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19 results on '"Rahman, Nadeem"'

2. Hypertriglyceridemia in Critically Ill Patients With SARS-CoV-2 Infection

Author

El Nekidy, Wasim S., Shatnawei, Abdullah, Abdelsalam, Manal M., Hassan, Mariam, Dajani, Ruba Z., Salem, Nouran, St. John, Terrence J. Lee, Rahman, Nadeem, Hamed, Fadi, and Mallat, Jihad

Abstract

Background Patients with SARS-CoV-2 infection could develop severe disease requiring critical care admission. Case reports indicated high incidence of hypertriglyceridemia (HTG) in critically ill patients infected with SARS-CoV-2, which might be related to the drugs.Objective We sought to determine the risk factors associated with HTG in this population and to investigate the relationship between HTG and lipase.Methods A retrospective observational study was conducted at our hospital between March 1 and June 30, 2020. Patients were included if they were ≥18 years old, admitted to the intensive care unit (ICU), tested positive for SARS-CoV-2, and had triglycerides (TG) checked during their hospital stay.Results Of the 111 critically ill patients, 103 patients were included. Males comprised 88.3% of the sample. The median TG at baseline was 197.4 (IQR: 139.8-283) mg/dL. The lipase median level at baseline was 23.00 (IQR: 0.00-69.50) IU/L. The results of the mixed-effects logistic regression analysis indicated that patient-level variables, favipiravir use, blood glucose level, and propofol use were significantly associated with HTG. There was no relationship between lipase and TG levels over time. Furthermore, TG concentrations over time showed a similar trend to inflammatory markers.Conclusion and Relevance The incidence of clinically significant HTG was high and was associated with propofol and favipiravir use. HTG might reflect the high inflammatory state in these patients. Clinicians should look at the full picture before changing therapies based only on HTG. Our findings need to be replicated in a larger prospective study.

Published
2022
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4. Physiology and Pharmacology of Erectile Dysfunction.

Author

Klein, Eric A., Broderick, Gregory A., Carrion, Rafael, Bochinski, Derek, Rahman, Nadeem, and Lue, Tom

Abstract

Erectile dysfunction affects a significant proportion of the male population, making it a common urological disorder. It is defined as the inability to obtain or maintain an erection that is sufficient for satisfactory sexual intercourse. Many factors contribute to erectile physiology and pathophysiology. Much of the current understanding of erectile physiology was acquired in the 1980s and 1990s. In addition to the role of smooth muscle in regulating arterial and venous flow, the three-dimensional structure of the tunica albuginea and its role in venous occlusion have been elucidated. Pivotal research identified the importance of nitric oxide (NO), which is the major neurotransmitter for penile tumescence, and its counterpart, the phosphodiesterases (PDEs), which return the penis to a flaccid state. Subsequent studies have shown an important distinction between neurogenic- and endothelial-generated NO, in that the latter essentially helps in maintaining penile erection. Moreover, the role of endothelium in regulating smooth muscle tone and the intercellular link by means of gap junctions have also been uncovered. More recently, research has shown that changes to the downstream signaling pathways (RhoA/Rho-kinase pathway) may be of physiological importance in regulating cavernosal smooth muscle tone. In the pathophysiology of erectile dysfunction, the changes in the smooth muscle, endothelium, and fibroelastic framework with hypertension, diabetes, atherosclerosis, and aging have also been identified. The anatomy and physiology of erectile function are discussed in detail in this chapter (1). [ABSTRACT FROM AUTHOR]

Published
2005
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5. A Teenager Presents With Fulminant Hepatic Failure and Acute Hemolytic Anemia

Author

Bose, Somnath, Sonny, Abraham, and Rahman, Nadeem

Abstract

A teenager was admitted to an outside hospital ED following an episode of melena. He had been complaining of intermittent abdominal pain, nausea, malaise, and easy fatigability for 2 months, with significant worsening of symptoms 2 weeks prior to this episode. He had no significant medical, surgical, or family history. On presentation at the outside ED, he was found to be profoundly icteric and encephalopathic. Initial laboratories suggested anemia, acute kidney injury, and acute liver failure, leading to a presumptive diagnosis of acute fulminant liver failure necessitating transfer to our institution.

