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19 results on '"Tseng, Yu-Chou"'

4. Data from Dysregulation of Mitochondrial Translation Caused by CBFB Deficiency Cooperates with Mutant PIK3CA and Is a Vulnerability in Breast Cancer

Author

Malik, Navdeep, primary, Kim, Young-Im, primary, Yan, Hualong, primary, Tseng, Yu-Chou, primary, du Bois, Wendy, primary, Ayaz, Gamze, primary, Tran, Andy D., primary, Vera-Ramirez, Laura, primary, Yang, Howard, primary, Michalowski, Aleksandra M., primary, Kruhlak, Michael, primary, Lee, Maxwell, primary, Hunter, Kent W., primary, and Huang, Jing, primary

Published
2023
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5. Table S2 from Dysregulation of Mitochondrial Translation Caused by CBFB Deficiency Cooperates with Mutant PIK3CA and Is a Vulnerability in Breast Cancer

Author

Malik, Navdeep, primary, Kim, Young-Im, primary, Yan, Hualong, primary, Tseng, Yu-Chou, primary, du Bois, Wendy, primary, Ayaz, Gamze, primary, Tran, Andy D., primary, Vera-Ramirez, Laura, primary, Yang, Howard, primary, Michalowski, Aleksandra M., primary, Kruhlak, Michael, primary, Lee, Maxwell, primary, Hunter, Kent W., primary, and Huang, Jing, primary

Published
2023
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6. Figure S1-9 from Dysregulation of Mitochondrial Translation Caused by CBFB Deficiency Cooperates with Mutant PIK3CA and Is a Vulnerability in Breast Cancer

Author

Malik, Navdeep, primary, Kim, Young-Im, primary, Yan, Hualong, primary, Tseng, Yu-Chou, primary, du Bois, Wendy, primary, Ayaz, Gamze, primary, Tran, Andy D., primary, Vera-Ramirez, Laura, primary, Yang, Howard, primary, Michalowski, Aleksandra M., primary, Kruhlak, Michael, primary, Lee, Maxwell, primary, Hunter, Kent W., primary, and Huang, Jing, primary

Published
2023
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7. Dysregulation of Mitochondrial Translation Caused by CBFB Deficiency Cooperates with Mutant PIK3CA and Is a Vulnerability in Breast Cancer

Author

Malik, Navdeep, primary, Kim, Young-Im, additional, Yan, Hualong, additional, Tseng, Yu-Chou, additional, du Bois, Wendy, additional, Ayaz, Gamze, additional, Tran, Andy D., additional, Vera-Ramirez, Laura, additional, Yang, Howard, additional, Michalowski, Aleksandra M., additional, Kruhlak, Michael, additional, Lee, Maxwell, additional, Hunter, Kent W., additional, and Huang, Jing, additional

Published
2023
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12. 1-03 Role of Activin A in human cancer cachexia (ACTICA study)

