CoChat
Sign Up
Cited by 182FOXO transcription factor regulationMuscle Physiology and DisordersFibroblast Growth Factor Research

OutFOXOing disease and disability: the therapeutic potential of targeting FoxO proteins

Open access
Maiese, Kenneth, Chong, Zhao Zhong, Shang, Yan Chen·2008·Trends in Molecular Medicine
DOI 10.1016/j.molmed.2008.03.002PMC PMC2572150
Open this paper in CoChat — free account

Abstract

Forkhead transcription factors have a 'winged helix' domain and regulate processes that range from cell longevity to cell death. Of the mammalian forkhead family members in the O class, FoxO1, FoxO3a and FoxO4 can fill a crucial void for the treatment of disorders that include aging, cancer, diabetes, infertility, neurodegeneration and immune system dysfunction. Yet, observations that forkhead family members also can compromise clinical utility have fueled controversy and highlight the necessity to further outline the integrated cellular pathways governed by these transcription factors. Here we discuss recent advances that have elucidated the unique cellular pathways and clinical potential of targeting FoxO proteins to develop novel therapeutic strategies and avert potential pitfalls that might be closely intertwined with its benefits for patient care.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.molmed.2008.03.002

Cites

4 of 4 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Apoptosis in cells involves both an early phase consisting of exposure of membrane PS residues and a late phase involving destruction of genomic DNA.

    “Apoptosis in cells involves both an early phase consisting of the exposure of membrane PS residues and a late phase that involves the destruction of genomic DNA [23, 45–47].”

    From Tuberous Sclerosis Protein 2 (TSC2) Modulates CCN4 Cytoprotection During Apoptotic Amyloid Toxicity in Microglia (2013) · cites this paper as [46]

    The Introduction discusses FoxO-related apoptotic pathways, but does not describe membrane phosphatidylserine exposure as an early phase or genomic DNA destruction as a late phase. Searches for those terms found only related reference titles, not a passage in this paper stating the claimed sequence. (LLM, conf=0.72)

    Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Research works printed but not linked: 86

