Phosphatidylinositol 3-kinases in tumor progression.
作者： Dirk Roymans , Herman Slegers
DOI: 10.1046/J.1432-1327.2001.01936.X
关键词: Cell biology 、 Tumor progression 、 Cell cycle 、 Phosphatidylinositol 3-Kinases 、 Metastasis 、 Biology 、 Oncogene 、 Angiogenesis 、 Cancer research 、 Motility 、 Phosphatidylinositol
摘要: Many cellular processes have been identified in which phosphatidylinositol 3-kinase has a key regulatory function. As an oncogene, it is also involved the development of cancer. The transformation and progression of normal cells towards advanced stage tumor and/or metastatic lesions involves complex series events, including genetic alterations, leading to aberrant cell cycle progression, altered adhesion motility characteristics, inhibition apoptosis induction angiogenesis. This review highlights pathogenesis cancer provides overview possible mechanisms by enzyme exerts its oncogenic action.
sci-hub.se 参考文章(130)
Robin C. Muise-Helmericks, H. Leighton Grimes, Alfonso Bellacosa, Scott E. Malstrom, Philip N. Tsichlis, Neal Rosen, Cyclin D Expression Is Controlled Post-transcriptionally via a Phosphatidylinositol 3-Kinase/Akt-dependent Pathway * Journal of Biological Chemistry. ,vol. 273, pp. 29864- 29872 ,(1998) , 10.1074/JBC.273.45.29864
Catherine D Nobes, Alan Hall, Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia Cell. ,vol. 81, pp. 53- 62 ,(1995) , 10.1016/0092-8674(95)90370-4
Johan Deprez, Didier Vertommen, Dario R. Alessi, Louis Hue, Mark H. Rider, Phosphorylation and activation of heart 6-phosphofructo-2-kinase by protein kinase B and other protein kinases of the insulin signaling cascades Journal of Biological Chemistry. ,vol. 272, pp. 17269- 17275 ,(1997) , 10.1074/JBC.272.28.17269
Daphne Haas-Kogan, Noga Shalev, Michelle Wong, Gordon Mills, Garret Yount, David Stokoe, None, Protein kinase B (PKB/Akt) activity is elevated in glioblastoma cells due to mutation of the tumor suppressor PTEN/MMAC Current Biology. ,vol. 8, pp. 1195- 1198 ,(1998) , 10.1016/S0960-9822(07)00493-9
Luis del Peso, Maribel González-Garcıa, Carmen Page, Román Herrera, Gabriel Nunez, Interleukin-3-Induced Phosphorylation of BAD Through the Protein Kinase Akt Science. ,vol. 278, pp. 687- 689 ,(1997) , 10.1126/SCIENCE.278.5338.687
M. Amano, K. Chihara, Y. Fukata, M. Nakafuku, B. Yamamori, J. Feng, T. Nakano, K. Okawa, A. Iwamatsu, K. Kaibuchi, K. Kimura, M. Ito, Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase) Science. ,vol. 273, pp. 245- 248 ,(1996) , 10.1126/SCIENCE.273.5272.245
Karen L. Philpott, Mary Jane McCarthy, Anke Klippel, Lee L. Rubin, Activated Phosphatidylinositol 3-Kinase and Akt Kinase Promote Survival of Superior Cervical Neurons Journal of Cell Biology. ,vol. 139, pp. 809- 815 ,(1997) , 10.1083/JCB.139.3.809
Meenakshi Chellaiah, Catherine Fitzgerald, Ulises Alvarez, Keith Hruska, c-Src Is Required for Stimulation of Gelsolin-associated Phosphatidylinositol 3-Kinase Journal of Biological Chemistry. ,vol. 273, pp. 11908- 11916 ,(1998) , 10.1074/JBC.273.19.11908
Yoji Shimizu, Stephen W. Hont, Regulating integrin-mediated adhesion: one more function for PI 3-kinase? Immunology Today. ,vol. 17, pp. 565- 573 ,(1996) , 10.1016/S0167-5699(96)10061-X
R. N. Mascardo, P. Sherline, Insulin and Multiplication-stimulating Activity Induce a Very Rapid Centrosomal Orientation Response to Wounding in Endothelial Cell Monolayers Diabetes. ,vol. 33, pp. 1099- 1105 ,(1984) , 10.2337/DIAB.33.11.1099