Author

Baracos, Vickie, Muscaritoli, Maurizio, Aversa, Zaira, Rossi Fanelli, Filippo, Loumaye, A, de Barsy, M, Nachit, M, Frateur, L, Lause, P, Van Maanen, A, Thissen, JP, Awasthi, R, Gillis, C, Liberman, S, Stein, B, Charlebois, P, Carli, F, Ahmad, Sultan, Chiche, Dan, Reza Kazemi-Bajestani, Seyyed Mohammad, Becher, Harald, Venner, Peter, North, Scott, Vickie, Baracos, Li, Yi-Ping, Zhang, Guohua, Ma, Jennifer, Hall, Derek, Patel, Devang, Robinson, Samantha, Di Marco, Sergio, Gallouzi, Imed-Eddine, Sartori, Roberta, Penna, Fabio, Costelli, Paola, Sandri, Marco, Gregorevic, Paul, Toth, Michael J, Miller, Mark S, Callahan, Damien M, Couch, Marion E, Dittus, Kim, Sharma, Mridula, Argilés, Josep M, Bedard, N, Wiles, B, Jammoul, S, Miao, M, Wykes, L, Coyne, E, Hallauer, PL, Hastings, KEM, Stretch, C, Baracos, VE, Chevalier, S, Wing, SS, Marchildon, François, Lala, Neena, St-Louis, Catherine, Wiper-Bergeron, Nadine, Santos Silva, Kleiton Augusto, Dong, Jiangling, Tweardy, David J, Mitch, William E, Zhang, Liping, Hall, Derek T, Ma, Jennifer F, Griss, Takla, Jones, Russell G, Marco, Sergio Di, Marks, Daniel L, Rudnicki, Michael A, Laine, Aaron, Narayanan, Sriram, Choy, Hak, Girard, Luc, Gazdar, Adi, Minna, John, Infante, Rodney, Iyengar, Puneeth, Petruzzelli, Michele, Schweiger, Martina, Rincon, Mercedes, Robertson, Graham, Zechner, Rudolf, Wagner, Erwin F, Pin, Fabrizio, Costamagna, Domiziana, Camperi, Andrea, Sampaolesi, Maurilio, He, Wei, Talbert, Erin, Londhe, Priya, Bloomston, Mark, Croce, Carlo, Guttridge, Denis, Breit, Samuel N, Tsai, Vicky WW, Manandhar, Rakesh, Lin, Shu, Sainsbury, Amanda, Brown, David A, Ferrara, Michele, Reano, Simone, Angelino, Elia, Sabry, Omar, Filigheddu, Nicoletta, Graziani, Andrea, Tsoli, Maria, Allen, John, Taylor, Ryland, Scwheiger, Martina, Swarbrick, Michael M, Ehteda, Anahid, Miekle, Peter, Molloy, Mark, Waning, David L, Mohammad, Khalid S, Reiken, Steven, Xie, Wenjun, Marks, Andrew R, Guise, Theresa A, Moya, Rosita, Zhao, Chunfang, Davies, Joanna D, Carson, James, Everett Couch, Marion, Stecher, Michael, El Mouelhi, Mohamed, Tseng, Yu-Chou, Kulp, Samuel K, Lai, I-Lu, Hsu, En-Chi, He, Wei A, Frankhouser, David E, Yan, Pearlly S, Mo, Xiaokui, Lesinski, Gregory B, Marcucci, Guido, Guttridge, Denis C, Bekaii-Saab, Tanios, Chen, Ching-Shih, Haddad, AHI Al, Al-Azwani, EK, Mahamoud, Y, Safi, F, Salhat, H El, Malek, JA, Adrian, TE, Fearon, K, Temel, J, Currow, D, Gleich, L, Friend, J, Abernethy, A, Garcia, Jose M, Dubé, A, Patoine, D, Lemire, BB, Thériault, M-E, Ribeiro, F, Debigaré, R, Maltais, F, Smuder, Ashley J, Min, Kisuk, Kwon, Oh-Sung, Wiggs, Michael P, Sollanenk, Kurt J, Christou, Demetra D, Yoo, Jeung-Ki, Hwang, Moon-Hyon, Szeto, Hazel H, Kavazis, Andreas N, Powers, Scott K, Kroenke, Candyce H, Meyerhardt, Jeffrey A, Kwan, Marilyn L, Prado, Carla, Xiao, Jingjie, Weltzien, Erin, Castillo, Adrienne, Caan, Bette