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Journal articles on the topic 'Akt'

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Published: 4 June 2021

Last updated: 6 July 2024

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1

Matheny, Ronald W., and Martin L. Adamo. "Current Perspectives on Akt Akt-ivation and Akt-ions." Experimental Biology and Medicine 234, no. 11 (November 2009): 1264–70. http://dx.doi.org/10.3181/0904-mr-138.

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2

Gömöri, George, and Piroska Szántó. "Akt." World Literature Today 70, no. 1 (1996): 212. http://dx.doi.org/10.2307/40151976.

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3

Kotecha, Anish. "AKT question relating to Mental Health Act." InnovAiT: Education and inspiration for general practice 10, no. 11 (October 13, 2017): e139-e139. http://dx.doi.org/10.1177/1755738017728167.

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4

Abdel Kerim, Yasser. "AKT question relating to Mental Health Act." InnovAiT: Education and inspiration for general practice 10, no. 11 (October 13, 2017): e147-e147. http://dx.doi.org/10.1177/1755738017728180.

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5

Dunn, Ewan F., Rachel Fearns, and John H. Connor. "Akt Inhibitor Akt-IV Blocks Virus Replication through an Akt-Independent Mechanism." Journal of Virology 83, no. 22 (September 9, 2009): 11665–72. http://dx.doi.org/10.1128/jvi.01092-09.

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ABSTRACT Many viruses activate the phosphatidylinositol 3′-kinase (PI3k)/Akt intracellular signaling pathway to promote viral replication. We have analyzed whether a rapidly replicating rhabdovirus, vesicular stomatitis virus (VSV), requires the PI3k/Akt signaling pathway for its replication. Through the use of chemical inhibitors of PI3k and Akt, we show that VSV replication and cytopathic effects do not require activation of these kinases. Inhibitors that block the activating phosphorylations of Akt at threonine 308 (Thr308) and serine 473 (Ser473) did not inhibit VSV protein expression or the induction of the cytopathic effects of VSV. One compound, Akt inhibitor Akt-IV, inhibited the replication of VSV, respiratory syncytial virus, and vaccinia virus but increased the phosphorylation of Akt at positions Thr308 and Ser473 and did not inhibit Akt kinase activity in vitro. Together, our data suggest that the PI3k/Akt pathway is of limited relevance to the replication of VSV but that Akt inhibitor Akt-IV is a novel broad-spectrum antiviral compound with a mechanism differing from that of its previously reported effect on the PI3k/Akt pathway. Identification of other targets for this compound may define a new approach for blocking virus replication.

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6

Danwerth, Christopher. "Die virtuelle Hauptversammlung – Dritter Akt! Letzter Akt?" Die Aktiengesellschaft 66, no. 19 (October 1, 2021): r283—r284. http://dx.doi.org/10.9785/ag-2021-661903.

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7

Kumar, Chandra C., and Vincent Madison. "AKT crystal structure and AKT-specific inhibitors." Oncogene 24, no. 50 (November 2005): 7493–501. http://dx.doi.org/10.1038/sj.onc.1209087.

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8

Nandakumar, Michael. "AKT question relating to the Mental Capacity Act." InnovAiT: Education and inspiration for general practice 7, no. 12 (December 2014): 767. http://dx.doi.org/10.1177/1755738014557737.

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9

Abdel Kerim, Yasser. "AKT question relating to Mental Health Act assessments." InnovAiT: Education and inspiration for general practice 10, no. 11 (October 13, 2017): e145-e145. http://dx.doi.org/10.1177/1755738017728178.

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10

Nandakumar, M. "AKT question relating to Mental Health Act 2007." InnovAiT 4, no. 5 (May 1, 2011): 287. http://dx.doi.org/10.1093/innovait/inr077.

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11

Reneer, Mary Catherine, and Francesc Marti. "The balancing act of AKT in T cells." Frontiers in Biology 8, no. 2 (March 31, 2012): 160–74. http://dx.doi.org/10.1007/s11515-012-1202-6.

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12

Lawlor, Margaret A., and Dario R. Alessi. "PKB/Akt." Journal of Cell Science 114, no. 16 (August 15, 2001): 2903–10. http://dx.doi.org/10.1242/jcs.114.16.2903.