  1. [1]Chong ZZ, et al. Oxidative stress in the brain: novel cellular targets that govern survival during neurodegenerative disease. Prog. Neurobiol. 2005;75:207–246. doi: 10.1016/j.pneurobio.2005.02.004. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  2. [2]Maiese K, et al. Sly as a FOXO: new paths with Forkhead signaling in the brain. Curr. Neurovasc. Res. 2007;4:295–302. doi: 10.2174/156720207782446306. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  3. [3]Hoekman MF, et al. Spatial and temporal expression of FoxO transcription factors in the developing and adult murine brain. Gene Expr. Patterns. 2006;6:134–140. doi: 10.1016/j.modgep.2005.07.003. [DOI] [PubMed] [Google Scholar] · DOI
  4. [4]Jagani Z, et al. FoxO tumor suppressors and BCR-ABL-induced leukemia: a matter of evasion of apoptosis. Biochim. Biophys. Acta. 2008;1785:63–84. doi: 10.1016/j.bbcan.2007.10.003. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  5. [5]Myatt SS, Lam EW. The emerging roles of forkhead box (Fox) proteins in cancer. Nat. Rev. Cancer. 2007;7:847–859. doi: 10.1038/nrc2223. [DOI] [PubMed] [Google Scholar] · DOI
  6. [7]Wijchers PJ, et al. In control of biology: of mice, men and Foxes. Biochem. J. 2006;397:233–246. doi: 10.1042/BJ20060387. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  7. [8]Biggs WH, 3rd, et al. Identification and characterization of members of the FKHR (FOX O) subclass of winged-helix transcription factors in the mouse. Mamm. Genome. 2001;12:416–425. doi: 10.1007/s003350020002. [DOI] [PubMed] [Google Scholar] · DOI
  8. [9]Huang H, Tindall DJ. Dynamic FoxO transcription factors. J. Cell Sci. 2007;120:2479–2487. doi: 10.1242/jcs.001222. [DOI] [PubMed] [Google Scholar] · DOI
  9. [10]Van Der Heide LP, et al. The ins and outs of FoxO shuttling: mechanisms of FoxO translocation and transcriptional regulation. Biochem. J. 2004;380:297–309. doi: 10.1042/BJ20040167. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  10. [11]Furuyama T, et al. Identification of the differential distribution patterns of mRNAs and consensus binding sequences for mouse DAF-16 homologues. Biochem. J. 2000;349:629–634. doi: 10.1042/0264-6021:3490629. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  11. [12]Hosaka T, et al. Disruption of forkhead transcription factor (FOXO) family members in mice reveals their functional diversification. Proc. Natl. Acad. Sci. U. S. A. 2004;101:2975–2980. doi: 10.1073/pnas.0400093101. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  12. [13]Castrillon DH, et al. Suppression of ovarian follicle activation in mice by the transcription factor Foxo3a. Science. 2003;301:215–218. doi: 10.1126/science.1086336. [DOI] [PubMed] [Google Scholar] · DOI
  13. [14]Liu L, et al. Infertility caused by retardation of follicular development in mice with oocyte-specific expression of Foxo3a. Development. 2007;134:199–209. doi: 10.1242/dev.02667. [DOI] [PubMed] [Google Scholar] · DOI
  14. [15]Lin L, et al. Regulation of NF-kappaB, Th activation, and autoinflammation by the forkhead transcription factor Foxo3a. Immunity. 2004;21:203–213. doi: 10.1016/j.immuni.2004.06.016. [DOI] [PubMed] [Google Scholar] · DOI
  15. [16]Jonsson H, et al. Inflammatory arthritis requires Foxo3a to prevent Fas ligand-induced neutrophil apoptosis. Nat. Med. 2005;11:666–671. doi: 10.1038/nm1248. [DOI] [PubMed] [Google Scholar] · DOI
  16. [18]Miyamoto K, et al. Foxo3a is essential for maintenance of the hematopoietic stem cell pool. Cell Stem Cell. 2007;1:101–112. doi: 10.1016/j.stem.2007.02.001. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  17. [19]Mahmud DL, et al. Phosphorylation of forkhead transcription factors by erythropoietin and stem cell factor prevents acetylation and their interaction with coactivator p300 in erythroid progenitor cells. Oncogene. 2002;21:1556–1562. doi: 10.1038/sj.onc.1205230. [DOI] [PubMed] [Google Scholar] · DOI