J, Guan, Chen, Giles, Kaitlin, Wing, Simon, Mazurak, Vera, Jagoe, R Thomas, Wiles, Benjamin, Miao, Miao, Coyne, Erin, Larose, Louise, Cybulsky, Andrey V, Wing, Simon S, Marino, Francesco Elia, Risbridger, Gail, Gold, Elspeth, Segatto, Marco, Fittipaldi, Raffaella, Caretti, Giuseppina, Lee, Hwabin, Fu, Dechen, Dwarkasing, JT, Boekschoten, MV, Argilès, JM, van Dijk, M, Busquets, S, Penna, F, Toledo, M, Laviano, A, Witkamp, RF, van Norren, K, Bédard, Nathalie, Plourde, Marie, Chevalier, Stéphanie, Lala-Tabbert, Neena, Marchildon, Francois, Torabi, S, Glare, P, Plodkowski, A, Margaron, Yoran, Fernandes, Mathieu, Morales, Delphine, Poydenot, Pauline, Menager, Pauline, Fuchs, Alexandra, Degot, Sébastien, Calore, Federica, Canella, Alessandro, Croce, Carlo M, Srinivasan, Kalayarasan, Pulliparracharuvil, Suprabha, Meyer, Jeffrey, Scherer, Philipp E, Kambadur, Ravi, Martinelli, Giulia B, Talamini, Laura, Previdi, Sara, Piccirillo, Rosanna, Jafri, Syed H, Previgliano, Carlos, Khandelwal, Keerti, Shi, Runhua, Mills, Glenn, Amato, Robert, Coats, Valérie, Ribeiro, Fernanda, Tremblay, Lise, Lacasse, Yves, Maltais, François, Saey, Didier, AL Vigano, Antonio, Ciutto, Lorella, Tomasso, Jonathan Di, Kilgour, Robert D, Morais, José A, Borod, Manuel, Almasud, A, Giles, K, Baracos, V, Guan, L, Mazurak, V, Khanuja, Jasleen, Gresham, Gillian, Osipov, Arsen, Tan, Carlyn-Rose, Tuli, Richard, Hendifar, Andrew, Narasimhan, Ashok, Greiner, Russell, Yasui, Yutaka, Bathe, Oliver, Fearon, Kenneth, Damaraju, Sambasivarao, Banh, Taylor, Kliewer, Kara, Hsiao, Yung-Hsuan, Belury, Martha A, Caan, Bette, Quesenberry, Charles, Kwan, Marilyn, Prado, Carla MM, Baracos, Vickie E, Birdsell, Laura, Stuyckens, Kim, Park, Youn Choi, Parekh, Trilok, Sawyer, Michael B, Wu, C, Fernandez, SA, Criswell, T, Chidiac, T, Guttridge, D, Villalona-Calero, M, Bekaii-Saab, T, Khan, Sarah, ALVigano, Antonio, Matos-Neto, EM, Figuerêdo, RG, Camargo, RG, Lima, JDCC, Alves, MJ, Riccardi, D, Alcantara, PS, Pinhata, J, Maximiano, L, Seelaender, M, Lamarche, Émilie, Au, Ernie D, Desai, Aditya P, Koniaris, Leonidas G, Zimmers, Teresa A, Manring, Heather, Weisleder, Noah, Okamura, Heidi, Frankhouser, David, Yan, Pearlly, Tomasso, Jonathan di, Fabbro, Egidio G Del, Davis, Mellar P, Fearon, Kenneth CH, Jatoi, Aminah A, Vigano, Antonio, Putman, Ted, Kezhuo, Zhang, Sladek, Robert, Enjiu, LM, Gomes, SP, Matos-Neto, E, Rossi-Fanneli, F, Seelaender, MC, Ebadi, Maryam, Mazurak, Vera C, Bhatia, Nikita, Padliya, Neerav D, Stadler, Volker, Dariani, Maghsoud, Hariri, Robert J, Parker, Valorie A, Matthews, Ryan R, Bonetto, Andrea, Puppa, Melissa, Kang, Kyung Shin, Mohammed, Khalid S, Robling, Alexander G, Toledo, Míriam, Oliva, Francesc, Luque, Melania, Betancourt, Angelica, Marmonti, Enrica, López-Soriano, Francisco J, Busquets, Sílvia, Theal, Rebecca, Jiang, Heng, Sanchez, Anthony, Hussain, Sabah N, Serpe, R, Madeddu, C, Gudiño, V, Gabba, S, Antoni, G, Macciò, A, and Banni, S