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The serine/threonine protein kinase PKB (also known as Akt) is thought to be a key mediator of signal transduction processes. The identification of PKB substrates and the role PKB phosphorylation plays in regulating these molecules have been a major focus of research in recent years. A recently developed motif-profile scoring algorithm that can be used to scan the genome for potential PKB substrates is therefore a useful tool, although additional considerations, such as the evolutionary conservation of the phosphorylation site, must also be taken into account. Recent evidence indicates that PKB plays a key role in cancer progression by stimulating cell proliferation and inhibiting apoptosis and is also probably a key mediator of insulin signalling. These findings indicate that PKB is likely to be a hot drug target for the treatment of cancer, diabetes and stroke. There are, however, a number of pitfalls of methodologies currently employed to study PKB function, and therefore caution should be used in interpretation of such experiments.

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13

Nandakumar, Michael. "AKT Questions." InnovAiT: Education and inspiration for general practice 5, no. 8 (August 2012): 455. http://dx.doi.org/10.1093/innovait/ins166.

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14

Roth, R. "Akt signalling." Biochemical Society Transactions 29, no. 3 (June 1, 2001): A59. http://dx.doi.org/10.1042/bst029a059a.

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15

Gough, N. R. "Inhibiting Akt." Science's STKE 2007, no. 411 (October 30, 2007): tw399. http://dx.doi.org/10.1126/stke.4112007tw399.

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16

Ray, L. B. "Regulating Akt." Science Signaling 2, no. 86 (September 1, 2009): ec293-ec293. http://dx.doi.org/10.1126/scisignal.286ec293.

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17

Humphrey, S. J., and D. E. James. "Uncaging Akt." Science Signaling 5, no. 223 (May 8, 2012): pe20. http://dx.doi.org/10.1126/scisignal.2003085.

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18

Ray, L. B. "Akt Acetylation." Science 333, no. 6043 (August 4, 2011): 675. http://dx.doi.org/10.1126/science.333.6043.675-c.

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19

Bucholc, Marta, and Maciej Komornik. "Finaler Akt." osteuropa 69, no. 12 (2019): 23–37. http://dx.doi.org/10.35998/oe-2019-0015.

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20

Lo, Hui-Wen. "Akt destabilizes p57Kip2: Akt at the converging crossroad?" Cell Cycle 12, no. 6 (March 7, 2013): 870–71. http://dx.doi.org/10.4161/cc.24155.

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21

Kim, Donghwa, Mei Sun, Lili He, Qing-Hua Zhou, Jun Chen, Xia-Meng Sun, Gerold Bepler, Said M. Sebti, and Jin Q. Cheng. "A Small Molecule Inhibits Akt through Direct Binding to Akt and Preventing Akt Membrane Translocation." Journal of Biological Chemistry 285, no. 11 (January 12, 2010): 8383–94. http://dx.doi.org/10.1074/jbc.m109.094060.

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22

Kim, Donghwa, Mei Sun, Lili He, Qing-Hua Zhou, Jun Chen, Xia-Meng Sun, Gerold Bepler, Said M. Sebti, and Jin Q. Cheng. "A small molecule inhibits Akt through direct binding to Akt and preventing Akt membrane translocation." Journal of Biological Chemistry 291, no. 43 (October 21, 2016): 22856. http://dx.doi.org/10.1074/jbc.a109.094060.

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23

Pawełczyk-Dura, Kamila. "Problemy opracowania akt miejskich na przykładzie akt miasta Pabianic." Archiwista Polski 27, no. 1 (102) (May 28, 2024): 69–86. http://dx.doi.org/10.4467/14259893arpl.23.005.19775.

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Description is one of the pillars of archival activity. It is supported by the multistage schemes of description, the methodological rules and experience of generations of archivists. However, it is hampered by the nature of the records, mainly the manner of its preparation, specific to a given historical period and the way of archiving. These factors are emphazed in the description of municipal records in general and the Records of the town Pabianice in particular – methodologically interesting archival constructs that are the subject of this paper.