Published
2015
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6. Mechanism of Continence After Repair of Posterior Urethral Disruption: Evidence of Rhabdosphincter Activity.

Author

Whitson, Jared M., McAninch, Jack W., Tanagho, Emil A., Metro, Michael J., and Rahman, Nadeem U.

Subjects
URINARY organs, WOUNDS & injuries, URINARY incontinence, URINATION disorders
Abstract

Purpose: Controversy exists regarding continence mechanisms in patients who undergo posterior urethral reconstruction after pelvic fracture. Some evidence suggests that continence after posterior urethroplasty is maintained by the bladder neck or proximal urethral mechanism without a functioning distal mechanism. We studied distal urethral sphincter activity in patients who have undergone posterior urethroplasty for pelvic fracture. Materials and Methods: A total of 12 patients who had undergone surgical repair of urethral disruption involving the prostatomembranous region underwent videourodynamics with urethral pressure profiles at rest, and during stress and hold maneuvers. Bladder pressure and urethral pressure, including proximal and distal urethral sphincter activity and pressure, were assessed in each patient. Results: All 12 patients had daytime continence of urine postoperatively with a followup after anastomotic urethroplasty of 12 to 242 months (mean 76). Average maximum urethral pressure was 71 cm H2O. Average maximum urethral closure pressure was 61 cm H2O. The average urethral pressure seen during a brief hold maneuver was 111 cm H2O. Average functional sphincteric length was 2.5 cm. Six of the 12 patients had clear evidence of distal urethral sphincter function, as demonstrated by the profile. Conclusions: Continence after anastomotic urethroplasty for posttraumatic urethral strictures is maintained primarily by the proximal bladder neck. However, there is a significant contribution of the rhabdosphincter in many patients. [Copyright &y& Elsevier]

Published
2008
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7. Platelet-Derived Growth Factor Receptor Association with Na+/H+Exchanger Regulatory Factor Potentiates Receptor Activity

Author

Maudsley, Stuart, Zamah, A. Musa, Rahman, Nadeem, Blitzer, Jeremy T., Luttrell, Louis M., Lefkowitz, Robert J., and Hall, Randy A.

Abstract

ABSTRACTPlatelet-derived growth factor (PDGF) is a potent mitogen for many cell types. The PDGF receptor (PDGFR) is a receptor tyrosine kinase that mediates the mitogenic effects of PDGF by binding to and/or phosphorylating a variety of intracellular signaling proteins upon PDGF-induced receptor dimerization. We show here that the Na+/H+exchanger regulatory factor (NHERF; also known as EBP50), a protein not previously known to interact with the PDGFR, binds to the PDGFR carboxyl terminus (PDGFR-CT) with high affinity via a PDZ (PSD-95/Dlg/Z0-1 homology) domain-mediated interaction and potentiates PDGFR autophosphorylation and extracellular signal-regulated kinase (ERK) activation in cells. A point-mutated version of the PDGFR, with the terminal leucine changed to alanine (L1106A), cannot bind NHERF in vitro and is markedly impaired relative to the wild-type receptor with regard to PDGF-induced autophosphorylation and activation of ERK in cells. NHERF potentiation of PDGFR signaling depends on the capacity of NHERF to oligomerize. NHERF oligomerizes in vitro when bound with PDGFR-CT, and a truncated version of the first NHERF PDZ domain that can bind PDGFR-CT but which does not oligomerize reduces PDGFR tyrosine kinase activity when transiently overexpressed in cells. PDGFR activity in cells can also be regulated in a NHERF-dependent fashion by stimulation of the ß2-adrenergic receptor, a known cellular binding partner for NHERF. These findings reveal that NHERF can directly bind to the PDGFR and potentiate PDGFR activity, thus elucidating both a novel mechanism by which PDGFR activity can be regulated and a new cellular role for the PDZ domain-containing adapter protein NHERF.