Subjects
Abstracts
Published
2015

13. Overcoming Resistance to Anabolic Selective Androgen Receptor Modulator (SARM) Therapy in Experimental Cancer Cachexia with Histone Deacetylase Inhibitor AR-42

Author

Tseng, Yu-Chou, primary, Liva, Sophia G., additional, Dauki, Anees M., additional, Sovic, Michael, additional, Henderson, Sally E., additional, Kuo, Yi-Chiu, additional, Benedict, Jason A., additional, Kulp, Samuel K., additional, Campbell, Moray, additional, Bekaii-Saab, Tanios, additional, Phelps, Mitchell A., additional, Chen, Ching-Shih, additional, and Coss, Christopher C., additional

Published
2017
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14. Preclinical Investigation of the Novel Histone Deacetylase Inhibitor AR-42 in the Treatment of Cancer-Induced Cachexia

Author

Samuel K. Kulp, Wei A. He, Gregory B. Lesinski, Denis C. Guttridge, En-Chi Hsu, Guido Marcucci, Tanios Bekaii-Saab, Ching-Shih Chen, Pearlly S. Yan, Xiaokui Mo, David Frankhouser, I-Lu Lai, Mark Bloomston, and Tseng Yu-Chou

Subjects
Cancer Research, Cachexia, Adipose tissue, Administration, Oral, Muscle Proteins, Pharmacology, Leukemia Inhibitory Factor, Ion Channels, Romidepsin, Tripartite Motif Proteins, Carcinoma, Lewis Lung, Mice, Medicine, Uncoupling Protein 3, Forkhead Box Protein O1, MEF2 Transcription Factors, Histone deacetylase inhibitor, Forkhead Transcription Factors, Phenylbutyrates, Oncology, Adipose Tissue, Colonic Neoplasms, Cytokines, medicine.drug, medicine.medical_specialty, medicine.drug_class, Ubiquitin-Protein Ligases, Protein degradation, Adenocarcinoma, Phenylbutyrate, Mitochondrial Proteins, Internal medicine, Weight Loss, Animals, Muscle Strength, Muscle, Skeletal, Vorinostat, SKP Cullin F-Box Protein Ligases, business.industry, Interleukin-6, Lipase, Neoplasms, Experimental, medicine.disease, Receptors, Interleukin-6, Survival Analysis, Histone Deacetylase Inhibitors, Endocrinology, Gene Expression Regulation, business, Leukemia inhibitory factor
Abstract

BACKGROUND Cancer cachexia is a debilitating condition that impacts patient morbidity, mortality, and quality of life and for which effective therapies are lacking. The anticachectic activity of the novel HDAC inhibitor AR-42 was investigated in murine models of cancer cachexia. METHODS The effects of AR-42 on classic features of cachexia were evaluated in the C-26 colon adenocarcinoma and Lewis lung carcinoma (LLC) models. Effects on survival in comparison with approved HDAC inhibitors (vorinostat, romidepsin) were determined. The muscle metabolome and transcriptome (by RNA-seq), as well as serum cytokine profile, were evaluated. Data were analyzed using mixed effects models, analysis of variance, or log-rank tests. All statistical tests were two-sided. RESULTS In the C-26 model, orally administered AR-42 preserved body weight (23.9±2.6 grams, AR-42-treated; 20.8±1.3 grams, vehicle-treated; P = .005), prolonged survival (P < .001), prevented reductions in muscle and adipose tissue mass, muscle fiber size, and muscle strength and restored intramuscular mRNA expression of the E3 ligases MuRF1 and Atrogin-1 to basal levels (n = 8). This anticachectic effect, confirmed in the LLC model, was not observed after treatment with vorinostat and romidepsin. AR-42 suppressed tumor-induced changes in inflammatory cytokine production and multiple procachexia drivers (IL-6, IL-6Rα, leukemia inhibitory factor, Foxo1, Atrogin-1, MuRF1, adipose triglyceride lipase, uncoupling protein 3, and myocyte enhancer factor 2c). Metabolomic analysis revealed cachexia-associated changes in glycolysis, glycogen synthesis, and protein degradation in muscle, which were restored by AR-42 to a state characteristic of tumor-free mice. CONCLUSIONS These findings support further investigation of AR-42 as part of a comprehensive therapeutic strategy for cancer cachexia.

Published
2014

15. Abstract 5540: Preclinical investigation of the novel histone deacetylase (HDAC) inhibitor AR-42 in the treatment of cancer-induced cachexia

Author

Tseng, Yu-Chou, primary, Kulp, Samuel, additional, Lai, I-Lu, additional, He, Wei, additional, Bundschuh, Ralf, additional, Frankhouser, David, additional, Yan, Pearlly, additional, Guttridge, Denis, additional, Marcucci, Guido, additional, Chen, Ching-Shih, additional, and Bekaii-Saab, Tanios, additional

Published
2014
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17. Preclinical Investigation of the Novel Histone Deacetylase Inhibitor AR-42 in the Treatment of Cancer-Induced Cachexia.