  18. [20]Maiese K, et al. New avenues of exploration for erythropoietin. J. Am. Med. Assoc. 2005;293:90–95. doi: 10.1001/jama.293.1.90. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  19. [21]Bakker WJ, et al. Differential regulation of Foxo3a target genes in erythropoiesis. Mol. Cell. Biol. 2007;27:3839–3854. doi: 10.1128/MCB.01662-06. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  20. [22]Srinivasan S, et al. Enteric neuroblasts require the phosphatidylinositol 3-kinase/Akt/Forkhead pathway for GDNF-stimulated survival. Mol. Cell. Neurosci. 2005;29:107–119. doi: 10.1016/j.mcn.2005.02.005. [DOI] [PubMed] [Google Scholar] · DOI
  21. [23]Maiese K, et al. Mechanisitic insights into diabetes mellitus and oxidative stress. Curr. Med. Chem. 2007;14:1729–1738. doi: 10.2174/092986707781058968. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  22. [24]Maiese K, et al. Oxidative stress biology and cell injury during type 1 and type 2 diabetes mellitus. Curr. Neurovasc. Res. 2007;4:63–71. doi: 10.2174/156720207779940653. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  23. [25]Fallarino F, et al. CTLA-4-Ig activates forkhead transcription factors and protects dendritic cells from oxidative stress in nonobese diabetic mice. J. Exp. Med. 2004;200:1051–1062. doi: 10.1084/jem.20040942. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  24. [26]Matsumoto M, et al. Impaired regulation of hepatic glucose production in mice lacking the forkhead transcription factor foxo1 in liver. Cell Metab. 2007;6:208–216. doi: 10.1016/j.cmet.2007.08.006. [DOI] [PubMed] [Google Scholar] · DOI
  25. [27]Kato M, et al. Role of the Akt/FoxO3a pathway in TGF-beta1-mediated mesangial cell dysfunction: a novel mechanism related to diabetic kidney disease. J. Am. Soc. Nephrol. 2006;17:3325–3335. doi: 10.1681/ASN.2006070754. [DOI] [PubMed] [Google Scholar] · DOI
  26. [28]Chong ZZ, et al. Vascular injury during elevated glucose can be mitigated by erythropoietin and Wnt signaling. Curr. Neurovasc. Res. 2007;4:194–204. doi: 10.2174/156720207781387150. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  27. [29]Anitha M, et al. GDNF rescues hyperglycemia-induced diabetic enteric neuropathy through activation of the PI3K/Akt pathway. J. Clin. Invest. 2006;116:344–356. doi: 10.1172/JCI26295. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  28. [30]Kwon HS, et al. Protein kinase B-alpha inhibits human pyruvate dehydrogenase kinase-4 gene induction by dexamethasone through inactivation of FOXO transcription factors. Diabetes. 2004;53:899–910. doi: 10.2337/diabetes.53.4.899. [DOI] [PubMed] [Google Scholar] · DOI
  29. [31]Kino T, et al. HIV-1 accessory protein Vpr inhibits the effect of insulin on the Foxo subfamily of forkhead transcription factors by interfering with their binding to 14-3-3 proteins: potential clinical implications regarding the insulin resistance of HIV-1-infected patients. Diabetes. 2005;54:23–31. doi: 10.2337/diabetes.54.1.23. [DOI] [PubMed] [Google Scholar] · DOI
  30. [32]Maiese K, Chong ZZ. Nicotinamide: necessary nutrient emerges as a novel cytoprotectant for the brain. Trends Pharmacol. Sci. 2003;24:228–232. doi: 10.1016/S0165-6147(03)00078-6. [DOI] [PubMed] [Google Scholar] · DOI
  31. [33]Furuyama T, et al. Effects of aging and caloric restriction on the gene expression of Foxo1, 3, and 4 (FKHR, FKHRL1, and AFX) in the rat skeletal muscles. Microsc. Res. Tech. 2002;59:331–334. doi: 10.1002/jemt.10213. [DOI] [PubMed] [Google Scholar] · DOI
  32. [34]Puig O, Tjian R. Transcriptional feedback control of insulin receptor by dFOXO/FOXO1. Genes Dev. 2005;19:2435–2446. doi: 10.1101/gad.1340505. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  33. [35]Kamei Y, et al. Skeletal muscle FOXO1 (FKHR) transgenic mice have less skeletal muscle mass, down-regulated Type I (slow twitch/red muscle) fiber genes, and impaired glycemic control. J. Biol. Chem. 2004;279:41114–41123. doi: 10.1074/jbc.M400674200. [DOI] [PubMed] [Google Scholar] · DOI
