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Angaben zur Quelle [Bearbeiten]

Autor     Thomas F. Franke, Christoph P. Hornik, Lisa Segev, Grigoriy A. Shostak und Chizuru Sugimoto
Titel    PI3K/Akt and apoptosis: size matters
Zeitschrift    Oncogene
Verlag    Nature Publishing Group
Ausgabe    22
Jahr    2003
Seiten    8983-8998
Anmerkung    PubMed ID: 14663477
DOI    10.1038/sj.onc.1207115
URL    http://www.nature.com/onc/journal/v22/n56/pdf/1207115a.pdf

Literaturverz.   

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Fußnoten    nein
Fragmente    2


Fragmente der Quelle:
[1.] Shg/Fragment 026 20 - Diskussion
Zuletzt bearbeitet: 2014-11-01 21:23:33 Singulus
Fragment, Franke et al 2003, Gesichtet, KomplettPlagiat, SMWFragment, Schutzlevel sysop, Shg

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KomplettPlagiat
Bearbeiter
Graf Isolan
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Untersuchte Arbeit:
Seite: 26, Zeilen: 20-31
Quelle: Franke et al 2003
Seite(n): 8989, Zeilen: li.Sp. 40-57
1.3.3. Apoptosis responses by AKT pathway

Akt is a good candidate for mediating PI3K-dependent cell-survival responses. An important function of activated PI3K in cells is the inhibition of programmed cell death [Yao and Cooper, 1995]. The first evidence to show that Akt acts as an anti-apoptotic signaling molecule was observed in cerebellar granule neurons after trophic factor withdrawal [Dudek et al., 1997], and in fibroblasts after forced expression of c-Myc [Kauffmann-Zeh et al., 1997]. Subsequent work in many laboratories has established the principle role of Akt in the regulation of cell survival in several cell types, consistent with its ubiquitous expression pattern. Akt has been implicated as an anti-apoptotic in many different cell death paradigms, including withdrawal of extracellular signaling factors, oxidative and osmotic stress, irradiation and treatment of cells with chemotherapeutic drugs and ischemic shock [Franke et al., 1997; Downward, 1998].


Downward J. (1998) Mechanisms and consequences of activation of protein kinase B/Akt. Curr Opin Cell Biol. 10:262-267.

Dudek H, Datta SR, Franke TF, Birnbaum MJ, Yao R, Cooper GM, Segal RA, Kaplan DR and Greenberg ME. (1997). Regulation of neuronal survival by the serine-threonine protein kinase Akt. Science, 275, 661–665.

Franke TF, Kaplan DR and Cantley LC. (1997). PI3K: downstream AKTion blocks apoptosis. Cell, 88, 435–437.

Kauffmann-Zeh A, Rodriguez-Viciana P, Ulrich E, Gilbert C, Coffer P, Downward J and Evan G. (1997). Suppression of c-Myc-induced apoptosis by Ras signalling through PI(3)K and PKB.(1997). Nature, 385, 544–548.

Yao R and Cooper GM. (1995) Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor.Science, 267, 2003–2006.

Apoptosis suppression by Akt

An important function of activated PI3K in cells is the inhibition of programmed cell death (Yao and Cooper, 1995), and Akt is a good candidate for mediating these PI3K-dependent cell-survival responses. The initial evidence to show that Akt acts as an anti-apoptotic signaling molecule was observed in cerebellar granule neurons after trophic factor withdrawal (Dudek et al., 1997), and in fibroblasts after forced expression of c-Myc (Kauffmann-Zeh et al., 1997). Subsequent work in many laboratories has established the principle role of Akt in the regulation of cell survival in several cell types, consistent with its ubiquitous expression pattern. Akt has been implicated as an anti-apoptotic in many different cell death paradigms, including withdrawal of extracellular signaling factors, oxidative and osmotic stress, irradiation and treatment of cells with chemotherapeutic drugs and ischemic shock (Franke et al., 1997a; Downward, 1998).


Downward J. (1998). Curr. Opin. Cell Biol., 10, 262–267.

Dudek H, Datta SR, Franke TF, Birnbaum MJ, Yao R, Cooper GM, Segal RA, Kaplan DR and Greenberg ME. (1997). Science, 275, 661–665.

Franke TF, Kaplan DR and Cantley LC. (1997a). Cell, 88, 435–437.

Kauffmann-Zeh A, Rodriguez-Viciana P, Ulrich E, Gilbert C, Coffer P, Downward J and Evan G. (1997). Nature, 385, 544–548.

Yao R and Cooper GM. (1995). Science, 267, 2003–2006.

Anmerkungen

Ohne Hinweis auf eine Übernahme.