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24

Wanas, Nisreen, Luma Mehdi, and Liqa Alzubaidi. "EVALUATION OF PHOSPHO-AKT IMMUNOHISTOCHEMICAL EXPRESSION IN PATIENTS WITH LARYNGEAL SQUAMOUS CELL CARCINOMA." Iraqi Journal of Medical Sciences 16, no. 2 (June 30, 2018): 177–81. http://dx.doi.org/10.22578/ijms.16.2.9.

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Background: Akt, is a serine/threonine protein kinase which act as an important regulator of cell proliferation and survival. The Akt complex is upregulated by phosphorylation producing phospho-Akt, which trigger a continued cell proliferation and survival and inhibit apoptosis, thereby promote cell survival. Objective: To evaluate the immunohistochemical expression of phosphorylated Akt (Phospho-Akt) in laryngeal squamous cell carcinoma (SCC) and to be correlated with different clinicopathological parameters. Methods: Phospho-Akt expression was investigated Immunohistochemically in 49 formalin-fixed paraffin embedded laryngeal SCC tissue sections collected from Teaching laboratories - Baghdad Medical City. Results: Phospho-Akt positive immunostaining appears in 57% of samples. Akt activation present in advanced stages of tumors with p value 0.02. Conclusion: The current findings may provide evidence that aberrant expression of Akt contributes to the pathogenesis (mechanism of disease development) of laryngeal SCC. Keywords: Akt, phospho-Akt, immunohistochemistry, laryngeal SCC, larynx Citation: Wanas NS, Mehdi LY, Alzubaidi LKA. Evaluation of phospho-AKt immunohistochemical expression in patients with laryngeal squamous cell carcinoma. Iraqi JMS. 2018; 16(2): 177-181. doi: 10.22578/IJMS.16.2.9

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25

Khalil, Md Imtiaz, Christopher Madere, Ishita Ghosh, Rosalyn M. Adam, and Arrigo De Benedetti. "Interaction of TLK1 and AKTIP as a Potential Regulator of AKT Activation in Castration-Resistant Prostate Cancer Progression." Pathophysiology 28, no. 3 (July 20, 2021): 339–54. http://dx.doi.org/10.3390/pathophysiology28030023.

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Prostate cancer (PCa) progression is characterized by the emergence of resistance to androgen deprivation therapy (ADT). AKT/PKB has been directly implicated in PCa progression, often due to the loss of PTEN and activation of PI3K>PDK1>AKT signaling. However, the regulatory network of AKT remains incompletely defined. Here, we describe the functional significance of AKTIP in PCa cell growth. AKTIP, identified in an interactome analysis as a substrate of TLK1B (that itself is elevated following ADT), enhances the association of AKT with PDK1 and its phosphorylation at T308 and S473. The interaction between TLK1 and AKTIP led to AKTIP phosphorylation at T22 and S237. The inactivation of TLK1 led to reduced AKT phosphorylation, which was potentiated with AKTIP knockdown. The TLK1 inhibitor J54 inhibited the growth of the LNCaP cells attributed to reduced AKT activation. However, LNCaP cells that expressed constitutively active, membrane-enriched Myr-AKT (which is expected to be active, even in the absence of AKTIP) were also growth-inhibited with J54. This suggested that other pathways (like TLK1>NEK1>YAP) regulating proliferation are also suppressed and can mediate growth inhibition, despite compensation by Myr-AKT. Nonetheless, further investigation of the potential role of TLK1>AKTIP>AKT in suppressing apoptosis, and conversely its reversal with J54, is warranted.

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26

Uko, Nne E., Osman F. Güner, Diane F. Matesic, and J. Phillip Bowen. "Akt Pathway Inhibitors." Current Topics in Medicinal Chemistry 20, no. 10 (May 19, 2020): 883–900. http://dx.doi.org/10.2174/1568026620666200224101808.