  34. [36]Chong ZZ, et al. Erythropoietin requires NF-kappaB and its nuclear translocation to prevent early and late apoptotic neuronal injury during beta-amyloid toxicity. Curr. Neurovasc. Res. 2005;2:387–399. doi: 10.2174/156720205774962683. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  35. [37]Chong ZZ, et al. Cellular demise and inflammatory microglial activation during beta-amyloid toxicity are governed by Wnt1 and canonical signaling pathways. Cell. Signal. 2007;19:1150–1162. doi: 10.1016/j.cellsig.2006.12.009. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  36. [38]Smith WW, et al. Phosphorylation of p66Shc and forkhead proteins mediates Abeta toxicity. J. Cell Biol. 2005;169:331–339. doi: 10.1083/jcb.200410041. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  37. [39]Essers MA, et al. Functional interaction between beta-catenin and FOXO in oxidative stress signaling. Science. 2005;308:1181–1184. doi: 10.1126/science.1109083. [DOI] [PubMed] [Google Scholar] · DOI
  38. [40]Nakamura T, Sakamoto K. Forkhead transcription factor FOXO subfamily is essential for reactive oxygen species-induced apoptosis. Mol. Cell. Endocrinol. 2008;281:47–55. doi: 10.1016/j.mce.2007.10.007. [DOI] [PubMed] [Google Scholar] · DOI
  39. [41]Won CK, et al. Estradiol prevents the focal cerebral ischemic injury-induced decrease of forkhead transcription factors phosphorylation. Neurosci. Lett. 2006;398:39–43. doi: 10.1016/j.neulet.2005.12.060. [DOI] [PubMed] [Google Scholar] · DOI
  40. [42]Chong ZZ, et al. Group I metabotropic receptor neuroprotection requires Akt and its substrates that govern FOXO3a, Bim, and beta-Catenin during oxidative stress. Curr. Neurovasc. Res. 2006;3:107–117. doi: 10.2174/156720206776875830. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  41. [43]Chong ZZ, et al. The NAD+ precursor nicotinamide governs neuronal survival during oxidative stress through protein kinase B coupled to FOXO3a and mitochondrial membrane potential. J. Cereb. Blood Flow Metab. 2004;24:728–743. doi: 10.1097/01.WCB.0000122746.72175.0E. [DOI] [PubMed] [Google Scholar] · DOI
  42. [44]Chong ZZ, Maiese K. Erythropoietin involves the phosphatidylinositol 3-kinase pathway, 14-3-3 protein and FOXO3a nuclear trafficking to preserve endothelial cell integrity. Br. J. Pharmacol. 2007;150:839–850. doi: 10.1038/sj.bjp.0707161. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  43. [45]Zheng WH, et al. FKHRL1 and its homologs are new targets of nerve growth factor Trk receptor signaling. J. Neurochem. 2002;80:1049–1061. doi: 10.1046/j.0022-3042.2002.00783.x. [DOI] [PubMed] [Google Scholar] · DOI
  44. [46]Barthélémy C, et al. Foxo3a induces motoneuron death through the Fas pathway in cooperation with JNK. BMC Neurosci. 2004;5:48. doi: 10.1186/1471-2202-5-48. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  45. [47]Obexer P, et al. FKHRL1-mediated expression of Noxa and Bim induces apoptosis via the mitochondria in neuroblastoma cells. Cell Death Differ. 2007;14:534–547. doi: 10.1038/sj.cdd.4402017. [DOI] [PubMed] [Google Scholar] · DOI
  46. [48]You H, et al. Regulation of transactivation-independent proapoptotic activity of p53 by FOXO3a. Proc. Natl. Acad. Sci. U. S. A. 2006;103:9051–9056. doi: 10.1073/pnas.0600889103. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  47. [49]Furukawa-Hibi Y, et al. FOXO forkhead transcription factors induce G(2)-M checkpoint in response to oxidative stress. J. Biol. Chem. 2002;277:26729–26732. doi: 10.1074/jbc.C200256200. [DOI] [PubMed] [Google Scholar] · DOI
  48. [50]Delpuech O, et al. Induction of Mxi1-SR{alpha} by FOXO3a contributes to repression of Myc-dependent gene expression. Mol. Cell. Biol. 2007;27:4917–4930. doi: 10.1128/MCB.01789-06. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  49. [51]Kikuchi S, et al. Active FKHRL1 overcomes imatinib resistance in chronic myelogenous leukemia-derived cell lines via the production of tumor necrosis factor-related apoptosis-inducing ligand. Cancer Sci. 2007;98:1949–1958. doi: 10.1111/j.1349-7006.2007.00623.x. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  50. [52]Jacobsen EA, et al. Growth, differentiation, and malignant transformation of pre-B cells mediated by inducible activation of v-Abl oncogene. J. Immunol. 2006;176:6831–6838. doi: 10.4049/jimmunol.176.11.6831. [DOI] [PubMed] [Google Scholar] · DOI
  51. [54]Kang JQ, et al. Critical role for Akt1 in the modulation of apoptotic phosphatidylserine exposure and microglial activation. Mol. Pharmacol. 2003;64:557–569. doi: 10.1124/mol.64.3.557. [DOI] [PubMed] [Google Scholar] · DOI