Author

Yu-Chou Tseng, Kulp, Samuel K., I-Lu Lai, En-Chi Hsu, Wei A. He, Frankhouser, David E., Yan, Pearlly S., Xiaokui Mo, Bloomston, Mark, Lesinski, Gregory B., Marcucci, Guido, Guttridge, Denis C., Bekaii-Saab, Tanios, Ching-Shih Chen, Tseng, Yu-Chou, Lai, I-Lu, Hsu, En-Chi, He, Wei A, Mo, Xiaokui, and Chen, Ching-Shih

Subjects
CANCER complications, PROTEIN metabolism, MUSCLE protein metabolism, ENZYME metabolism, ADENOCARCINOMA, ADIPOSE tissues, ANIMAL experimentation, CACHEXIA, CELL receptors, COLON tumors, CYTOKINES, ENZYME inhibitors, GENES, INTERLEUKINS, LIPASES, MEMBRANE proteins, MICE, MUSCLE strength, ORAL drug administration, SURVIVAL analysis (Biometry), TUMORS, WEIGHT loss, CARBOCYCLIC acids, SKELETAL muscle, IN vivo studies, DISEASE complications, PHARMACODYNAMICS, PREVENTION
Abstract

Background: Cancer cachexia is a debilitating condition that impacts patient morbidity, mortality, and quality of life and for which effective therapies are lacking. The anticachectic activity of the novel HDAC inhibitor AR-42 was investigated in murine models of cancer cachexia.Methods: The effects of AR-42 on classic features of cachexia were evaluated in the C-26 colon adenocarcinoma and Lewis lung carcinoma (LLC) models. Effects on survival in comparison with approved HDAC inhibitors (vorinostat, romidepsin) were determined. The muscle metabolome and transcriptome (by RNA-seq), as well as serum cytokine profile, were evaluated. Data were analyzed using mixed effects models, analysis of variance, or log-rank tests. All statistical tests were two-sided.Results: In the C-26 model, orally administered AR-42 preserved body weight (23.9±2.6 grams, AR-42-treated; 20.8±1.3 grams, vehicle-treated; P = .005), prolonged survival (P < .001), prevented reductions in muscle and adipose tissue mass, muscle fiber size, and muscle strength and restored intramuscular mRNA expression of the E3 ligases MuRF1 and Atrogin-1 to basal levels (n = 8). This anticachectic effect, confirmed in the LLC model, was not observed after treatment with vorinostat and romidepsin. AR-42 suppressed tumor-induced changes in inflammatory cytokine production and multiple procachexia drivers (IL-6, IL-6Rα, leukemia inhibitory factor, Foxo1, Atrogin-1, MuRF1, adipose triglyceride lipase, uncoupling protein 3, and myocyte enhancer factor 2c). Metabolomic analysis revealed cachexia-associated changes in glycolysis, glycogen synthesis, and protein degradation in muscle, which were restored by AR-42 to a state characteristic of tumor-free mice.Conclusions: These findings support further investigation of AR-42 as part of a comprehensive therapeutic strategy for cancer cachexia. [ABSTRACT FROM AUTHOR]

Published
2015
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18. Application of Histone Deacetylase Inhibitor AR-42 in the Treatment of Cancer-induced Cachexia

Author

Tseng, Yu-Chou

Subjects
Pharmacy Sciences, Pharmacy Science
Abstract

Cancer is among the top five leading causes of death in the United States. Part of the contributing of death comes from cancer cachexia, a debilitating condition characterized by depletion of skeletal muscle with or without adipose tissue wasting, which leads to pronounced weight loss, weakness, fatigue, lower tolerance to chemotherapy and radiation treatment, and ultimately decreased survival. Cachexia occurs in more than 50% of cancer patients, and is particularly prevalent in pancreatic cancer patients, of whom over 80% suffer from cachexia. Thus, the development of effective therapies against cachexia has tremendous potential to improve quality of life and increase survival of pancreatic cancer patients. However, no effective treatments for cachexia currently exist.In this study, we report the in vivo efficacy of the HDAC inhibitor, AR-42, provided significant protective effects against cachexia in three different animal models of cancer-induced cachexia. AR-42, a histone deacetylase (HDAC) inhibitor, reduced cachexia-induced losses in skeletal muscle mass, adipose tissue mass, preserved muscle function and prolonged survival in C-26 tumor-bearing mice. Importantly, AR-42 was much more effective than two other HDAC inhibitors, vorinostat and romidepsin, to suppress cachexia induced muscle atrophy.Suppression of the mRNA expression of the E3 ligases Atrogin-1/MAFbx and MuRF1 in the skeletal muscle of tumor-bearing mice can be found in all AR-42 treated mice, which indicated the ability of AR-42 to inhibit cancer cachexia progression. Cytokine profiling and RNA-seq analyses revealed that the suppressive effect of AR-42 on cachectic muscle atrophy arises from its diverse effects on tumor-induced changes in inflammatory cytokine production and multiple transcriptional programs. Our previous studies indicated that AR-42 showed potent ability to suppress muscle catabolic effects in cancer cachexia models. Therefore, to further improve AR-42, we hypothesized that co-treat AR-42 with selective androgen receptor modulators (SARM) with effective anabolic effect on muscle, might potential enhance the efficacy against cancer cachexia. Non-steroidal, orally available, SARMs have recently been developed that demonstrate full agonist in anabolic tissues like skeletal muscle and bone but are devoid of the side effects associated with 5a-reductase and aromatase substrates. Clinically, GTX-024, has shown promising gains in fat free mass in cancer patients[1] but failed to demonstrate a clear functional benefit in a cachectic cancer population[2]. Here, we reported that GTx-024 alone cannot prevent cancer induced cachexia, however, once GTx-024 co-treated with relative low dose of AR-42, it can protect cancer cachexia induced losses of body weight, skeletal muscle weight, and adipose tissue in C-26 tumor bearing mice model. Consistent with the protective effect on muscle mass, handgrip dynamometry showed that AR-42 was able to preserve muscle function in combination treatment group comparing to vehicle control. We also found this synergistic effect was not GTx-024 dependent; both DHT and TFM-4AS-1 can repeat the protective effect co-treated with AR-42 in C-26 bearing mice model, but failed to achieve the protection when treated alone. Together, these results support further evaluation of combined AR-42 and SARMs administration as a potential treatment against cancer induced cachexia.