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Cancer is a devastating disease that has plagued humans from ancient times to this day. After decades of slow research progress, promising drug development, and the identification of new targets, the war on cancer was launched, in 1972. The P13K/Akt pathway is a growth-regulating cellular signaling pathway, which in many human cancers is over-activated. Studies have demonstrated that a decrease in Akt activity by Akt inhibitors is associated with a reduction in tumor cell proliferation. There have been several promising drug candidates that have been studied, including but not limited to ipatasertib (RG7440), 1; afuresertib (GSK2110183), 2; uprosertib (GSK2141795), 3; capivasertib (AZD5363), 4; which reportedly bind to the ATP active site and inhibit Akt activity, thus exerting cytotoxic and antiproliferative activities against human cancer cells. For most of the compounds discussed in this review, data from preclinical studies in various cancers suggest a mechanistic basis involving hyperactivated Akt signaling. Allosteric inhibitors are also known to alter the activity of kinases. Perifosine (KRX- 0401), 5, an alkylphospholipid, is known as the first allosteric Akt inhibitor to enter clinical development and is mechanistically characterized as a PH-domain dependent inhibitor, non-competitive with ATP. This results in a reduction in Akt enzymatic and cellular activities. Other small molecule (MK- 2206, 6, PHT-427, Akti-1/2) inhibitors with a similar mechanism of action, alter Akt activity through the suppression of cell growth mediated by the inhibition of Akt membrane localization and subsequent activation. The natural product solenopsin has been identified as an inhibitor of Akt. A few promising solenopsin derivatives have emerged through pharmacophore modeling, energy-based calculations, and property predictions.

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27

Mordka, Cezary. "Świadomy akt spostrzeżenia." Σοφια 18 (2018): 59–73. http://dx.doi.org/10.15584/sofia.2018.18.4.

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28

Luger, Kurt. "Der letzte Akt?" MedienJournal 11, no. 3 (May 7, 2017): 104–10. http://dx.doi.org/10.24989/medienjournal.v11i3.929.

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29

Elfes, Chris. "The AKT Exam." InnovAiT: Education and inspiration for general practice 4, no. 12 (October 23, 2011): 736–37. http://dx.doi.org/10.1093/innovait/inr138.

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30

Mahajan, Kiran N., and Nupam P. Mahajan. "Akt Goes Cycling." Cancer Control 21, no. 3 (July 2014): 239–41. http://dx.doi.org/10.1177/107327481402100310.

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31

Gough, N. R. "Antibiotics Target Akt." Science's STKE 2007, no. 415 (November 27, 2007): tw441. http://dx.doi.org/10.1126/stke.4152007tw441.

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32

Gough, N. R. "Cycling Akt Activity." Science Signaling 7, no. 323 (April 29, 2014): ec116-ec116. http://dx.doi.org/10.1126/scisignal.2005422.

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33

Chenette, Emily J. "Akt Skps through." Nature Reviews Cancer 9, no. 5 (April 3, 2009): 316–17. http://dx.doi.org/10.1038/nrc2649.

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34

Wong, W. "Unexpected Akt-ions." Science Signaling 5, no. 216 (March 20, 2012): ec82-ec82. http://dx.doi.org/10.1126/scisignal.2003052.

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35

Restuccia, D. F., and B. A. Hemmings. "Blocking Akt-ivity." Science 325, no. 5944 (August 27, 2009): 1083–84. http://dx.doi.org/10.1126/science.1179972.

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36

Wei, Yingze, Jianyun Zhou, Haiyan Yu, and Xiaoxia Jin. "AKT phosphorylation sites of Ser473 and Thr308 regulate AKT degradation." Bioscience, Biotechnology, and Biochemistry 83, no. 3 (November 29, 2018): 429–35. http://dx.doi.org/10.1080/09168451.2018.1549974.

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37

Gonzalez, Eva, and Timothy E. McGraw. "Insulin-modulated Akt subcellular localization determines Akt isoform-specific signaling." Proceedings of the National Academy of Sciences 106, no. 17 (April 16, 2009): 7004–9. http://dx.doi.org/10.1073/pnas.0901933106.

