The development of phosphatidylinositol ether lipid analogues as inhibitors of the serine/threonine kinase, Akt

Bibliography

• COFFER PJ, JIN J, WOODGETT JR: Protein kinase B (c-Akt): a multifunctional mediator of phosphatidylinositol 3-kinase activation. Biochern. J. (1998) 335(Pt 1):1–13.
   PubMed Web of Science ®Google Scholar
• ZINDA MJ, JOHNSON MA, PAUL JD et al.: AKT-1, -2, and -3 are expressed in both normal and tumor tissues of the lung, breast, prostate, and colon. Clin. Cancer Res. (2001) 7(8):2475–2479.
   PubMed Web of Science ®Google Scholar
• HEWITT S, YANG X, STEINBERG X, SWAIN SM, DENNIS PA: In situ analysis of the PI3K/Akt pathway in normal and cancerous tissues on human multi-tissue arrays. (Submitted).
   Google Scholar
• ERMOIAN RP, FURNISS CS, LAMBORN KR et al.: Dysregulation of PTEN and protein kinase B is associated with glioma histology and patient survival. Clin. Cancer Res. (2002) 8(5):1100–1106.
   PubMed Web of Science ®Google Scholar
• PEREZ-TENORIO G, STAL 0: Activation of AKT/PKB in breast cancer predicts a worse outcome among endocrine treated patients. Br. J. Cancer (2002) 86(4):540–545.
   PubMed Web of Science ®Google Scholar
• TSAO AS, MeDONNELL T, LAM Set al.: Increased phospho-AKT (Ser(473)) expression in bronchial dysplasia: implications for lung cancer prevention studies. Cancer Epidennol. Biomarkers Prey. (2003) 12(7):660–664.
   Google Scholar
• ROY HK, OLUSOLA BE CLEMENS DL et al.: AKT proto-oncogene overexpression is an early event during sporadic colon carcinogenesis. Carcinogenesis (2002) 23(1):201–205.
   Google Scholar
• STAAL SP: Molecular cloning of the akt oncogene and its human homologues AKT1 and AKT2: amplification of AKT1 in a primary human gastric adenocarcinoma. Proc. Nati Acad. Sd. USA (1987) 84(14):5034–5037.
   PubMed Web of Science ®Google Scholar
• RUGGERI BA, HUANG L, WOOD M, CHENG JQ, TESTA JR: Amplification and overexpression of the AKT2 oncogene in a subset of human pancreatic ductal adenocarcinomas. Mol. Carcinog. (1998) 21(2):81–86.
   PubMed Web of Science ®Google Scholar
• BELLACOSA A, DE EEO D, GODWIN AK et al.: Molecular alterations of the AKT2 oncogene in ovarian and breast carcinomas. hat. Cancer(1995) 64(4):280–285.
   Web of Science ®Google Scholar
• SHAYESTEH L, LUY, KUO WL et al.: PIK3CA is implicated as an oncogene in ovarian cancer. Nat. Genet. (1999) 21(1):99–102.
   PubMed Web of Science ®Google Scholar
• MA YY, WET SJ, UN YC et al.: PIK3CA as an oncogene in cervical cancer. Oncogene (2000) 19(23):2739–2744.
   PubMed Web of Science ®Google Scholar
• VIVANCO I, SAWYERS CL: The phosphatidylinositol 3-kinase AKT pathway in human cancer. Nat. Rev Cancer (2002) 2(7):489–501.
   PubMed Web of Science ®Google Scholar
• ••Excellent, comprehensive review of theP13-K/Akt pathway in cancer biology.
   Google Scholar
• CANTLEY LC, NEEL BG: New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway. Proc. Nati Acad. Sd. USA (1999) 96(8):4240–4245.
   PubMed Web of Science ®Google Scholar
• STAMBOLIC V, TSAO MS, MACPHERSON D, SUZUKI A, CHAPMAN WB, MAK TW: High incidence of breast and endometrial neoplasia resembling human Cowden syndrome in PTEN ± mice. Cancer Res. (2000) 60(13):3605–3611.
   PubMed Web of Science ®Google Scholar
• CLARK AS, WEST K, STRETCHERS, DENNIS PA: Constitutive and inducible Akt activity promotes resistance to chemotherapy, trastuzumab, or tamoxifen in breast cancer cells. Mol. Cancer Ther. (2002) 1(9):707–717.
   PubMed Web of Science ®Google Scholar
• BROGNARD J, CLARK AS, NI Y, DENNIS PA: Akt/protein kinase B is constitutively active in non-small cell lung cancer cells and promotes cellular survival and resistance to chemotherapy and radiation. Cancer Res. (2001) 61(10):3986–3997.