  52. [55]Li F, et al. Microglial integrity is maintained by erythropoietin through integration of Akt and its substrates of glycogen synthase kinase-3beta, beta-catenin, and nuclear factor-kappaB. Curr. Neurovasc. Res. 2006;3:187–201. doi: 10.2174/156720206778018758. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  53. [56]Sela U, et al. The negative regulators Foxj1 and Foxo3a are up-regulated by a peptide that inhibits systemic lupus erythematosus-associated T cell responses. Eur. J. Immunol. 2006;36:2971–2980. doi: 10.1002/eji.200636137. [DOI] [PubMed] [Google Scholar] · DOI
  54. [57]Hur EM, et al. Osteopontin-induced relapse and progression of autoimmune brain disease through enhanced survival of activated T cells. Nat. Immunol. 2007;8:74–83. doi: 10.1038/ni1415. [DOI] [PubMed] [Google Scholar] · DOI
  55. [58]Li F, et al. Cell life versus cell longevity: the mysteries surrounding the NAD(+) precursor nicotinamide. Curr. Med. Chem. 2006;13:883–895. doi: 10.2174/092986706776361058. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  56. [59]Tissenbaum HA, Guarente L. Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature. 2001;410:227–230. doi: 10.1038/35065638. [DOI] [PubMed] [Google Scholar] · DOI
  57. [60]Nemoto S, et al. Nutrient availability regulates SIRT1 through a forkhead-dependent pathway. Science. 2004;306:2105–2108. doi: 10.1126/science.1101731. [DOI] [PubMed] [Google Scholar] · DOI
  58. [61]Motta MC, et al. Mammalian SIRT1 represses forkhead transcription factors. Cell. 2004;116:551–563. doi: 10.1016/s0092-8674(04)00126-6. [DOI] [PubMed] [Google Scholar] · DOI
  59. [62]Kobayashi Y, et al. SIRT1 is critical regulator of FOXO-mediated transcription in response to oxidative stress. Int. J. Mol. Med. 2005;16:237–243. [PubMed] [Google Scholar]
  60. [63]van der Horst A, et al. FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1) J. Biol. Chem. 2004;279:28873–28879. doi: 10.1074/jbc.M401138200. [DOI] [PubMed] [Google Scholar] · DOI
  61. [64]Kyoung Kim H, et al. Down-regulation of a forkhead transcription factor, FOXO3a, accelerates cellular senescence in human dermal fibroblasts. J. Gerontol. A Biol. Sci. Med. Sci. 2005;60:4–9. doi: 10.1093/gerona/60.1.4. [DOI] [PubMed] [Google Scholar] · DOI
  62. [65]Ferrara N, et al. Exercise training promotes SIRT1 activity in aged rats. Rejuvenation Res. 2008;11:139–150. doi: 10.1089/rej.2007.0576. [DOI] [PubMed] [Google Scholar] · DOI
  63. [66]Li M, et al. Down-regulation of manganese-superoxide dismutase through phosphorylation of FOXO3a by Akt in explanted vascular smooth muscle cells from old rats. J. Biol. Chem. 2006;281:40429–40439. doi: 10.1074/jbc.M606596200. [DOI] [PubMed] [Google Scholar] · DOI
  64. [67]Miyauchi H, et al. Akt negatively regulates the in vitro lifespan of human endothelial cells via a p53/p21-dependent pathway. EMBO J. 2004;23:212–220. doi: 10.1038/sj.emboj.7600045. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  65. [68]Paik JH, et al. FoxOs are lineage-restricted redundant tumor suppressors and regulate endothelial cell homeostasis. Cell. 2007;128:309–323. doi: 10.1016/j.cell.2006.12.029. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI · Paper page
  66. [69]Sunters A, et al. Paclitaxel-induced nuclear translocation of FOXO3a in breast cancer cells is mediated by c-Jun NH2-terminal kinase and Akt. Cancer Res. 2006;66:212–220. doi: 10.1158/0008-5472.CAN-05-1997. [DOI] [PubMed] [Google Scholar] · DOI
  67. [70]Eddy SF, et al. Trastuzumab-resistant HER2-driven breast cancer cells are sensitive to epigallocatechin-3 gallate. Cancer Res. 2007;67:9018–9023. doi: 10.1158/0008-5472.CAN-07-1691. [DOI] [PubMed] [Google Scholar] · DOI
  68. [71]Modur V, et al. FOXO proteins regulate tumor necrosis factor-related apoptosis inducing ligand expression. Implications for PTEN mutation in prostate cancer. J. Biol. Chem. 2002;277:47928–47937. doi: 10.1074/jbc.M207509200. [DOI] [PubMed] [Google Scholar] · DOI
  69. [72]Lynch RL, et al. The progression of LNCaP human prostate cancer cells to androgen independence involves decreased FOXO3a expression and reduced p27KIP1 promoter transactivation. Mol. Cancer Res. 2005;3:163–169. doi: 10.1158/1541-7786.MCR-04-0163. [DOI] [PubMed] [Google Scholar] · DOI