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The 3 Akt protein kinase isoforms have critical and distinct functions in the regulation of metabolism, cell growth, and apoptosis, yet the mechanisms by which their signaling specificity is achieved remain largely unclear. Here, we investigated potential mechanisms underlying Akt isoform functional specificity by using Akt2-specific regulation of glucose transport in insulin-stimulated adipocytes as a model system. We found that insulin activates both Akt1 and Akt2 in adipocytes, but differentially regulates the subcellular distribution of these Akt isoforms. The greater accumulation of Akt2 at the plasma membrane (PM) of insulin-stimulated adipocytes correlates with Akt2-specific regulation of the trafficking of the GLUT4 glucose transporter. Consistent with this pattern, Akt constructs that do not accumulate at the PM to the same degree as Akt2 fail to regulate GLUT4 translocation to the PM, whereas enhancement of Akt1 PM association through mutation in Akt1 PH domain is sufficient to overcome Akt-isoform specificity in GLUT4 regulation. Indeed, we found that this distinct insulin-induced PM accumulation of Akt kinases is translated into a differential regulation by the Akt isoforms of AS160, a RabGAP that regulates GLUT4 trafficking. Our data show that Akt2 specifically regulates AS160 phosphorylation and membrane association providing molecular basis for Akt2 specificity in the modulation of GLUT4 trafficking. Together, our findings reveal the stimulus-induced subcellular compartmentalization of Akt kinases as a mechanism contributing to specify Akt isoform functions.

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38

Yudushkin, Ivan. "Getting the Akt Together: Guiding Intracellular Akt Activity by PI3K." Biomolecules 9, no. 2 (February 16, 2019): 67. http://dx.doi.org/10.3390/biom9020067.

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Intracellular signaling pathways mediate the rapid response of cells to environmental cues. To control the fidelity of these responses, cells coordinate the activities of signaling enzymes with the strength, timing, and localization of the upstream stimuli. Protein kinase Akt links the PI3K-coupled receptors to cellular anabolic processes by phosphorylating multiple substrates. How the cells ensure that Akt activity remains proportional to upstream signals and control its substrate specificity is unclear. In this review, I examine how cell-autonomous and intrinsic allosteric mechanisms cooperate to ensure localized, context-specific signaling in the PI3K/Akt axis.

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39

Ding, Jixin, and Keyong Du. "ClipR-59 Interacts with Akt and Regulates Akt Cellular Compartmentalization." Molecular and Cellular Biology 29, no. 6 (January 12, 2009): 1459–71. http://dx.doi.org/10.1128/mcb.00754-08.

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ABSTRACT Akt is activated on the plasma membrane and its substrates are distributed throughout various cellular compartments. To phosphorylate its substrates, Akt needs to be recruited to specific intracellular compartments. Thus, regulation of Akt cellular compartmentalization constitutes an important mechanism to specify Akt signaling. Here, we report the identification of ClipR-59 as an Akt interaction protein. We show that the interaction of ClipR-59 with Akt is mediated by the CAP-Gly domain of ClipR-59 and kinase domain of Akt and is regulated by Akt phosphorylation. We demonstrate that ClipR-59 regulates the Akt membrane association through its interaction with Akt and membrane localization and, by modulating Akt cellular compartmentalization, differentially modulates phosphorylation of Akt substrates in adipocytes. Finally, we provide evidence that one of the Akt substrates whose phosphorylation is upregulated by ClipR-59 is AS160, a negative regulator of adipocyte glucose transport. Accordingly, ectopic expression of ClipR-59 enhances, whereas knockdown of ClipR-59 suppresses, adipocyte glucose transport. We suggest that ClipR-59 functions as a scaffold protein that interacts with phospho-Akt and recruits active Akt on the membrane and may play an important role in adipocyte glucose transport.

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40

Hatta, Rieko, Kaoru Ito, Yoshitsugu Hosaki, Takayoshi Tanaka, Aiko Tanaka, Mikihiro Yamamoto, Kazuya Akimitsu, and Takashi Tsuge. "A Conditionally Dispensable Chromosome Controls Host-Specific Pathogenicity in the Fungal Plant Pathogen Alternaria alternata." Genetics 161, no. 1 (May 1, 2002): 59–70. http://dx.doi.org/10.1093/genetics/161.1.59.