   PubMed Web of Science ®Google Scholar
• WEST KA, BROGNARD J, CLARK AS et al.: Rapid Akt activation by nicotine and a tobacco carcinogen modulates the phenotype of normal human airway epithelial cells. J. Clin. Invest. (2003) 111(1):81–90.
   PubMed Web of Science ®Google Scholar
• BURDICK AD, DAVIS JW 2nd, LIU KJ et al.: Benzo(a)pyrene quinones increase cell proliferation, generate reactive oxygen species, and transactivate the epidermal growth factor receptor in breast epithelial cells. Cancer Res. (2003) 63(22):7825–7833.
   Google Scholar
• SEGRELLES C, RUIZ S, PEREZ P et al.: Functional roles of Akt signaling in mouse skin tumorigenesis. Oncogene (2002) 21(1):53–64.
   PubMed Web of Science ®Google Scholar
• SOUZA K, MADDOCK DA, ZHANG Q et al.: Arsenite activation of P 1 3K/AKT cell survival pathway is mediated by p38 in cultured human keratinocytes. Mol. Med. (2001) 7(11):767–772.
   PubMed Web of Science ®Google Scholar
• MANNING G, WHYTE DB, MARTINEZ R, HUNTER T, SUDARSANAM S: The protein kinase complement of the human genome. Science (2002) 298(5600):1912–1934.
   PubMed Web of Science ®Google Scholar
• LEMMON MA, FERGUSON KM, ABRAMS CS: Pleckstrin homology domains and the cytoskeleton. FEBS Lett. (2002) 513(1):71–76.
   PubMed Web of Science ®Google Scholar
• BALENDRAN A, CASAMAYOR A, DEAK M et al.: PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2. Carr. Biol. (1999) 9(8):393–404.
   PubMed Web of Science ®Google Scholar
• DELCOMMENNE M, TAN C, GRAY V, RUE L, WOOD GETT J, DEDHAR S: Phosphoinositide-3-0H kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. Proc. Natl. Acad. Sci. USA (1998) 95(19):11211–11216.
   PubMed Web of Science ®Google Scholar
• LYNCH DK, ELLIS CA, EDWARDS PA, HILES ID: Integrin-linked kinase regulates phosphorylation of serine 473 of protein kinase B by an indirect mechanism. Oncogene (1999) 18(56):8024–8032.
   PubMed Web of Science ®Google Scholar
• TOKER A, NEWTON AC: Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK-2 site. 1 Biol. Chem. (2000) 275(12):8271–8274.
   Google Scholar
• HILL MM, FENG J, HEMMINGS BA: Identification of a plasma membrane Raft-associated PKB Ser473 kinase activity that is distinct from ILK and PDK1. Curt: Biol. (2002) 12(14):1251–1255.
   PubMed Web of Science ®Google Scholar
• FILIPPA N, SABLE CL, FILLOUX C, HEMMINGS B, VAN OBBERGHEN E: Mechanism of protein kinase B activation by cyclic AMP-dependent protein kinase. Mol. Cell. Biol. (1999) 19(7):4989–5000.
   PubMed Web of Science ®Google Scholar
• YANO S, TOKUMITSU H, SODERLING TR: Calcium promotes cell survival through CaM-K kinase activation of the protein-kinase-B pathway. Nature (1998) 396(6711):584–587.
   PubMed Web of Science ®Google Scholar
• POWELL DJ, HAJDUCH E, KULAR G, HUNDAL HS: Ceramide disables 3-phosphoinositide binding to the pleckstrin homology domain of protein kinase B (PKB)/Akt by a PKCzeta-dependent mechanism. Mol. Cell. Biol. (2003) 23(21):7794–7808.
   PubMed Web of Science ®Google Scholar
• CONUS NM, HANNAN KM, CRISTIANO BE, HEMMINGS BA, PEARSON RB: Direct identification of tyrosine 474 as a regulatory phosphorylation site for the Akt protein kinase. 1 Biol. Chem. (2002) 277(41):38021–38028.
   Google Scholar
• BASSO AD, SOLIT DB, CHIOSIS G, GIRI B, TSICHLIS P, ROSEN N: Akt forms an intracellular complex with Hsp90 and Cdc37 and is destabilized by inhibitors of Hsp90 function.' Biol. Chem. (2002) 277(4):39858–39866.
   Google Scholar
• PEKARSKY Y, KOVAL A, HALLAS C et al.: Tcll enhances Akt kinase activity and mediates its nuclear translocation. Proc. Nati Acad. Sci. USA (2000) 97(7):3028–3033.