Published
2000
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8. Platelet-Derived Growth Factor Receptor Association with Na+/H+Exchanger Regulatory Factor Potentiates Receptor Activity

Author

Maudsley, Stuart, Zamah, A. Musa, Rahman, Nadeem, Blitzer, Jeremy T., Luttrell, Louis M., Lefkowitz, Robert J., and Hall, Randy A.

Abstract

Platelet-derived growth factor (PDGF) is a potent mitogen for many cell types. The PDGF receptor (PDGFR) is a receptor tyrosine kinase that mediates the mitogenic effects of PDGF by binding to and/or phosphorylating a variety of intracellular signaling proteins upon PDGF-induced receptor dimerization. We show here that the Na+/H+exchanger regulatory factor (NHERF; also known as EBP50), a protein not previously known to interact with the PDGFR, binds to the PDGFR carboxyl terminus (PDGFR-CT) with high affinity via a PDZ (PSD-95/Dlg/Z0-1 homology) domain-mediated interaction and potentiates PDGFR autophosphorylation and extracellular signal-regulated kinase (ERK) activation in cells. A point-mutated version of the PDGFR, with the terminal leucine changed to alanine (L1106A), cannot bind NHERF in vitro and is markedly impaired relative to the wild-type receptor with regard to PDGF-induced autophosphorylation and activation of ERK in cells. NHERF potentiation of PDGFR signaling depends on the capacity of NHERF to oligomerize. NHERF oligomerizes in vitro when bound with PDGFR-CT, and a truncated version of the first NHERF PDZ domain that can bind PDGFR-CT but which does not oligomerize reduces PDGFR tyrosine kinase activity when transiently overexpressed in cells. PDGFR activity in cells can also be regulated in a NHERF-dependent fashion by stimulation of the β2-adrenergic receptor, a known cellular binding partner for NHERF. These findings reveal that NHERF can directly bind to the PDGFR and potentiate PDGFR activity, thus elucidating both a novel mechanism by which PDGFR activity can be regulated and a new cellular role for the PDZ domain-containing adapter protein NHERF.

Published
2000
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9. Assessment of 28-Day In-Hospital Mortality in Mechanically Ventilated Patients With Coronavirus Disease 2019: An International Cohort Study