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Abstract The filamentous fungus Alternaria alternata contains seven pathogenic variants (pathotypes), which produce host-specific toxins and cause diseases on different plants. Previously, the gene cluster involved in host-specific AK-toxin biosynthesis of the Japanese pear pathotype was isolated, and four genes, named AKT genes, were identified. The AKT homologs were also found in the strawberry and tangerine pathotypes, which produce AF-toxin and ACT-toxin, respectively. This result is consistent with the fact that the toxins of these pathotypes share a common 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid structural moiety. In this study, three of the AKT homologs (AFT1-1, AFTR-1, and AFT3-1) were isolated on a single cosmid clone from strain NAF8 of the strawberry pathotype. In NAF8, all of the AKT homologs were present in multiple copies on a 1.05-Mb chromosome. Transformation-mediated targeting of AFT1-1 and AFT3-1 in NAF8 produced AF-toxin-minus, nonpathogenic mutants. All of the mutants lacked the 1.05-Mb chromosome encoding the AFT genes. This chromosome was not essential for saprophytic growth of this pathogen. Thus, we propose that a conditionally dispensable chromosome controls host-specific pathogenicity of this pathogen.

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41

Hong, Jung Yong, Moon Ki Choi, Young Saing Kim, Chi Hoon Maeng, Su Jin Lee, Won Jin Chang, Silvia Park, et al. "The Impact of Activated Akt Expression On Clinical Outcome in Diffuse Large B-Cell Lymphoma: A Clinicopathological Study of 99 Cases." Blood 120, no. 21 (November 16, 2012): 2676. http://dx.doi.org/10.1182/blood.v120.21.2676.2676.

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Abstract Abstract 2676 Purpose Akt is a serine/threonine kinase that plays a central role in cell proliferation and growth. To define clinical impact of Akt expression in diffuse large B-cell lymphoma(DLBCL), we investigated the expression of phospho-Akt(p-Akt) in DLBCL and analyzed clinical impact of p-Akt expression on patient survival. Methods We evaluated the p-Akt expression in 99 DLBCL patients using tissue microarray(TMA) technology. Results Positive p-Akt expression was observed in 15.2% of the patients and significantly associated with elevated lactic dehydrogenase level (P = .044). Kaplan-Meier survival analysis showed that the patients with positive p-Akt expression showed substantially poorer overall survival (p-Akt+ vs p-Akt- 25.3 months [95% confidence interval(CI), 14.4–36.2 months] vs 192.6 months [95% CI, 131.3–253.9 months], P < .001) and progression-free survival (p-Akt+ vs p-Akt- 13.6 months[95% CI, 14.4–36.2 months] vs 134.5 months [95% CI, 131.3–253.9 months], P < .001), respectively. Multivariate Cox regression analysis revealed that patients with DLBCL with p-Akt positivity showed poorer overall survival with 3.2 fold (95% CI, 1.6–6.8, P = .002) risk for death compared to patients with DLBCL with p-Akt negativity. Conclusion Positive expression of p-Akt in DLBCL patients is associated with poorer overall and progression-free survival. Expression of p-Akt may act as an independent poor prognostic factor and might be a novel therapeutic target for DLBCL. Disclosures: No relevant conflicts of interest to declare.

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42

Chaurasiya, Surendra, Wanfu Wu, Anders M. Strom, Margaret Warner, and Jan-Åke Gustafsson. "Estrogen receptor β regulates AKT activity through up-regulation of INPP4B and inhibits migration of prostate cancer cell line PC-3." Proceedings of the National Academy of Sciences 117, no. 42 (October 5, 2020): 26347–55. http://dx.doi.org/10.1073/pnas.2007160117.

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Loss of the tumor suppressor, PTEN, is one of the most common findings in prostate cancer (PCa). This loss leads to overactive Akt signaling, which is correlated with increased metastasis and androgen independence. However, another tumor suppressor, inositol-polyphosphate 4-phosphatase type II (INPP4B), can partially compensate for the loss of PTEN. INPP4B is up-regulated by androgens, and this suggests that androgen-deprivation therapy (ADT) would lead to hyperactivity of AKT. However, in the present study, we found that in PCa, samples from men treated with ADT, ERβ, and INPP4B expression were maintained in some samples. To investigate the role of ERβ1 in regulation of INPPB, we engineered the highly metastatic PCa cell line, PC3, to express ERβ1. In these cells, INPP4B was induced by ERβ ligands, and this induction was accompanied by inhibition of Akt activity and reduction in cell migration. These findings reveal that, in the absence of androgens, ERβ1 induces INPP4B to dampen AKT signaling. Since the endogenous ERβ ligand, 3β-Adiol, is lost upon long-term ADT, to obtain the beneficial effects of ERβ1 on AKT signaling, an ERβ agonist should be added along with ADT.