  70. [73]Li Y, et al. Regulation of FOXO3a/beta-catenin/GSK-3beta signaling by 3, 3′-diindolylmethane contributes to inhibition of cell proliferation and induction of apoptosis in prostate cancer cells. J. Biol. Chem. 2007;282:21542–21550. doi: 10.1074/jbc.M701978200. [DOI] [PubMed] [Google Scholar] · DOI
  71. [75]Ticchioni M, et al. Homeostatic chemokines increase survival of B-chronic lymphocytic leukemia cells through inactivation of transcription factor FOXO3a. Oncogene. 2007;26:7081–7091. doi: 10.1038/sj.onc.1210519. [DOI] [PubMed] [Google Scholar] · DOI
  72. [76]Munoz-Fontela C, et al. Latent protein LANA2 from Kaposi's sarcoma-associated herpesvirus interacts with 14-3-3 proteins and inhibits FOXO3a transcription factor. J. Virol. 2007;81:1511–1516. doi: 10.1128/JVI.01816-06. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  73. [77]Arimoto-Ishida E, et al. Inhibition of phosphorylation of a forkhead transcription factor sensitizes human ovarian cancer cells to cisplatin. Endocrinology. 2004;145:2014–2022. doi: 10.1210/en.2003-1199. [DOI] [PubMed] [Google Scholar] · DOI
  74. [78]Chong ZZ, et al. Erythropoietin is a novel vascular protectant through activation of Akt1 and mitochondrial modulation of cysteine proteases. Circulation. 2002;106:2973–2979. doi: 10.1161/01.cir.0000039103.58920.1f. [DOI] [PubMed] [Google Scholar] · DOI
  75. [79]Chong ZZ, et al. Activating Akt and the brain's resources to drive cellular survival and prevent inflammatory injury. Histol. Histopathol. 2005;20:299–315. doi: 10.14670/hh-20.299. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  76. [80]Hu MC, et al. IkappaB kinase promotes tumorigenesis through inhibition of forkhead FOXO3a. Cell. 2004;117:225–237. doi: 10.1016/s0092-8674(04)00302-2. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  77. [81]Leong ML, et al. Expression of the serum- and glucocorticoid-inducible protein kinase, Sgk, is a cell survival response to multiple types of environmental stress stimuli in mammary epithelial cells. J. Biol. Chem. 2003;278:5871–5882. doi: 10.1074/jbc.M211649200. [DOI] [PubMed] [Google Scholar] · DOI
  78. [82]Lehtinen MK, et al. A conserved MST-FOXO signaling pathway mediates oxidative-stress responses and extends life span. Cell. 2006;125:987–1001. doi: 10.1016/j.cell.2006.03.046. [DOI] [PubMed] [Google Scholar] · DOI
  79. [83]Watkins WJ, et al. Mutational screening of FOXO3A and FOXO1A in women with premature ovarian failure. Fertil. Steril. 2006;86:1518–1521. doi: 10.1016/j.fertnstert.2006.03.054. [DOI] [PubMed] [Google Scholar] · DOI
  80. [84]Ludikhuize J, et al. Inhibition of forkhead box class O family member transcription factors in rheumatoid synovial tissue. Arthritis Rheum. 2007;56:2180–2191. doi: 10.1002/art.22653. [DOI] [PubMed] [Google Scholar] · DOI
  81. [85]Kuo CC, Lin SC. Altered FOXO1 transcript levels in peripheral blood mononuclear cells of systemic lupus erythematosus and rheumatoid arthritis patients. Mol. Med. 2007;13:561–566. doi: 10.2119/2007-00021.Kuo. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  82. [86]Kim JR, et al. Polymorphisms in FOXO gene family and association analysis with BMI. Obesity (Silver Spring) 2006;14:188–193. doi: 10.1038/oby.2006.24. [DOI] [PubMed] [Google Scholar] · DOI
  83. [87]Kuningas M, et al. Haplotypes in the human Foxo1a and Foxo3a genes; impact on disease and mortality at old age. Eur. J. Hum. Genet. 2007;15:294–301. doi: 10.1038/sj.ejhg.5201766. [DOI] [PubMed] [Google Scholar] · DOI
  84. [88]Bosque A, et al. The induction of Bim expression in human T-cell blasts is dependent on nonapoptotic Fas/CD95 signaling. Blood. 2007;109:1627–1635. doi: 10.1182/blood-2006-05-022319. [DOI] [PubMed] [Google Scholar] · DOI
  85. [89]Jin GS, et al. Expression and intracellular localization of FKHRL1 in mammary gland neoplasms. Acta Med. Okayama. 2004;58:197–205. doi: 10.18926/AMO/32088. [DOI] [PubMed] [Google Scholar] · DOI
  86. [90]Gomez-Gutierrez JG, et al. Adenovirus-mediated gene transfer of FKHRL1 triple mutant efficiently induces apoptosis in melanoma cells. Cancer Biol. Ther. 2006;5:875–883. doi: 10.4161/cbt.5.7.2911. [DOI] [PubMed] [Google Scholar] · DOI