   PubMed Web of Science ®Google Scholar
• BRAZIL DP, PARK J, HEMMINGS BA: PKB binding proteins. Getting in on the Akt. Ceil (2002) 111(3):293–303.
   PubMed Web of Science ®Google Scholar
• DU K, HERZIG S, KULKARNI RN, MONTMINY M: TRB3: a tribbles homolog that inhibits Akt/PKB activation by insulin in liver. Science (2003) 300(5625):1574–1577.
   PubMed Web of Science ®Google Scholar
• POWIS G, AKSOY IA, MELDER DC et al.: D-3-deoxy-3-substituted myo-inositol analogues as inhibitors of cell growth. Cancer Chemother. Pharmacol. (1991) 29(2):95–104.
   PubMed Web of Science ®Google Scholar
• •A description of the synthesis and biological activity of 3-deoxy-myo-inositol.
   Google Scholar
• ANTONSSON B: Phosphatidylinositol synthase from mammalian tissues. Biochim. Biophys. Acta (1997) 1348(1-2):179–186.
   PubMed Web of Science ®Google Scholar
• KOZIKOWSKI AP, KIDDLE JJ, FREW T, BERGGREN M, POWIS G: Synthesis and biology of 1D-3-deoxyphosphatidylinositol: a putative antimetabolite of phosphatidylinositol-3-phosphate and an inhibitor of cancer cell colony formation. J. Med. Chem. (1995) 38(7):1053–1056.
   PubMed Web of Science ®Google Scholar
• ••A description of the synthesis of DPI, precursor to DPIEL.
   Google Scholar
• QIAO L, NAN F, KUNKEL M, GALLEGOS A, POWIS G, KOZIKOWSKI AP: 3-Deoxy-D-myo-inositol 1-phosphate, 1-phosphonate, and ether lipid analogues as inhibitors of phosphatidylinositol-3-kinase signaling and cancer cell growth. J. Med. Chem. (1998) 41(18):3303–3306.
   PubMed Web of Science ®Google Scholar
• ••A useful description of the synthetic stepsin making DPIEL.
   Google Scholar
• HU Y, QIAO L, WANG S et al: 3- (Hydroxymethyl)-bearing phosphatidylinositol ether lipid analogues and carbonate surrogates block P13-K, Akt, and cancer cell growth. I Med. Chem. (2000) 43(16):3045–3051.
   PubMed Web of Science ®Google Scholar
• •This paper is notable because it shows that a PIA with a 3'-hydroxymethyl group in an axial orientation has greater selectivity for growth factor-induced Akt inhibition than one in an equatorial position.
   Google Scholar
• MEUILLET EJ, MAHADEVAN D, VANKAYALAPATI H et al: Specific inhibition of the Aktl pleckstrin homology domain by D-3-deoxy-phosphatidyl-myo-inositol analogues. MM. Cancer Ther: (2003) 2(4):389–399.
   PubMed Web of Science ®Google Scholar
• ••An excellent paper describing thebiological activity of DPIEL, the authors show that DPIEL binds to the PH domain of Akt and inhibits growth factor-induced Akt activity.
   Google Scholar
• RONG SB, HU Y, ENYEDY I et al.: Molecular modeling studies of the Akt PH domain and its interaction with phosphoinositides. J. Med. Chem. (2001) 44(6):898–908.
   PubMed Web of Science ®Google Scholar
• •The authors perform docking studies using a model of the PH domain of Akt to explain why different PIAs have varying affinities for Akt.
   Google Scholar
• HONDAL RJ, ZHAO Z, KRAVCHUK AV et al: Mechanism of phosphatidylinositol-specific phospholipase C: a unified view of the mechanism of catalysis. Biochemistry (1998) 37(13):4568–4580.
   PubMed Web of Science ®Google Scholar
• KOZIKOWSKI AP, SUN H, BROGNARD J, DENNIS PA: Novel PI analogues selectively block activation of the pro-survival serine/threonine kinase Akt. Am. Chem. Soc. (2003) 125(5):1144–1145.
   PubMed Web of Science ®Google Scholar
• ••The initial paper describing the synthesisof 2'-substituted, 3'-deoxy PIAs, and the first to show that PIAs inhibit endogenous Akt activity in cancer cell lines.
   Google Scholar
• CASTILLO SS, BROGNARD J, PETUKHOV PA et al.: Preferential inhibition of Akt and killing of Akt-dependent cancer cells by rationally designed phosphatidylinositol ether lipid analogues. Cancer Res. (2004) 64:2782–2792.