Author

Li Bassi, Gianluigi, Suen, Jacky Y., White, Nicole, Dalton, Heidi J., Fanning, Jonathon, Corley, Amanda, Shrapnel, Sally, Hinton, Samuel, Forsyth, Simon, Parsons, Rex, Laffey, John G., Fan, Eddy, Bartlett, Robert, Brodie, Daniel, Burrell, Aidan, Chiumello, Davide, Elhazmi, Alyaa, Grasselli, Giacomo, Hodgson, Carol, Ichiba, Shingo, Luna, Carlos, Marwali, Eva, Merson, Laura, Murthy, Srinivas, Nichol, Alistair, Panigada, Mauro, Pelosi, Paolo, Torres, Antoni, Ng, Pauline Yeung, Ogino, Mark, Fraser, John F., Al-Dabbous, Tala, Alfoudri, Huda, Shamsah, Mohammed, Elapavaluru, Subbarao, Berg, Ashley, Horn, Christina, Schroll, Stephan, Velazco, Jorge, Ploskanych, Ludmyla, Fikes, Wanda, Meyer, Dan, Ehlers, Ashley, Shalabi-McGuire, Maysoon, Witt, Trent, Grazioli, Lorenzo, Lorini, Luca, Grandin, E. Wilson, Nunez, Jose, Reyes, Tiago, O’Briain, Diarmuid, Hunter, Stephanie, Ramanan, Mahesh, Affleck, Julia, Hurkadli Veerendra, Hemanth, Rai, Sumeet, Russell-Brown, Josie, Nourse, Mary, Joseph, Mark, Mitchell, Brook, Tenzer, Martha, Clinic, Carilion, Abe, Ryuzo, Jin Cho, Hwa, Jeong, In Seok, Brozzi, Nicolas, Mehkri, Omar, Krishnan, Sudhir, Duggal, Abhijit, Houltham, Stuart, Graf, Jerónimo, Diaz, Roderigo, Delgado, Camila, González, Joyce, Soledad Sanchez, Maria, Bautista Rincón, Diego Fernando, Marulanda Yanten, Angela Maria, Bustamante Duque, Melissa, Brodie, Daniel, Rusmawatiningtyas, Desy, Callahan, Maria, Taufik, M. Azhari, Yasmin Wardoyo, Elizabeth, Gunawan, Margaretha, Trisnaningrum, Nurindah S, Irawany, Vera, Rayhan, Muhammad, Panigada, Mauro, Pesenti, Antonia, Zanella, Alberto, Leone, Michela, Grasselli, Giacomo, Coppola, Silvia, Colombo, Sebastiano, Antonelli, Massimo, Carelli, Simone, Grieco, Domenico L., Asaki, Motohiro, Hoshino, Kota, Salazar, Leonardo, Duarte, Laura, Laffey, John, McNicholas, Bairbre, Cosgrave, David, McCaffrey, Joseph, Bone, Allison, Hakeem, Yusuff, Winearls, James, Tallott, Mandy, Thomson, David, Arnold-Day, Christel, Cupido, Jerome, Fanie, Zainap, Miller, Malcom, Seymore, Lisa, van Straaten, Dawid, Hssain, Ali Ait, Aliudin, Jeffrey, Alqahtani, Al-Reem, Mohamed, Khoulod, Mohamed, Ahmed, Tan, Darwin, Villanueva, Joy, Zaqout, Ahmed, Kurtzman, Ethan, Ademi, Arben, Dobrita, Ana, El Aoudi, Khadija, Segura, Juliet, Giwangkancana, Gezy, Ohshimo, Shinichiro, Hoshino, Koji, Hitoshi, Saito, Osatnik, Javier, Joosten, Anne, Torres, Antoni, Yang, Minlan, Motos, Ana, Luna, Carlos, Arancibia, Francisco, Williams, Virginie, Noel, Alexandre, Luque, Nestor, Huynh Trung, Trieu, Yacoub, Sophie, Fantini, Marina, Noemi Jorge García, Ruth, Chicote Alvarez, Enrique, Greti, Anna, Ceccato, Adrian, Sanchez, Angel, Loza Vazquez, Ana, Roche-Campo, Ferran, Franch-Llasat, Diego, Tuazon, Divina, Amato, Marcelo, Cassimiro, Luciana, Pola, Flavio, Ribeiro, Francis, Fonseca, Guilherme, Dalton, Heidi, Desai, Mehul, Osborn, Erik, Deeb, Hala, Arcadipane, Antonio, Martucci, Gennaro, Panarello, Giovanna, Vitiello, Chiara, Bianco, Claudia, Occhipinti, Giovanna, Rossetti, Matteo, Cuffaro, Raffaele, Cho