Добірка наукової літератури з теми "P13K signalling"
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Статті в журналах з теми "P13K signalling"
Mei, Qiyuan, Xiaohu Chen, and Wei Liu. "Protocatechuic Acid Induces Apoptosis in Human Osteosarcoma Cells by Regulating P13K/AKT/ROS Pathway." Sains Malaysiana 51, no. 4 (April 30, 2022): 1167–79. http://dx.doi.org/10.17576/jsm-2022-5104-18.
Повний текст джерелаGoruppi, S., E. Ruaro, B. Varnum, and C. Schneider. "Requirement of phosphatidylinositol 3-kinase-dependent pathway and Src for Gas6-Axl mitogenic and survival activities in NIH 3T3 fibroblasts." Molecular and Cellular Biology 17, no. 8 (August 1997): 4442–53. http://dx.doi.org/10.1128/mcb.17.8.4442.
Повний текст джерелаQattan, Malak Yahia, Mohammad Idreesh Khan, Shudayyed Hasham Alharbi, Amit Kumar Verma, Fatimah A. Al-Saeed, Alduwish Manal Abduallah, and Azza A. Al Al Areefy. "Therapeutic Importance of Kaempferol in the Treatment of Cancer through the Modulation of Cell Signalling Pathways." Molecules 27, no. 24 (December 13, 2022): 8864. http://dx.doi.org/10.3390/molecules27248864.
Повний текст джерелаGao, Hui, Hui Wang, and Jianjun Peng. "Hispidulin Induces Apoptosis Through Mitochondrial Dysfunction and Inhibition of P13k/Akt Signalling Pathway in HepG2 Cancer Cells." Cell Biochemistry and Biophysics 69, no. 1 (September 26, 2013): 27–34. http://dx.doi.org/10.1007/s12013-013-9762-x.
Повний текст джерелаGauglitz, G. G., S. C. Halder, G. Kulp, F. N. Williams, D. N. Herndon, and M. G. Jeschke. "91. Postburn Hepatic Insulin Resistance is Due to Altered JNK/IRS-1 Activation Leading to Impaired P13K/AKT Signalling." Journal of Surgical Research 151, no. 2 (February 2009): 212. http://dx.doi.org/10.1016/j.jss.2008.11.098.
Повний текст джерелаBurgos, Sergio A., Stephanie Chevalier, Jose A. Morais, Marie Lamarche, and Errol B. Marliss. "Insulin Stimulates Grb10 Phosphorylation by mTORC1 and Mediates its Feedback Inhibition on P13K/Akt Signalling in Human Skeletal Muscle." Canadian Journal of Diabetes 37 (October 2013): S62—S63. http://dx.doi.org/10.1016/j.jcjd.2013.08.189.
Повний текст джерелаWerzowa, J., B. Pratscher, D. Cejka, H. Pehamberger, and V. Wacheck. "583 POSTER mTORC1 inhibition with rapamycin leads to activation of P13K/AKT signalling via an mTORC2 dependent mechanism in melanoma cells." European Journal of Cancer Supplements 4, no. 12 (November 2006): 176–77. http://dx.doi.org/10.1016/s1359-6349(06)70588-2.
Повний текст джерелаElekofehinti, Olusola Olalekan, Victor Oluwatoyin Oyedokun, Opeyemi Iwaloye, Akeem Olalekan Lawal, and Oluwamodupe Cecilia Ejelonu. "Momordica charantia silver nanoparticles modulate SOCS/JAK/STAT and P13K/Akt/PTEN signalling pathways in the kidney of streptozotocin-induced diabetic rats." Journal of Diabetes & Metabolic Disorders 20, no. 1 (February 5, 2021): 245–60. http://dx.doi.org/10.1007/s40200-021-00739-w.
Повний текст джерелаRodgers, J., C. Murray, and N. Leaves. "Comparison of three methods to detect mutations in the PI3K oncogene in FFPE cancer samples." Journal of Clinical Oncology 27, no. 15_suppl (May 20, 2009): e22212-e22212. http://dx.doi.org/10.1200/jco.2009.27.15_suppl.e22212.
Повний текст джерелаTAKEUCHI, Hiroshi, Masahiro OIKE, Hugh F. PATERSON, Victoria ALLEN, Takashi KANEMATSU, Yushi ITO, Christophe ERNEUX, Matilda KATAN, and Masato HIRATA. "Inhibition of Ca2+ signalling by p130, a phospholipase-C-related catalytically inactive protein: critical role of the p130 pleckstrin homology domain." Biochemical Journal 349, no. 1 (June 26, 2000): 357–68. http://dx.doi.org/10.1042/bj3490357.
Повний текст джерелаДисертації з теми "P13K signalling"
Street-Docherty, Louise Michelle. "Identification of a Gab1-Tribbles 2 interaction and its role in P13K/Akt signalling and cellular morphology." Thesis, University of Sheffield, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.578713.