   PubMedGoogle Scholar
• ••In this study, the authors characterise thebiological effects of a series of PIAs on the P13-K/Akt pathway. PIAs selectively cause apoptosis in cancer cell lines with high levels of active Akt.
   Google Scholar
• MILBURN CC, DEAK M, KELLY SM, PRICE NC, ALESSI DR, VAN AALTEN DM: Binding of phosphatidylinositol 3,4, 5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change. Biochem. (2003) 375(Pt 3):531–538.
   Google Scholar
• ••An elegant structural study showing thatAkt undergoes a large conformational change on phosphoinositide binding, based on the crystal structure of the PH domain of Akt.
   Google Scholar
• WEST KA, LINNOILA IR, BELINSKY SA, HARRIS CC, DENNIS PA: Tobacco carcinogen-induced cellular transformation increases activation of the phosphatidylinositol 3'-kinase/Akt pathway in vitro and in vivo. Cancer Res. (2004) 64(2):446–451.
   PubMed Web of Science ®Google Scholar
• •Using PIA5, the authors show that immortalised and transformed human lung epithelial cells depend upon Akt for survival.
   Google Scholar
• MARTELLI AM, TAZZARI PL, TABELLINI G et al.: A new selective AKT pharmacological inhibitor reduces resistance to chemotherapeutic drugs, TRAIL, all-trans-retinoic acid, and ionizing radiation of human leukemia cells. Leukemia (2003) 17(9):1794–1805.
   PubMed Web of Science ®Google Scholar
• •The first demonstration that PIAs can increase therapeutic efficacy. The authors show that a 3'-hydroxymethyl-substituted PIA reverses resistance to chemo- and radiation therapies in leukaemic cell lines.
   Google Scholar
• WEST KA, CASTILLO SS, DENNIS PA: Activation of the PI3K/Akt pathway and chemotherapeutic resistance. Drug Resist. Updat. (2002) 5(6):234–248.
   PubMed Web of Science ®Google Scholar
• GUO M, JOIAKIM A, REINERS JJ Jr: Suppression of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD)-mediated aryl hydrocarbon receptor transformation and CYP1A1 induction by the phosphatidylinositol 3-kinase inhibitor 2- (4-morpholiny1)-8-phenyl-4H-1- benzopyran-4-one (LY294002). Biochem. Pharmacol (2000) 60(5):635–642.
   PubMed Web of Science ®Google Scholar
• DAVIES SP, REDDY H, CAIVANO M, COHEN P: Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. (2000) 351(Pt 1):95–105.
   Google Scholar
• REUVENI H, LIVNAH N, GEIGER T et al.: Toward a PKB inhibitor: modification of a selective PKA inhibitor by rational design. Biochemistry (2002) 41(32):10304–10314.
   PubMed Web of Science ®Google Scholar
• LUO Y, SMITH RA, GUAN R et al.: Pseudosubstrate peptides inhibit Akt and induce cell growth inhibition. Biochemistry (2004) 43(5):1254–1263.
   PubMed Web of Science ®Google Scholar
• JETZT A, HOWE JA, HORN MT et al.: Adenoviral-mediated expression of a kinase-dead mutant of Akt induces apoptosis selectively in tumor cells and suppresses tumor growth in mice. Cancer Res. (2003) 63(20):6697–6706.
   PubMed Web of Science ®Google Scholar
• HU Y, MEUILLET EJ, BERGGREN M, POWIS G, KOZIKOWSKI AP: 3-Deoxy-3-substituted-D-myo-inositol imidazolyl ether lipid phosphates and carbonate as inhibitors of the phosphatidylinositol 3-kinase pathway and cancer cell growth. Bioorg. Med. Chem. Lett (2001) 11(2):173–176.
   PubMed Web of Science ®Google Scholar
• EGORIN MJ, PARISE RA, JOSEPH E et al.: Plasma pharmacokinetics and bioavailability of the phosphatidylinosotide-3-kinase inhibitor, OMDPI in CD2F1 mice. PrOC. Am. ASSOC. Cancer Res. (2002) 43:604–605.
   Google Scholar
• ••A thorough pharmacokinetic study ofDPIEL, available only in abstract form.
   Google Scholar
• CHEN WS, XU PZ, GOTTLOB K et al: Growth retardation and increased apoptosis in mice with homozygous disruption of the Aktl gene. Genes Dev. (2001) 15(17):2203–2208.
   PubMed Web of Science ®Google Scholar
• CHO H, MU J, KIM JK et al.: Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKB-I3). Science (2001) 292(5522):1728–1731.
   PubMed Web of Science ®Google Scholar