Johns, Sung-Min, Shimizu, Hiroaki, Moriyama, Naoki, Kim, Jae-Burm, Kitamura, Nobuya, Elhazmi, Alyaa, Al-Hudaib, Abdullah, Gebauer, Johannes, Yokoyama, Toshiki, Al-Fares, Abdulrahman, Buabbas, Sarah, Alamad, Esam, Alawadhi, Fatma, Alawadi, Kalthoum, Tanaka, Hiro, Hashimoto, Satoru, Yamazaki, Masaki, Oh, Tak-Hyuck, Epler, Mark, Forney, Cathleen, Kruse, Louise, Feister, Jared, Williamson, Joelle, Grobengieser, Katherine, Gnall, Eric, Golden, Sasha, Caroline, Mara, Shapiro, Timothy, Karaj, Colleen, Thome, Lisa, Sher, Lynn, Vanderland, Mark, Welch, Mary, McDermott, Sherry, Brain, Matthew, Mineall, Sarah, Kimura, Dai, Brazzi, Luca, Sales, Gabriele, Ogston, Tawnya, Nagpal, Dave, Fischer, Karlee, Lorusso, Roberto, Esperatti, Mariano, O’Briain, Diarmuid, Carton, Edmund G., Sen, Ayan, Palacios, Amanda, Rainey, Deborah, Samoukoviv, Gordan, Campisi, Josie, Neumann, Emily, Seefeldt, Cassandra, Durham, Lucia, Falcucci, Octavio, Emmrich, Amanda, Guy, Jennifer, Johns, Carling, Buchtele, Nina, Schwameis, Michael, Stecher, Stephanie-Susanne, Singh, Delila, Barnikel, Michaela, Arenz, Lukas, Zaaqoq, Akram, Anh Galloway, Lan, Merley, Caitlin, Csete, Marc, Quesada, Luisa, Saba, Isabela, Kasugai, Daisuke, Hiraiwa, Hiroaki, Tanaka, Taku, Marwali, Eva, Purnama, Yoel, Rahayu Dewayanti, Santi, Ardiyan, Arifa Juzar, Dafsah, Siagian, Debby, Jakarta, Kita, Chen, Yih-Sharng, Ogino, Mark, Ratsep, Indrek, Oigus, Getter, Erikson, Kristo, Post, Andra-Maris, Enneveer, Lauri, Sillaots, Piret, Manetta, Frank, Mihelis, Effe, Claire Sarmiento, Iam, Narasimhan, Mangala, Varrone, Michael, Komats, Mamoru, Satyapriya, S. Veena, Bhatt, Amar, Mokadam, Nahush A., Uribe, Alberto, Gonzalez, Alicia, Shi, Haixia, McKeown, Johnny, Pasek, Joshua, Fiorda, Juan, Echeverria, Marco, Moreno, Rita, Zakhary, Bishoy, Cavana, Marco, Cucino, Alberto, Foti, Giuseppe, Giani, Marco, Russotto, Vincenzo, Chiumello, Davide, Castagna, Valentina, Dell’Amore, Andrea, Navalesi, Paolo, Shum, Hoi-Ping, Vuysteke, Alain, Usman, Asad, Acker, Andrew, Smood, Benjamin, Mergler, Blake, Sertic, Federico, Subramanian, Madhu, Sperry, Alexandra, Rizer, Nicolas, Burhan, Erlina, Rasmin, Menaldi, Akmal, Ernita, Sitompul, Faya, Lolong, Navy, Naivedh, Bhat, Erickson, Simon, Barrett, Peter, Dean, David, Daugherty, Julia, Loforte, Antonio, Khan, Irfan, Abraar Quraishi, Mohammed, DeSantis, Olivia, So, Dominic, Kandamby, Darshana, Mandei, Jose M., Natanael, Hans, YudhaLantang, Eka, Lantang, Anastasia, Oto Wijaya, Surya, Jung, Anna, Ng, George, Yiu Ng, Wing, Yeung Ng, Pauline, Tabah, Alexis, Ratcliffe, Megan, Duroux, Maree, Adachi, Shingo, Nakao, Shota, Blanco, Pablo, Prieto, Ana, Sánchez, Jesús, Nicholson, Meghan, Butt, Warwick, Serratore, Alyssa, Delzoppo, Carmel, Janin, Pierre, Yarad, Elizabeth, Totaro, Richard, Coles, Jennifer, Pujo, Bambang, Balk, Robert, Vissing, Andy, Kapania, Esha, Hays, James, Fox, Samuel, Yantosh, Garrett, Mishin, Pavel, Yuliarto, Saptadi, Hari Santoso, Kohar, Djajalaksana, Susanthy, Zainul