Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
Gautam N Bijur, Richard S Jop. Rapid accumulation of Akt in mitochondria following phosphatidylinositol 3-kinase activation. Journal of neurochemistry. vol 87. issue 6. 2004-01-26. PMID:14713298. |
akt (protein kinase b) was shown for the first time to be localized in mitochondria, where it was found to reside in the matrix and the inner and outer membranes, and the level of mitochondrial akt was very dynamically regulated. |
2004-01-26 |
2023-08-12 |
Not clear |
Abdelkarim Sabri, Sasha G Alcott, Hasnae Elouardighi, Elena Pak, Claudia Derian, Patricia Andrade-Gordon, Kathleen Kinnally, Susan F Steinber. Neutrophil cathepsin G promotes detachment-induced cardiomyocyte apoptosis via a protease-activated receptor-independent mechanism. The Journal of biological chemistry. vol 278. issue 26. 2003-08-20. PMID:12707281. |
of note, prolonged incubation of cardiomyocytes with cathepsin g results in the activation of caspase-3, cleavage of fak and akt, sarcomeric disassembly, cell rounding, cell detachment from underlying matrix, and morphologic features of apoptosis. |
2003-08-20 |
2023-08-12 |
mouse |
Paola Borgatti, Alberto M Martelli, Giovanna Tabellini, Alfonso Bellacosa, Silvano Capitani, Luca M Ner. Threonine 308 phosphorylated form of Akt translocates to the nucleus of PC12 cells under nerve growth factor stimulation and associates with the nuclear matrix protein nucleolin. Journal of cellular physiology. vol 196. issue 1. 2003-07-16. PMID:12767043. |
threonine 308 phosphorylated form of akt translocates to the nucleus of pc12 cells under nerve growth factor stimulation and associates with the nuclear matrix protein nucleolin. |
2003-07-16 |
2023-08-12 |
Not clear |
Paola Borgatti, Alberto M Martelli, Giovanna Tabellini, Alfonso Bellacosa, Silvano Capitani, Luca M Ner. Threonine 308 phosphorylated form of Akt translocates to the nucleus of PC12 cells under nerve growth factor stimulation and associates with the nuclear matrix protein nucleolin. Journal of cellular physiology. vol 196. issue 1. 2003-07-16. PMID:12767043. |
both total and active akt associated with the nuclear matrix and, in particular, with the protein nucleolin, with which akt co-immunoprecipitated. |
2003-07-16 |
2023-08-12 |
Not clear |
Hidemi Teramoto, Renae L Malek, Babak Behbahani, Maria Domenica Castellone, Norman H Lee, J Silvio Gutkin. Identification of H-Ras, RhoA, Rac1 and Cdc42 responsive genes. Oncogene. vol 22. issue 17. 2003-05-28. PMID:12730683. |
for example, h-ras v12 upregulated osteopontin and akt 1, and h-ras and rhoa stimulated cyclin g1, cyclin-dependent kinase 8, cyclin a2 and hmgi-c, while rac1 ql and cdc42 ql upregulated extracellular matrix and cell adhesion proteins such as alpha-actinin 4, procollagen type i and v and neuropilin. |
2003-05-28 |
2023-08-12 |
Not clear |
Hiroki Kuniyasu, Yoshitomo Chihara, Hideaki Kond. Differential effects between amphoterin and advanced glycation end products on colon cancer cells. International journal of cancer. vol 104. issue 6. 2003-05-12. PMID:12640679. |
phosphorylation of extracellular signal-regulated kinase-1/2, rac1 and akt and production of matrix metalloproteinase 9 were increased to a greater degree by amphoterin than by age-bsa. |
2003-05-12 |
2023-08-12 |
Not clear |
Maria Sternberger, Anett Schmiedeknecht, Anny Kretschmer, Frank Gebhardt, Frauke Leenders, Frank Czauderna, Ira Von Carlowitz, Mike Engle, Klaus Giese, Leonid Beigelman, Anke Klippe. GeneBlocs are powerful tools to study and delineate signal transduction processes that regulate cell growth and transformation. Antisense & nucleic acid drug development. vol 12. issue 3. 2003-01-22. PMID:12162696. |
specifically, cells treated with pten geneblocs show functional activation of akt, a downstream effector of pi 3-kinase signaling, and exhibit enhanced proliferation when seeded on a basement membrane matrix. |
2003-01-22 |
2023-08-12 |
Not clear |
Hui Zhang, Xiangming Zha, Yi Tan, Peter V Hornbeck, Allison J Mastrangelo, Dario R Alessi, Roberto D Polakiewicz, Michael J Com. Phosphoprotein analysis using antibodies broadly reactive against phosphorylated motifs. The Journal of biological chemistry. vol 277. issue 42. 2002-12-19. PMID:12151408. |
to identify phosphoproteins detected using the akt substrate antibody, we characterized the antibody binding specificity to generate a specificity matrix useful in predicting antibody reactivity. |
2002-12-19 |
2023-08-12 |
Not clear |