Cited by

Sorted by citations

Authors
Maiese, K., Chong, Z. Z., & Shang, Y. C.
Affiliations
Wayne State University (US)
ORCID
Venue
Trends in Molecular Medicine
Publisher
Elsevier BV
Published
2008-05
Volume
14
Issue
5
Pages
219-227
ISSN
1471-4914 (ISSN-L)
DOI
10.1016/j.molmed.2008.03.002
PMC
PMC2572150
OpenAlex
W2020777578
Cited by
182
References
4
Citations by year
2026: 3 · 2025: 4 · 2024: 6 · 2023: 13 · 2022: 8 · 2021: 8 · 2020: 7 · 2019: 4 · 2018: 5 · 2017: 9 · 2016: 10 · 2015: 15 · 2014: 13 · 2013: 5 · 2012: 17
FWCI
1.39
Type
journal article
Language
en
Open access
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Trends in Molecular Medicine (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institutes of Health (5p30es006639-15)
  • National Institute of Neurological Disorders and Stroke (R01NS053946)
  • National Institute of Environmental Health Sciences (P30-ES006639)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › FOXO transcription factor regulation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fibroblast Growth Factor Research
Keywords
FOXO transcription factors, forkhead transcription factor, FOXO1, FOXO3, FOXO4, therapeutic targeting, aging, cancer, diabetes mellitus, infertility, neurodegeneration, immune dysfunction
MeSH terms
Forkhead Box Protein O1, Forkhead Box Protein O3, Animals, Cell Movement, Gene Expression Regulation, Humans, Models, Biological, Neoplasms, Transcription Factors, Drug Design, Signal Transduction, Apoptosis, Oxidative Stress, Cell Cycle Proteins, Protein Transport, Forkhead Transcription Factors

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review