Fatoni, Arie, Fukuda, Masahiro, Liu, Keibun, Pelosi, Paolo, Battaglini, Denise, Bastos, Diego, Gaião, Sérgio, Buchner, Jessica, Cho, Young-Jae, Hwan Lee, Su, Sakiyalak, Pranya, Nitayavardhana, Prompak, Seitz, Tamara, Arora, Rakesh, Kent, David, Parwar, Swapnil, Cheng, Andrew, Miller, Jennene, Fujitani, Shigeki, Shimizu, Naoki, Madhok, Jai, Owyang, Clark, Buscher, Hergen, Reynolds, Claire, Maasikas, Olavi, Beljantsev, Aleksan, Mihnovits, Vladislav, Akimoto, Takako, Aizawa, Mariko, Horibe, Kanako, Onodera, Ryota, Hodgson, Carol, Burrell, Aidan, Young, Meredith, Shekar, Kiran, McGuinness, Niki, Irvine, Lacey, Flynn, Brigid, Sugiyama, Kazuhiro, Shimizu, Keiki, Fan, Eddy, Exconde, Kathleen, Ichiba, Shingo, Lussier, Leslie, Lotz, Gösta, Maier, Lars, Dreier, Esther, Permata Kusumastuti, Neurinda, McCloskey, Colin, Dabaliz, Al-Awwab, Elshazly, Tarek B, Smith, Josiah, Szuldrzynski, Konstanty S., Bielański, Piotr, Wille, Keith, Murthy, Srinivas, Parhar, Ken Kuljit S., Fiest, Kirsten M., Codan, Cassidy, Shahid, Anmol, Fayed, Mohamed, Evans, Timothy, Garcia, Rebekah, Gutierrez, Ashley, Shimizu, Hiroaki, Song, Tae, Rose, Rebecca, Bennett, Suzanne, Richardson, Denise, Arora, Lovkesh, Rappapport, Kristina, Rudolph, Kristina, Sibenaller, Zita, Stout, Lori, Walter, Alicia, Herr, Daniel, Vedadi, Nazli, Bartlett, Robert, Pesenti, Antonio, Thompson, Shaun, Sindt, Lace, Rajnic, Sean, Ewald, Cale, Hoffman, Julie, Griffee, Matthew, Ciullo, Anna, Kida, Yuri, Ferrer Roca, Ricard, Riera, JordI, Contreras, Sofia, Alegre, Cynthia, Kay, Christy, Fischer, Irene, Renner, Elizabeth, Taniguci, Hayato, Fraser, John, Li Bassi, Gianluigi, Suen, Jacky, Barnett, Adrian, White, Nicole, Gibbons, Kristen, Forsyth, Simon, Corley, Amanda, Pearse, India, Hinton, Samuel, Abbate, Gabriella, Hassan, Halah, Heinsar, Silver, Karnik, Varun A, Ki, Katrina, O’Neill, Hollier F., Obonyo, Nchafatso, Reid, Janice D., Sato, Kei, Shekar, Kiran, Vuorinen, Aapeli, Wildi, Karin S., Wood, Emily S., Yerkovich, Stephanie, Lee, James, Plotkin, Daniel, Merson, Laura, Hartley, Emma, Lubis, Bastian, Ikeyama, Takanari, Bhaskar, Balu, Jung, Jae-Seung, McGuinness, Shay, Eastwood, Glenn, Rossi Marta, Sandra, Guarracino, Fabio, Guarracino, Fabio, Gerle, Stacy, Coxon, Emily, Claro, Bruno, Gonzalez-Stawinski, Gonzo, Loverde, Daniel, Patil, Namrata, Parrini, Vieri, McBride, Angela, Negaard, Kathryn, Ratsch, Angela, Abdelaziz, Ahmad, David Uribe, Juan, Peris, Adriano, Sanders, Mark, Emerson, Dominic, Kamal, Muhammad, Povoa, Pedro, Francis, Roland, Cherif, Ali, Joseph, Sunimol, Di Nardo, Matteo, Heard, Micheal, Kyle, Kimberly, Blackwell, Ray A, Piagnerelli, Michael, Biston, Patrick, Won Jeong, Hye, Smith, Reanna, Prawira, Yogi, Montrucchio, Giorgia, Rahman, Nadeem, Kakar, Vivek, Piagnerelli, Michael, Valenzuela Sarrazin, Josefa, Huerta Garcia, Arturo, Salterain, Nahikari, Meyns, Bart, Moreno, Marsha, Walia, Rajat, Mehta, Amit, Schweda, Annette, Supriatna, Moh, Yudo, Bhirowo, Kirakli, Cenk, Williams, Melissa, Hoon