J Kijowski, M Baj-Krzyworzeka, M Majka, R Reca, L A Marquez, M Christofidou-Solomidou, A Janowska-Wieczorek, M Z Ratajcza. The SDF-1-CXCR4 axis stimulates VEGF secretion and activates integrins but does not affect proliferation and survival in lymphohematopoietic cells. Stem cells (Dayton, Ohio). vol 19. issue 5. 2001-12-07. PMID:11553854. |
we evaluated the phosphorylation of mapk p42/44, akt, and stat proteins and examined the ability of the ligands for these receptors (stromal-derived factor-1 [sdf-1] and macrophage inflammatory protein-1beta [mip-1beta]) to influence cell growth, apoptosis, adhesion, and production of vascular endothelial growth factors (vegf), matrix metalloproteinases (mmps) and their tissue inhibitors (timps) in these cell lines. |
2001-12-07 |
2023-08-12 |
human |
J T Yu, R G Foster, D C Dea. Transcriptional repression by RB-E2F and regulation of anchorage-independent survival. Molecular and cellular biology. vol 21. issue 10. 2001-06-07. PMID:11313458. |
adhesion of integrin receptors to extracellular matrix activates a survival signaling pathway in epithelial cells where akt phosphorylates and blocks the activity of proapoptotic proteins such as the bcl2 family member bad, the forkhead transcription factor fkhrl-1, and caspase 9. |
2001-06-07 |
2023-08-12 |
Not clear |
J T Yu, R G Foster, D C Dea. Transcriptional repression by RB-E2F and regulation of anchorage-independent survival. Molecular and cellular biology. vol 21. issue 10. 2001-06-07. PMID:11313458. |
insulin-like growth factor 1 (igf-1) is a well-established epithelial cell survival factor that also triggers activation of akt and can maintain akt activity after cells lose matrix contact. |
2001-06-07 |
2023-08-12 |
Not clear |
J T Yu, R G Foster, D C Dea. Transcriptional repression by RB-E2F and regulation of anchorage-independent survival. Molecular and cellular biology. vol 21. issue 10. 2001-06-07. PMID:11313458. |
while igf-1 is able to maintain akt activity and phosphorylation of proapoptotic proteins in cells that have lost matrix contact, akt is not able to phosphorylate and inactivate another of its substrates, glycogen synthase kinase 3beta (gsk-3beta), under these conditions. |
2001-06-07 |
2023-08-12 |
Not clear |
J T Yu, R G Foster, D C Dea. Transcriptional repression by RB-E2F and regulation of anchorage-independent survival. Molecular and cellular biology. vol 21. issue 10. 2001-06-07. PMID:11313458. |
the reason for this appears to be a rapid translocation of active akt away from gsk-3beta when cells lose matrix contact. |
2001-06-07 |
2023-08-12 |
Not clear |
J T Yu, R G Foster, D C Dea. Transcriptional repression by RB-E2F and regulation of anchorage-independent survival. Molecular and cellular biology. vol 21. issue 10. 2001-06-07. PMID:11313458. |
this feedback loop containing gsk-3beta, cyclin d, hdac-rb-e2f, and igf-1 then determines how long akt will remain active after cells lose matrix contact, and thus it serves to regulate the onset of apoptosis in such cells. |
2001-06-07 |
2023-08-12 |
Not clear |
A M Mirza, A D Kohn, R A Roth, M McMaho. Oncogenic transformation of cells by a conditionally active form of the protein kinase Akt/PKB. Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research. vol 11. issue 6. 2000-11-02. PMID:10910095. |
consistent with these observations, activation of m+ akt:er* suppressed the apoptosis of rat1 cells that occurs after the detachment of these cells from extracellular matrix. |
2000-11-02 |
2023-08-12 |
Not clear |
K Fujikawa, I de Aos Scherpenseel, S K Jain, E Presman, R A Christensen, L Varticovsk. Role of PI 3-kinase in angiopoietin-1-mediated migration and attachment-dependent survival of endothelial cells. Experimental cell research. vol 253. issue 2. 2000-01-11. PMID:10585289. |
here we show that pi 3-kinase-dependent activation of akt and attachment to extracellular matrix are required for angiopoietin-1-mediated endothelial cell survival. |
2000-01-11 |
2023-08-12 |
Not clear |
M Tamura, J Gu, E H Danen, T Takino, S Miyamoto, K M Yamad. PTEN interactions with focal adhesion kinase and suppression of the extracellular matrix-dependent phosphatidylinositol 3-kinase/Akt cell survival pathway. The Journal of biological chemistry. vol 274. issue 29. 1999-08-19. PMID:10400703. |
in pten-mutated cancer cells, fak phosphorylation was retained even in suspension after detachment from extracellular matrix, accompanied by enhanced pi 3-k association with fak and sustained pi 3-k activity, pip3 levels, and akt phosphorylation; expression of exogenous pten suppressed all five properties. |
1999-08-19 |
2023-08-12 |
Not clear |