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43

Bao, Fan, Peiqi Hao, Su An, Yang Yang, Ying Liu, Qian Hao, Mubashir Ejaz, Xiao-Xi Guo, and Tian-Rui Xu. "Akt scaffold proteins: the key to controlling specificity of Akt signaling." American Journal of Physiology-Cell Physiology 321, no. 3 (September 1, 2021): C429—C442. http://dx.doi.org/10.1152/ajpcell.00146.2020.

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The phosphatidylinositol 3-kinase-Akt signaling pathway plays an essential role in regulating cell proliferation and apoptosis. Akt kinase is at the center of this signaling pathway and interacts with a variety of proteins. Akt is overexpressed in almost 80% of tumors. However, inhibiting Akt has serious clinical side effects so is not a suitable treatment for cancer. During recent years, Akt scaffold proteins have received increasing attention for their ability to regulate Akt signaling and have emerged as potential targets for cancer therapy. In this paper, we categorize Akt kinase scaffold proteins into four groups based on their cellular location: membrane-bound activator and inhibitor, cytoplasm, and endosome. We describe how these scaffolds interact with Akt kinase, how they affect Akt activity, and how they regulate the specificity of Akt signaling. We also discuss the clinical application of Akt scaffold proteins as targets for cancer therapy.

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44

Houghton, Mike. "AKT Answer Relating to Thyroid Disease: AKT Answer Relating to Osteoporosis." InnovAiT: Education and inspiration for general practice 1, no. 12 (December 2008): 828. http://dx.doi.org/10.1093/innovait/inn180.

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45

Liu, Pengda, Zhiwei Wang, and Wenyi Wei. "Phosphorylation of Akt at the C-terminal tail triggers Akt Activation." Cell Cycle 13, no. 14 (June 16, 2014): 2162–64. http://dx.doi.org/10.4161/cc.29584.

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46

Tan, Shi-Xiong, Yvonne Ng, and David E. James. "Akt inhibitors reduce glucose uptake independently of their effects on Akt." Biochemical Journal 432, no. 1 (October 25, 2010): 191–98. http://dx.doi.org/10.1042/bj20100750.

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The protein kinase Akt is involved in various cellular processes, including cell proliferation, growth and metabolism. Hyperactivation of Akt is commonly observed in human tumours and so this pathway has been the focus of targeted drug discovery. However, Akt also plays an essential role in other physiological processes, such as the insulin-regulated transport of glucose into muscle and fat cells. This process, which is essential for whole-body glucose homoeostasis in mammals, is thought to be mediated via Akt-dependent movement of GLUT4 glucose transporters to the plasma membrane. In the present study, we have investigated the metabolic side effects of non-ATP-competitive allosteric Akt inhibitors. In 3T3-L1 adipocytes, these inhibitors caused a decrease in the Akt signalling pathway concomitant with reduced glucose uptake. Surprisingly, a similar reduction in GLUT4 translocation to the plasma membrane was not observed. Further investigation revealed that the inhibitory effects of these compounds on glucose uptake in 3T3-L1 adipocytes were independent of the Akt signalling pathway. The inhibitors also inhibited glucose transport into other cell types, including human erythrocytes and T-47D breast cancer cells, suggesting that these effects are not specific to GLUT4. We conclude that these drugs may, at least in part, inhibit tumorigenesis through inhibition of tumour cell glucose transport.

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47

Guo, Jianping, Xiangpeng Dai, Benoit Laurent, Nana Zheng, Wenjian Gan, Jian Zhang, Ailan Guo, et al. "AKT methylation by SETDB1 promotes AKT kinase activity and oncogenic functions." Nature Cell Biology 21, no. 2 (January 28, 2019): 226–37. http://dx.doi.org/10.1038/s41556-018-0261-6.