Kim, Kyung, Assad, Alexandra, Giraldo, Estefania, Karolak, Wojtek, Balik, Martin, Pocock, Elizabeth, Gajkowski, Evan, Masafumi, Kanamoto, Barrett, Nicholas, Takeyama, Yoshihiro, Park, Sunghoon, Amin, Faizan, Meilyana Andriyani, Fina, Sudakevych, Serhii, Ratsch, Angela, Vera, Magdalena, Cornejo, Rodrigo, Schwarz, Patrícia, Carolina Mardini, Ana, Serpa Neto, Ary, Villoldo, Andrea, Siciliano Colafranceschi, Alexandre, Ubeda, Alejandro, Granjean, Juan, Maria Garcia Melro, Lívia, Fioravante Romualdo, Giovana, Gaia, Diego, Souza, Helmgton, Bastos, Diego, Galas, Filomena, Máñez Mendiluce, Rafael, Sosa, Alejandra, Martinez, Ignacio, Kurosawa, Hiroshi, Salgado, Juan, Hugi-Mayr, Beate, Charbonneau, Eric, Salvatore Barzilai, Vitor, Monteiro, Veronica, Ribeiro de Souza, Rodrigo, Harper, Michael, Suzuki, Hiroyuki, Adams, Celina, Brieva, Jorge, Nyale, George, Saleem Eltatar, Faisal, Fatani, Jihan, Baeissa, Husam, Masri, Ayman AL, Rabie, Ahmed, Yee Hui, Mok, Yamane, Masahiro, Jung, Hanna, Mojisola, Ayorinde, Margaret, Nacpil, Newell, Ruck, Katja, Bakken, Rhonda, Jara, Claire, Felton, Tim, Berra, Lorenzo, Shah, Bobby, Chakraborty, Arpan, Cardona, Monika, Capatos, Gerry, Akkanti, Bindu, Orija, Abiodun, Jain, Harsh, Ito, Asami, Housni, Brahim, Low, Sennen, Iihara, Koji, Chavez, Joselito, Ramanathan, Kollengode, Zabert, Gustavo, Naidoo, Krubin, Seppelt, Ian, VanDyk, Marlice, MacDonald, Sarah, Ichiba, Shingo, McGregor, Randy, Siebenaler, Teka, Flynn, Hannah, Garcia-Diaz, Julia, Harmon, Catherine, Lofton, Kristi, Aokage, Toshiyuki, Shigemitsu, Kazuaki, Moscatelli, Andrea, Fiorentino, Giuseppe, Baumgaertel, Matthias, Eddy Mba, Serge, Assy, Jana, Hutahaean, Amelya, Roush, Holly, Sichting, Kay A, Alessandri, Francesco, Burns, Debra, Rabie, Ahmed, Salt, Gavin, Garabedian, Carl P., Millar, Jonathan, Sim, Malcolm, Mattke, Adrian, McAuley, Danny, Tadili, Jawad, Frenzel, Tim, Bar-Lavie, Yaron, Blandino Ortiz, Aaron, Stone, Jackie, Tabah, Alexis, Attokaran, Antony, Farquharson, Michael, Patel, Brij, Gunning, Derek, Baillie, Kenneth, Watson, Pia, Tamai, Kenji, Ketut Sajinadiyasa, Gede, Kanyawati, Dyah, Salgado, Marcello, Sassine, Assad, Yudo, Bhirowo, McCaul, Scott, Lee, Bongjin, Min Lee, Sang, Afek, Arnon, Iwashita, Yoshiaki, Munshi, Laveena, Pujo Semedi, Bambang, Permata, Neurinda, Kusumastuti, Metiva, Jack, Van Belle, Nicole, Marino, Daniel, Martin-Loeches, Ignacio, Buscher, Hergen, Ivatt, Lenny, Yew Woon, Chia, Mi Kang, Hyun, Smith, Timothy, James, Erskine, Al-Rawas, Nawar, Endo, Tomoyuki, Iwasaki, Yudai, Chan King-Chung, Kenny, Gudzenko, Vadim, Hugi-Mayr, Beate, Taccone, Fabio, Perdhana, Fajar, Lamarche, Yoan, Miguel Ribeiro, Joao, Bradic, Nikola, Van den Bossche, Klaartje, Lansink, Oude, Singh, Gurmeet, Debeuckelaere, Gerdy, Stelfox, Henry T., Yi, Cassia, Elia, Jennifer, Fang, Shu, Tribble, Thomas, Shankar, Shyam, Navalesi, Paolo, Padmanabhan, Raj, Hallinan, Bill, Paoletti, Luca, Leyva, Yolanda, Fykuda, Tatuma, Badulak, Jenelle, Koch, Jillian, Hackman, Amy, Janowaik, Lisa, Hernandez, Deb, Osofsky, Jennifer, Donadello, Katia, Lawang, Aizah, Fine, Josh, Davidson, Benjamin, and Oswaldo Razo Vazquez, Andres