Повний текст джерелаLong, Quan. "Phosphory regulation of SGK isoforms downstream of the P13K signalling pathway and the SGK isoform-specific upstream regulation of transcription factors NFκB". Thesis, University of Newcastle upon Tyne, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.519636.
Повний текст джерелаOjaniemi, M. (Marja). "Docking proteins p130Cas and p120Cbl in integrin and growth factor receptor signalling." Doctoral thesis, University of Oulu, 1999. http://urn.fi/urn:isbn:9514253078.
Повний текст джерелаSishi, Balindiwe J. N. "An investigation into the P13-K/AKT signalling pathway in TNF-a-induced muscle proeolysis in L6 myotubes." Thesis, Stellenbosch : Stellenbosch University, 2008. http://hdl.handle.net/10019.1/3039.
Повний текст джерелаIntroduction: Skeletal muscle atrophy is a mitigating complication that is characterized by a reduction in muscle fibre cross-sectional area as well as protein content, reduced force, elevated fatigability and insulin resistance. It seems to be a highly ordered and regulated process and signs of this condition are often seen in inflammatory conditions such as cancer, AIDS, diabetes and chronic heart failure (CHF). It has long been understood that an imbalance between protein degradation (increase) and protein synthesis (decrease) both contribute to the overall loss of muscle protein. Although the triggers that cause atrophy are different, the loss of muscle mass in each case involves a common phenomenon that induces muscle proteolysis. It is becoming evident that interactions among known proteolytic systems (ubiquitin-proteosome) are actively involved in muscle proteolysis during atrophy. Factors such as TNF-α and ROS are elevated in a wide variety of chronic inflammatory diseases in which skeletal muscle proteolysis presents a lethal threat. There is an increasing body of evidence that implies TNF-α may play a critical role in skeletal muscle atrophy in a number of clinical settings but the mechanisms mediating its effects are not completely understood. It is also now apparent that the transcription factor NF-κB is a key intracellular signal transducer in muscle catabolic conditions. This study investigated the various proposed signalling pathways that are modulated by increasing levels of TNF-α in a skeletal muscle cell line, in order to synthesize our current understanding of the molecular regulation of muscle atrophy. Materials and Methods: L6 (rat skeletal muscle) cells were cultured under standard conditions where after reaching ± 60-65% confluency levels, differentiation was induced for a maximum of 8 days. During the last 2 days, myotubes were incubated with increasing concentrations of recombinant TNF-α (1, 3, 6 and 10 ng/ml) for a period of 40 minutes, 24 and 48 hours. The effects of TNF-α on proliferation and cell viability were measured by MTT assay and Trypan Blue exclusion technique. Morphological assessment of cell death was conducted using the Hoechst 33342 and Propidium Iodide staining method. Detection of apoptosis was assessed by DNA isolation and fragmentation assay. The HE stain was used for the measurement of cell size. In order to determine the source and amount of ROS production, MitoTracker Red CM-H2 X ROS was utilised. Ubiquitin expression was assessed by immunohistochemistry. PI3-K activity was calculated by using an ELISA assay and the expression of signalling proteins was analysed by Western Blotting using phospho-specific and total antibodies. Additionally, the antioxidant Oxiprovin was used to investigate the quantity of ROS production in TNF-α-induced muscle atrophy. Results and Discussion: Incubation of L6 myotubes with increasing concentrations of recombinant TNF-α revealed that the lower concentrations of TNF-α used were not toxic to the cells but data analysis of cell death showed that 10 ng/ml TNF-α induced apoptosis and necrosis. Long-term treatment with TNF-α resulted in an increase in the upregulation of TNF- α receptors, specifically TNF-R1. The transcription factors NF-κB and FKHR were rapidly activated thus resulting in the induction of the ubiquitin-proteosome pathway. Activation of this pathway produced significant increases in the expression of E3 ubiquitin ligases MuRF-1 and MAFbx. Muscle fibre diameter appeared to have decreased with increasing TNF-α concentrations in part due to the suppressed activity of the PI3-K/Akt pathway as well as significant reductions in differentiation markers. Western blot analysis also showed that certain MAPKs are activated in response to TNF-α. No profound changes were observed with ROS production. Finally, the use Oxiprovin significantly lowered cell viability and ROS production. These findings suggest that TNF-α may elicit strong catabolic effects on L6 myotubes in a dose and time dependent manner. Conclusion: These observations suggest that TNF-α might have beneficial effects in skeletal muscle in certain circumstances. This beneficial effect however is limited by several aspects which include the concentration of TNF-α, cell type, time of exposure, culture conditions, state of the cell (disturbed or normal) and the cells stage of differentiation. The effect of TNF-α can be positive or negative depending on the concentration and time points analysed. This action is mediated by various signal transduction pathways that are thought to cooperate with each other. More understanding of these pathways as well as their subsequent upstream and downstream constituents is obligatory to clarify the central mechanism/s that control physiological and pathophysiological effects of TNF-α in skeletal muscle.
