Fosfoinositide 3-chinasi: differenze tra le versioni
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== Bibliografia == |
== Bibliografia == |
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=== Riviste === |
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*{{Cite journal |author=Vanhaesebroeck B, Leevers S, Ahmadi K, Timms J, Katso R, Driscoll P, Woscholski R, Parker P, Waterfield M|title=Synthesis and function of 3-phosphorylated inositol lipids |journal=Annu Rev Biochem |volume=70 |issue= |pages=535–602 |year= 2001|id= PMID 11395417 |doi=10.1146/annurev.biochem.70.1.535}} |
*{{Cite journal |author=Vanhaesebroeck B, Leevers S, Ahmadi K, Timms J, Katso R, Driscoll P, Woscholski R, Parker P, Waterfield M|title=Synthesis and function of 3-phosphorylated inositol lipids |journal=Annu Rev Biochem |volume=70 |issue= |pages=535–602 |year= 2001|id= PMID 11395417 |doi=10.1146/annurev.biochem.70.1.535}} |
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*{{Cite journal |author=Schild C, Wirth M, Reichert M, Schmid RM, Saur D, Schneider G |title=PI3K signaling maintains c-myc expression to regulate transcription of E2F1 in pancreatic cancer cells |journal=Mol. Carcinog. |volume= 48|issue= 12|pages= 1149–58|year=2009 |month=July|id= PMID 19603422 |doi=10.1002/mc.20569 |url=}} |
*{{Cite journal |author=Schild C, Wirth M, Reichert M, Schmid RM, Saur D, Schneider G |title=PI3K signaling maintains c-myc expression to regulate transcription of E2F1 in pancreatic cancer cells |journal=Mol. Carcinog. |volume= 48|issue= 12|pages= 1149–58|year=2009 |month=July|id= PMID 19603422 |doi=10.1002/mc.20569 |url=}} |
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*{{Cite journal |url=http://www.biochemsoctrans.org/bst/037/0615/bst0370615.htm |title=Form and flexibility in phosphoinositide 3-kinases|first5=X |last5=Zhang |first4=WC |last4=Hon |first3=S |last3=Miller |first2=A |last2=Berndt |author=Williams et al. |year=2009 |id= PMID 19614567|doi=10.1042/BST0370615 |journal=Biochemical Society Transactions |volume=37 |issue=Pt 4 |pages=615–626}} |
*{{Cite journal |url=http://www.biochemsoctrans.org/bst/037/0615/bst0370615.htm |title=Form and flexibility in phosphoinositide 3-kinases|first5=X |last5=Zhang |first4=WC |last4=Hon |first3=S |last3=Miller |first2=A |last2=Berndt |author=Williams et al. |year=2009 |id= PMID 19614567|doi=10.1042/BST0370615 |journal=Biochemical Society Transactions |volume=37 |issue=Pt 4 |pages=615–626}} |
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=== Testi === |
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*{{cite book|author1=Bart Vanhaesebroeck|author2=Christian Rommel|title=Phosphoinositide 3-Kinase in Health and Disease, Volume 1|url=http://books.google.com/books?id=RI3dSUJ0BbcC&pg=PA72|accessdate= |date=30 December 2010|publisher=Springer|isbn=978-3-642-13662-7|pages=72–}} |
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*{{cite book|author1=David J. Matthews|author2=Mary E. Gerritsen|title=Targeting Protein Kinases for Cancer Therapy|url=http://books.google.com/books?id=I5Xg905JDcoC&pg=PA275|accessdate=8 September 2011|date= |publisher=John Wiley and Sons|isbn=978-0-470-22965-1|pages=275–}} |
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*{{cite book|author1=Vassil St. Georgiev|author2=Kathryn C. Zoon, Ph.D. (FRW)|title=National Institute of Allergy and Infectious Diseases, NIH: Volume 3: Intramural Research|url=http://books.google.com/books?id=WWhcvy2hTtQC&pg=PA292|accessdate= |date=28 September 2010|publisher=Springer|isbn=978-1-60761-511-8|pages=292–}} |