Abstract

Supplemental Digital Content is available in the text.

Published
2021
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10. G Protein-coupled Receptor Kinase 6A Phosphorylates the Na+/H+Exchanger Regulatory Factor via a PDZ Domain-mediated Interaction*

Author

Hall, Randy A., Spurney, Robert F., Premont, Richard T., Rahman, Nadeem, Blitzer, Jeremy T., Pitcher, Julie A., and Lefkowitz, Robert J.

Abstract

The Na+/H+exchanger regulatory factor (NHERF) is constitutively phosphorylated in cells, but the site(s) of this phosphorylation and the kinase(s) responsible for it have not been identified. We show here that the primary site of constitutive NHERF phosphorylation in human embryonic kidney 293 (HEK-293) cells is Ser289, and that the stoichiometry of phosphorylation is near 1 mol/mol. NHERF contains two PDZ domains that recognize the sequence S/T-X-L at the carboxyl terminus of target proteins, and thus we examined the possibility that kinases containing this motif might associate with and phosphorylate NHERF. Overlay experiments and co-immunoprecipitation studies revealed that NHERF binds with high affinity to a splice variant of the G protein-coupled receptor kinase 6, GRK6A, which terminates in the motif T-R-L. NHERF does not associate with GRK6B or GRK6C, alternatively spliced variants that differ from GRK6A at their extreme carboxyl termini. GRK6A phosphorylates NHERF efficiently on Ser289in vitro, whereas GRK6B, GRK6C, and GRK2 do not. Furthermore, the endogenous “NHERF kinase” activity in HEK-293 cell lysates is sensitive to treatments that alter the activity of GRK6A. These data suggest that GRK6A phosphorylates NHERF via a PDZ domain-mediated interaction and that GRK6A is the kinase in HEK-293 cells responsible for the constitutive phosphorylation of NHERF.

Published
1999
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19. PSA screening: The controversy that refuses to die.

Author

Rahman, Nadeem

Subjects
PROSTATE-specific antigen, PROSTATE cancer
Abstract

The author discusses the controversies surrounding the prostate-specific antigen (PSA) screening in the U.S. that has provided a dramatic change in the presentation of the disease since its widespread use.

Published
2011

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