, Millard H., additional, Lambright, David G., additional, Lancet, Doron, additional, Landry, Reiko, additional, Langdon, Wallace Y., additional, Langeberg, Lorene K., additional, Lasko, Paul, additional, Latham, Vaughn, additional, Lavin, Martin F., additional, Lease, Kevin A., additional, Leffler, Hakon, additional, Lemmon, Mark A., additional, Leonard, Ann E., additional, Levitzki, Alexander, additional, Liao, Hong-Jun, additional, Liaw, Lucy, additional, Liberi, Giordano, additional, Lickert, Heiko, additional, Liddington, Robert C., additional, Lincoln, Thomas M., additional, Linder, Jürgen U., additional, Linder, Maurine E., additional, Liu, Hui, additional, Liu, Zhengchang, additional, Lohela, Marja K., additional, Louie, Sarah H., additional, Luttrell, Deirdre K., additional, Luttrell, Louis M., additional, Lyons, Karen M., additional, Macaulay, S. Lance, additional, Maceyka, Michael, additional, Maciag, Thomas, additional, Macian, Fernando, additional, MacKintosh, Carol, additional, MacLennan, David H., additional, Mahmood, Nadir A., additional, Malbon, Craig C., additional, Malik, Sohail, additional, Man, Orna, additional, Manahan, Carol L., additional, Mandinova, Anna, additional, Manganiello, Vincent C., additional, Manley, James L., additional, Mann, Matthias, additional, Manning, Gerald, additional, Manser, Ed, additional, Margeta-Mitrovic, Marta, additional, Margolskee, Robert F., additional, Marinissen, Julia, additional, Mariuzza, Roy A., additional, Marmor, Mina D., additional, Martin, G. Steven, additional, Martin, Karen H., additional, Martinez, Sergio E., additional, Mathews, Michael B., additional, Mayer, Bruce J., additional, Mayer, Mark L., additional, Mazzoni, Maria R., additional, McCormick, Frank, additional, McGowan, Clare H., additional, McKay, Melissa M., additional, McKeehan, Wallace L., additional, McLean, Alison J., additional, Means, Anthony R., additional, Meili, Ruedi, additional, Meng, Jingwei, additional, Merchant, Mark, additional, Mercurio, Frank, additional, Milligan, Graeme, additional, Ming, Guo-Li, additional, Minor, Daniel L., additional, Moghal, Nadeem, additional, Møller, Neils Peter H., additional, Mongillo, Marco, additional, Montminy, Marc, additional, Moon, Randall T., additional, Morimoto, Richard I., additional, Moss, Stephen E., additional, Mott, Helen R., additional, Mouta, Carla, additional, Muda, Marco, additional, Mumby, Marc C., additional, Murphy, Gretchen A., additional, Muzi-Falconi, Marco, additional, Nagaraj, Raghavendra, additional, Nahorski, Stefan R., additional, Nairn, Angus C., additional, Nash, Piers, additional, Neel, Benjamin G., additional, Newton, Alexandra C., additional, Nishizuka, Yasutomi, additional, Noel, Joseph P., additional, Nollen, Ellen A.A., additional, Nooren, Irene M.A., additional, O'Connor, Rodney, additional, Offermanns, Stefan, additional, Olender, Tsviya, additional, Ong, Shao-En, additional, Owen, Darerca, additional, Pagliari, Lisa J., additional, Pao, Lily, additional, Papaconstantinou, John, additional, Pardo, Leonardo, additional, Park, Hay-Oak, additional, Park, Young Chul, additional, Parker, Peter J., additional, Parsons, J. Thomas, additional, Passner, J.M., additional, Pawson, Tony, additional, Pelliccioli, Achille, additional, Perez-Polo, J. Regino, additional, Perrimon, Norbert, additional, Petite, Fabrice G., additional, Petroulakis, Emmanuel, additional, Pfaff, Samuel L., additional, Piehler, Jacob, additional, Pike, Linda J., additional, Pinkoski, Michael J., additional, Pixley, Fiona J., additional, Plevani, Paolo, additional, Poo, Mu-ming, additional, Pozzan, Tullioi, additional, Prescott, Stephen M., additional, Prudovsky, Igor, additional, Putney, James W., additional, Radimerski, Thomas, additional, Radzio-Andzelm, Elzbieta, additional, Ram, Prahlad T., additional, Rameh, Lucia, additional, Ramljak, Danica, additional, Ranscht, Barbara, additional, Rao, Anjana, additional, Raport, Carol J., additional, Reeves, Jacqueline D., additional, Rehman, Holger, additional, Reichman, Trevor W., additional, Reiter, Eric, additional, Resnick, Michael A., additional, Reth, Michael, additional, Rhee, Sue Goo, additional, Richter, Joel D., additional, Rietze, Rodney L., additional, Rini, James M., additional, Ripperger, Jürgen A., additional, Rizo, Josep, additional, Robishaw, Janet D., additional, Roderick, H. Llewelyn, additional, Roeder, Robert G., additional, Rohrschneider, Larry R., additional, Ron, David, additional, Rosenfeld, Michael G., additional, Rosenfeldt, Hans, additional, Rossman, Kent L., additional, Roth, Christopher B., additional, Rudolph, Markus G., additional, Ruppelt, Anja, additional, Saez, Lino, additional, Sakmar, Thomas P., additional, Salvesen, Guy S., additional, Sassone-Corsi, Paolo, additional, Saxe, Charles L., additional, Schäfer, Beat W., additional, Schibler, Ueli, additional, Schindler, Christian W., additional, Schmelzle, Tobias, additional, Schmid, Sandra L., additional, Schmidt, Anja, additional, Schmidt, Eric F., additional, Schreiber, Gideon, additional, Schultz, Joachim E., additional, Schwaller, Beat, additional, Schwamborn, Klaus, additional, Schwartz, Thue, additional, Schwindinger, William F., additional, Scita, Giorgio, additional, Scott, John D., additional, Scott, Shaun, additional, Seebeck, Thomas, additional, Serhan, Charles N., additional, Shabb, John B., additional, Shaw, Andrey S., additional, Shears, Stephen B., additional, Shenolikar, Shirish, additional, Shi, Lei, additional, Shin, Chanseok, additional, Shiozaki, Kazuhiro, additional, Shokat, Kevan M., additional, Shuttleworth, Trevor J., additional, Siderovski, David P., additional, Siegelbaum, Steven A., additional, Silverstein, Adam M., additional, Singer, Robert H., additional, Skinner, Michael K., additional, Slack-Davis, Jill K., additional, Smerdon, Stephen J., additional, Smith, Graeme C.M., additional, Smits, Guillaume, additional, Smolik, Sarah M., additional, Smotrys, Jessica E., additional, Smyth, Emer M., additional, Snyder, Jason T., additional, Sogame, Naoko, additional, Soldi, Raffaella, additional, Sondek, John, additional, Sonenberg, Nahum, additional, Sonneberg, Erica Dutil, additional, Sparrow, Lindsay G., additional, Spiegel, Sarah, additional, Sprang, Stephen R., additional, Srivastava, Deepak, additional, Stanfield, Robyn L., additional, Stanley, E. 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2003
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43. Protein kinase G is not essential to NO-cGMP modulation of basal tone in rat pulmonary circulation