Sichter
(Graf Isolan), SleepyHollow02

[2.] Shg/Fragment 027 01 - Diskussion
Zuletzt bearbeitet: 2014-11-01 21:27:21 Singulus
Fragment, Franke et al 2003, Gesichtet, KomplettPlagiat, SMWFragment, Schutzlevel sysop, Shg

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Untersuchte Arbeit:
Seite: 27, Zeilen: 1-23
Quelle: Franke et al 2003
Seite(n): 8989, Zeilen: li.Sp. 57-58 - re.Sp. 1ff.
[Multiple studies supporting the role of Akt in apoptosis suppression have] connected Akt to cell death regulation either by demonstrating its downregulation following pro-apoptotic insults, or by using gene-transfer experiments that transduce both activated, anti-apoptotic and inactive, pro-apoptotic mutants of Akt.

Taken together, these observations suggest that Akt may play a critical role both in the function of cancer cells and in the pathogenesis of degenerative diseases. By promoting the cell survival of mutated, damaged or transformed cells even under adverse conditions, Akt can promote cancer cell growth by protecting cells from apoptosis, which would otherwise be eliminated by programmed cell death. To experimentally prove the importance of Akt kinases in oncogenic transformation, in a seminal paper, Peter Vogt and colleagues demonstrated that a transformed cellular phenotype could be reverted to normal when using a cell model for PI3K-dependent oncogenesis as long as dominant-negative mutants of Akt were expressed concomitantly [Aoki et al., 1998]. Akt is also likely to play a significant role in degenerative diseases, where excessive or inappropriate cell death occurs possibly because proper trophic factor support is lacking. The relevance of Akt signaling in neurodegenerative disease is supported by studies that examine its activity and function in Alzheimer's disease models in vitro [Hong and Lee, 1997; Weihl et al., 1999]. A role for Akt has also been suggested in other models of human degenerative diseases, including cardiac failure [Matsui et al., 1999] and other cardiovascular diseases where there is increased and chronic loss of cells [Reed and Paternostro, 1999].


Aoki M, Batista O, Bellacosa A, Tsichlis P and Vogt PK. The akt kinase: molecular determinants of oncogenicity. (1998). Proc. Natl. Acad. Sci. USA, 95, 14950–14955.

Hong M and Lee VM. (1997). Insulin and insulin-like growth factor-1 regulate tau phosphorylation in cultured human neuronsJ. Biol. Chem. 272, 19547–19553.

Matsui T, Li L, del Monte F, Fukui Y, Franke TF, Hajjar RJ and Rosenzweig A. (1999). Adenoviral gene transfer of activated phosphatidylinositol 3'-kinase and Akt inhibits apoptosis of hypoxic cardiomyocytes in vitro. Circulation, 100, 2373–2379.

Reed JC and Paternostro G. (1999). Postmitochondrial regulation of apoptosis during heart failure. (Proc. Natl. Acad. Sci. USA, 96, 7614–7616.

Weihl CC, Ghadge GD, Kennedy SG, Hay N, Miller RJ and Roos RP. (1999). Mutant presenilin-1 induces apoptosis and downregulates Akt/PKB. J. Neurosci., 19, 5360–5369.

Multiple studies supporting the role of Akt in apoptosis suppression have connected Akt to cell death regulation either by demonstrating its downregulation following pro-apoptotic insults, or by using gene-transfer experiments that transduce both activated, anti-apoptotic and inactive, pro-apoptotic mutants of Akt.

Taken together, these observations suggest that Akt may play a critical role both in the function of cancer cells and in the pathogenesis of degenerative diseases. By promoting the cell survival of mutated, damaged or transformed cells even under adverse conditions, Akt can promote cancer cell growth by protecting cells from apoptosis, which would otherwise be eliminated by programmed cell death. To experimentally prove the importance of Akt kinases in oncogenic transformation, in a seminal paper, Peter Vogt and colleagues demonstrated that a transformed cellular phenotype could be reverted to normal when using a cell model for PI3K-dependent oncogenesis as long as dominant-negative mutants of Akt were expressed concomitantly (Aoki et al., 1998). Akt is also likely to play a significant role in degenerative diseases, where excessive or inappropriate cell death occurs possibly because proper trophic factor support is lacking. The relevance of Akt signaling in neurodegenerative disease is supported by studies that examine its activity and function in Alzheimer’s disease models in vitro (Hong and Lee, 1997; Weihl et al., 1999). A role for Akt has also been suggested in other models of human degenerative diseases, including cardiac failure (Matsui et al., 1999) and other cardiovascular diseases where there is increased and chronic loss of cells (Reed and Paternostro, 1999).


Aoki M, Batista O, Bellacosa A, Tsichlis P and Vogt PK. (1998). Proc. Natl. Acad. Sci. USA, 95, 14950–14955.

Hong M and Lee VM. (1997). J. Biol. Chem., 272, 19547–19553.

Matsui T, Li L, del Monte F, Fukui Y, Franke TF, Hajjar RJ and Rosenzweig A. (1999). Circulation, 100, 2373–2379.

Reed JC and Paternostro G. (1999). Proc. Natl. Acad. Sci. USA, 96, 7614–7616.

Weihl CC, Ghadge GD, Kennedy SG, Hay N, Miller RJ and Roos RP. (1999). J. Neurosci., 19, 5360–5369.

Anmerkungen

Ohne Hinweis auf eine Übernahme.

Sichter
(Graf Isolan), SleepyHollow02

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