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*{{cite book|author=Miguel H. Bronchud|title=Principles of molecular oncology|url=http://books.google.com/books?id=vdHJAyll5XMC&pg=PA169|accessdate= |year=2008|publisher=Springer|isbn=978-1-934115-25-1|pages=169–}} |
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{{portale|biologia}} |
{{portale|biologia}} |
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Versione delle 14:44, 8 set 2011
| fosfatidilinositolo-3-chinasi | |
|---|---|
 Modello tridimensionale dell'enzima | |
| Numero EC | 2.7.1.4 |
| Classe | Transferasi |
| Altri nomi | |
| PI 3-chinasi; PI3K | |
| Banche dati | BRENDA, EXPASY, GTD, PDB (RCSB PDB PDBe PDBj PDBsum) |
| Fonte: IUBMB | |
La fosfoinositide 3-chinasi o fosfatidilinositolo-3-chinasi o PI 3-chinasi o PI3K sono una famiglia di enzimi coinvolti in complessi meccanismi cellulari come la crescita cellulare, la proliferazione, la differenziazione, la motilità e la sopravvivenza intracellulare;[1] meccanismi questi coinvolti, anche, nello sviluppo del cancro.[2]
Le PI3K sono enzimi che trasducono i segnali intracellulari che sono in grado di fosforilare l'idrossile in posizione 3 presente sull'anello dell'inositolo, trasformandolo in fosfatidilinositolo (PtdIns).[3] Questa classe di enzimi è anche nota come fosfatidilinositolo-3-chinasi. La via metabolica, con oncogene PIK3CA e con il gene oncosoppressore PTEN, è implicata nei fenomeni di insensibilità dei tumori all'insulina e di IGF1 , in soggetti sottoposti alla restrizione calorica.[4][5]
Note
- ^ The phosphoinositide (PI) 3-kinase family, su jcs.biologists.org.
- ^ Prospects for phosphoinositide 3-kinase inhibition as a cancer treatment., su erc.endocrinology-journals.org.
- ^ myo-inositol, su chem.qmul.ac.uk.
- ^ Giese N, Cell pathway on overdrive prevents cancer response to dietary restriction, su physorg.com, 11 marzo 2009. URL consultato il 22 aprile 2009.
- ^ Kalaany NY, Sabatini DM, Tumours with PI3K activation are resistant to dietary restriction, in Nature, vol. 458, n. 7239, April 2009, pp. 725–31, DOI:10.1038/nature07782.
Bibliografia
Riviste
- Vanhaesebroeck B, Leevers S, Ahmadi K, Timms J, Katso R, Driscoll P, Woscholski R, Parker P, Waterfield M, Synthesis and function of 3-phosphorylated inositol lipids, in Annu Rev Biochem, vol. 70, 2001, pp. 535–602, DOI:10.1146/annurev.biochem.70.1.535, PMID 11395417.
- Schild C, Wirth M, Reichert M, Schmid RM, Saur D, Schneider G, PI3K signaling maintains c-myc expression to regulate transcription of E2F1 in pancreatic cancer cells, in Mol. Carcinog., vol. 48, n. 12, July 2009, pp. 1149–58, DOI:10.1002/mc.20569, PMID 19603422.
- Williams et al., Form and flexibility in phosphoinositide 3-kinases, in Biochemical Society Transactions, vol. 37, Pt 4, 2009, pp. 615–626, DOI:10.1042/BST0370615, PMID 19614567.
Testi
- Phosphoinositide 3-Kinase in Health and Disease, Volume 1, Springer, 30 December 2010, pp. 72–, ISBN 978-3-642-13662-7.
- Targeting Protein Kinases for Cancer Therapy, John Wiley and Sons, pp. 275–, ISBN 978-0-470-22965-1. URL consultato l'8 September 2011.
- National Institute of Allergy and Infectious Diseases, NIH: Volume 3: Intramural Research, Springer, 28 September 2010, pp. 292–, ISBN 978-1-60761-511-8.
- Miguel H. Bronchud, Principles of molecular oncology, Springer, 2008, pp. 169–, ISBN 978-1-934115-25-1.