Author

Fouty, Brian, Komalavilas, Padmini, Muramatsu, Masashi, Cohen, Alan, McMurtry, Ivan F., Lincoln, Thomas M., and Rodman, David M.

Subjects
Cyclic guanylic acid -- Physiological aspects, Protein kinases -- Physiological aspects, Lungs -- Blood-vessels, Blood vessels -- Dilatation, Nitric oxide -- Physiological aspects, Biological sciences
Abstract

Isolated perfused lungs from both normotensive and hypertensive rats were used in the investigation of the role of protein kinase G in the nitric oxide (NO) and cyclic guanosine monophosphate (cGMP) regulation of pulmonary vascular tone. Results show that blocking the synthesis of cGMP increased the hypoxia-induced vasoconstriction but inhibiting protein kinase G (PKG) had no effect. This suggests that while cGMP has a role in NO modulation of vascular tone in the lungs, PKG does not.

Published
1998

48. Impaired cyclic nucleotide-dependent vasorelaxation in human umbilical artery smooth muscle

Author

Bergh, Constance M., Brophy, Colleen M., Dransfield, Daniel T., Lincoln, Thomas, Goldenring, James R., and Rasmussen, Howard

Subjects
Vascular smooth muscle -- Research, Vasoconstrictors -- Physiological aspects, Umbilical arteries -- Physiological aspects, Biological sciences
Abstract

A comparative study of the bovine carotid artery smooth muscle (BCASM)- and human umbilical artery smooth muscle (HUASM) responses to contractile and relaxant agents reveals that passive relaxations of both smooth muscle types are normal after a washout of vasoactive agents. HUASM does not exhibit active relaxation, unlike BCASM, probably due to changes induced in cyclic nucleotide-dependent kinases in HUASM. The active relaxation refractoriness may lead to the vasospasm that appears due to parturition in umbilical vasculature.

Published
1995

50. Inhibition of smooth muscle cell growth by nitric oxide and activation of cAMP-dependent protein kinase by cGMP

Author

Cornwell, Trudy L., Arnold, Elizabeth, Boerth, Nancy J., and Lincoln, Thomas M.

Subjects
Cell proliferation -- Research, Protein kinases -- Physiological aspects, Nitric oxide -- Physiological aspects, Cyclic adenylic acid -- Physiological aspects, Biological sciences
Abstract

A study of the NO- and cGMP-dependent inhibition of cultured rat aortic smooth muscle cells (SMC) suggested that the activation of cAMP-dependent protein kinase (cAMP kinase) by cGMP was responsible for the growth-suppression of rat aortic SMC in an NO-dependent manner. Interleukin-1beta induced a rise in cGMP that stimulated cAMP kinase activity. cAMP kinase activity decreased with the introduction of factors that prevent NO and cGMP production.

Published
1994

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