Christian, Sherri Lynn. "B cell antigen receptor signalling : regulation and targets of the P13K/AKT pathway." Thesis, 2004. http://hdl.handle.net/2429/16872.
Повний текст джерелаScience, Faculty of
Microbiology and Immunology, Department of
Graduate
Turvey, Michelle Elizabeth. "The role and regulation of the p84 adaptor subunit in phosphatidylinositol 3-kinase γ lipid-kinase signalling and the control of PI3Kγ-dependent cell migration". Thesis, 2015. http://hdl.handle.net/2440/111403.
Повний текст джерелаThesis (Ph.D.) -- University of Adelaide, School of Biological Sciences, 2015.
Chi, Mengna. "Inositol polyphosphate 4-phosphatase II (INPP4B) promotes P13K signalling and functions as an oncogenic regulator in human colon cancer and melanoma." Thesis, 2015. http://hdl.handle.net/1959.13/1059871.
Повний текст джерелаAberrant activation of survival-signaling pathways causes uncontrolled cell proliferation and resistance to apoptosis, and plays an important role in cancer development, progression, and resistance to treatment (Courtney et al., 2010; Ferte et al., 2010). In colorectal cancer (CRC), activation of the phosphatidylinositol 3-kinase (PI3K) pathway is of particular importance, in that many common genetic and epigenetic anomalies in the disease, such as amplification of epidermal growth factor (EGF) receptor, activating mutations in KRAS, and loss of phosphate and tensin homolog deleted on chromosome 10 (PTEN), converge on activation of PI3K signalling (Colakoglu et al., 2008). Moreover, activating mutations of PIK3CA, the gene encoding the catalytic subunit of PI3K, is found in up to 40% of colon cancers (Colakoglu et al., 2008; De Roock et al., 2011). In melanoma, identification of activating mutations in BRAF as the major cause of constitutive activation of the mitogen activated protein kinase (MAPK) pathway has led to successful development of mutant BRAF-specific inhibitors in the treatment of the disease (Chapman et al., 2011; Davies et al., 2002; Houslay, 2011; Ribas and Flaherty, 2011). However, primary and acquired resistance, which is commonly associated with activation of other survival pathways, in particular, the phosphatidylinositol 3-kinase (PI3K) signaling pathway, remains a major obstacle in the quest for curative treatment (Jiang et al., 2011; Karreth et al., 2011; Paraiso et al., 2011; Poulikakos and Rosen, 2011). Indeed, activation of PI3K signaling has been shown to cooperate with mutant BRAF in melanomagenesis using in vivo models (Cheung et al., 2008; Dankort et al., 2009). Activation of PI3K signaling is negatively regulated by three classes of inositol polyphosphate phosphatases (Fedele et al., 2010; Gewinner et al., 2009; Kisseleva et al., 2002). The inositol polyphosphate 3-phosphatase (3-phosphatase) PTEN dephosphorylates the 3-position of PI(3,4,5)P₃ to generate PI(4,5)P₂ (Carracedo et al., 2011; Ma et al., 2008), whereas 5-phosphatases, such as Src homology 2-containing inositol 5- phosphatase (SHIP) and phosphatidylinositol 4,5-Bisphosphate 5- Phosphatase (PIB5PA)/proline-rich inositol polyphosphate phosphatase (PIPP) dephosphorylate the 5-position to produce PI(3,4)P₂ (Ooms et al., 2006; Ye et al., 2013a). PI(3,4)P₂ is in turn subjected to dephosphorylation by inositol polyphosphate 4-phosphatase type I (INPP4A) and type II (INPP4B) at the 4-position to generate PI(3)P, thus terminating PI3K signaling (Fedele et al., 2010; Gewinner et al., 2009; Hodgson et al., 2011). Interestingly, despite INPP4B tumor suppressive role in some other tissues, in this study we found that inositol polyphosphate 4-phosphatase type II (INPP4B) functions as an oncogenic regulator in human colon cancer and melanoma. While INPP4B is upregulated in two cancers and its high expression is associated with poor patient survival, INPP4B knockdown blocks activation of PI3K downstream signaling, inhibits proliferation, undermines survival of colon cancer and melanoma cells, and retards cancer growth in a xenograft model. Conversely, overexpression of INPP4B causes increased proliferation and anchorage-independent growth in normal colon epithelial cells and melanocytes. However, INPP4B regulates PI3K signalling pathway in two cancers by different mechanisms. It plays an important role for maintaining cellular PI(3,4,5)P₃ and PI(3,4)P₂ levels in colon cancer whereas PI(3)P levels in melanoma cells. Also, the increase in INPP4B is primarily due to Ets-1-mediated transcriptional upregulation in colon cancer cells, whereas a posttranscriptional increase via reduction of miRNA-494 and miRNA-599 in melanoma.