Published
2017

19. GABAA receptor endocytosis in the basolateral amygdala is critical to the reinstatement of fear memory measured by fear-potentiated startle.

Author

Lin HC, Tseng YC, Mao SC, Chen PS, and Gean PW

Subjects
6-Cyano-7-nitroquinoxaline-2,3-dione pharmacology, Adrenergic beta-Agonists pharmacology, Amygdala cytology, Amygdala drug effects, Analysis of Variance, Animals, Behavior, Animal drug effects, Biotinylation, Conditioning, Classical drug effects, Dynamins antagonists & inhibitors, Endocytosis drug effects, Excitatory Amino Acid Antagonists pharmacology, Extinction, Psychological drug effects, Immunoprecipitation, Isoproterenol pharmacology, Male, Maze Learning drug effects, Memory drug effects, PTEN Phosphohydrolase pharmacology, Patch-Clamp Techniques, Propranolol pharmacology, Rats, Rats, Sprague-Dawley, Recombinant Fusion Proteins pharmacology, Synaptic Transmission drug effects, Valine analogs & derivatives, Valine pharmacology, tat Gene Products, Human Immunodeficiency Virus pharmacology, Amygdala physiology, Endocytosis physiology, Fear, Memory physiology, Receptors, GABA-A metabolism, Reward
Abstract

Reinstatement represents a phenomenon that may be used to model the effects of retraumatization observed in patients with posttraumatic stress disorder (PTSD). In this study, we found intraperitoneal injection of the β-adrenergic receptor antagonist propranolol (10 mg/kg) 1 h before reinstatement training attenuated reinstatement of fear memory in rats. Conversely, reinstatement was facilitated by intra-amygdalar administration of β-adrenergic receptor agonist isoproterenol (Iso; 2 μg per side) 30 min before reinstatement training. The frequency and amplitude of the miniature IPSC (mIPSC) and the surface expression of the β3 and γ2 subunits of the GABA(A) receptor (GABA(A)R) were significantly lower in reinstated than in extinction rats, whereas the AMPA/NMDA ratio and the surface expression of GluR1 and GluR2 in the amygdala did not differ between groups. In amygdala slices, Iso-induced decrease in the surface β3 subunit of GABA(A) receptor was blocked by a Tat-conjugated dynamin function-blocking peptide (Tat-P4) pretreatment (10 μm for 30 min). By contrast, Tat-scramble peptide had no effect. Intravenous injection (3 μmol/kg) or intra-amygdalar infusion (30 pmol per side) of Tat-P4 interfered with reinstatement. Reinstatement increased the association between protein phosphatase 2A (PP2A) and the β3 subunit of the GABA(A)R, which was abolished by PP1/PP2A inhibitors okadaic acid and calyculin A. These results suggest the involvement of β-adrenergic receptor activation and GABA(A) receptor endocytosis in the amygdala for the reinstatement in fear memory.

Published
2011
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