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48

Robey, R. Brooks, and Nissim Hay. "Is Akt the “Warburg kinase”?—Akt-energy metabolism interactions and oncogenesis." Seminars in Cancer Biology 19, no. 1 (February 2009): 25–31. http://dx.doi.org/10.1016/j.semcancer.2008.11.010.

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Bao, Haifeng, Sarah M. Jacobs-Helber, Amy E. Lawson, Kalyani Penta, Amittha Wickrema, and Stephen T. Sawyer. "Protein Kinase B (c-Akt), Phosphatidylinositol 3-Kinase, and STAT5 Are Activated by Erythropoietin (EPO) in HCD57 Erythroid Cells But Are Constitutively Active in an EPO-Independent, Apoptosis-Resistant Subclone (HCD57-SREI Cells)." Blood 93, no. 11 (June 1, 1999): 3757–73. http://dx.doi.org/10.1182/blood.v93.11.3757.

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Abstract:

Abstract We found that erythropoietin (EPO) and stem cell factor (SCF) activated protein kinase B (PKB/Akt) in EPO-dependent HCD57 erythroid cells. To better understand signals controlling proliferation and viability, erythroid cells that resist apoptosis in the absence of EPO were subcloned and characterized (HCD57-SREI cells). Constitutive activations of PKB/Akt, STAT5a, and STAT5b were noted in these EPO-independent cells. PI3-kinase activity was an upstream activator of PKB/Akt because the PI3-kinase inhibitor LY294002 blocked both constitutive PKB/Akt and factor-dependent PKB/Akt activity. The LY294002 study showed that proliferation and viability of both HCD57-SREI and HCD57 cells correlated with the activity of PKB/Akt; however, PKB/Akt activity alone did not protect these cells from apoptosis. Treatment of HCD57 cells with SCF also activated PKB/Akt, but did not protect from apoptosis. This result suggested that PKB/PI3-kinase activity is necessary but not sufficient to promote viability and/or proliferation. Constitutive STAT5 activity, activated through an unknown pathway not including JAK2 or EPOR, may act in concert with the constitutive PI3-kinase/PKB/Akt pathway to protect the EPO-independent HCD57-SREI cells from apoptosis and promote limited proliferation.

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Bao, Haifeng, Sarah M. Jacobs-Helber, Amy E. Lawson, Kalyani Penta, Amittha Wickrema, and Stephen T. Sawyer. "Protein Kinase B (c-Akt), Phosphatidylinositol 3-Kinase, and STAT5 Are Activated by Erythropoietin (EPO) in HCD57 Erythroid Cells But Are Constitutively Active in an EPO-Independent, Apoptosis-Resistant Subclone (HCD57-SREI Cells)." Blood 93, no. 11 (June 1, 1999): 3757–73. http://dx.doi.org/10.1182/blood.v93.11.3757.411a34_3757_3773.

Full text

Abstract:

We found that erythropoietin (EPO) and stem cell factor (SCF) activated protein kinase B (PKB/Akt) in EPO-dependent HCD57 erythroid cells. To better understand signals controlling proliferation and viability, erythroid cells that resist apoptosis in the absence of EPO were subcloned and characterized (HCD57-SREI cells). Constitutive activations of PKB/Akt, STAT5a, and STAT5b were noted in these EPO-independent cells. PI3-kinase activity was an upstream activator of PKB/Akt because the PI3-kinase inhibitor LY294002 blocked both constitutive PKB/Akt and factor-dependent PKB/Akt activity. The LY294002 study showed that proliferation and viability of both HCD57-SREI and HCD57 cells correlated with the activity of PKB/Akt; however, PKB/Akt activity alone did not protect these cells from apoptosis. Treatment of HCD57 cells with SCF also activated PKB/Akt, but did not protect from apoptosis. This result suggested that PKB/PI3-kinase activity is necessary but not sufficient to promote viability and/or proliferation. Constitutive STAT5 activity, activated through an unknown pathway not including JAK2 or EPOR, may act in concert with the constitutive PI3-kinase/PKB/Akt pathway to protect the EPO-independent HCD57-SREI cells from apoptosis and promote limited proliferation.

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