REFERENCES
- Bahn RS. Graves’ ophthalmopathy. N Engl J Med 2010;362:726–738.
- Hiromatsu Y, Yang D, Bednarczuk T, Miyake I, Nonaka K, Inoue Y. Cytokine profiles in eye muscle tissue and orbital fat tissue from patients with thyroid-associated ophthalmopathy. J Clin Endocrinol Metab 2000;85:1194–1199.
- Gu LQ, Jia HY, Zhao YJ, Liu N, Wang S, Cui B et al. Association studies of interleukin-8 gene in Graves’ disease and Graves’ ophthalmopathy. Endocrine 2009;36:452–456.
- Baggiolini M, Loetscher P, Moser B. Interleukin-8 and the chemokine family. Int J Immunopharmacol 1995;17:103–108.
- van Steensel L, Dik WA. The orbital fibroblast: a key player and target for therapy in graves’ ophthalmopathy. Orbit 2010;29:202–206.
- van Steensel L, Paridaens D, Dingjan GM, van Daele PL, van Hagen PM, Kuijpers RW et al. Platelet-derived growth factor-BB: a stimulus for cytokine production by orbital fibroblasts in Graves’ ophthalmopathy. Invest Ophthalmol Vis Sci 2010;51:1002–1007.
- Chang S, Perry JD, Kosmorsky GS, Braun WE. Rapamycin for treatment of refractory dysthyroid compressive optic neuropathy. Ophthal Plast Reconstr Surg 2007;23:225–226.
- Bahn YS, Xue C, Idnurm A, Rutherford JC, Heitman J, Cardenas ME. Sensing the environment: lessons from fungi. Nat Rev Microbiol 2007;5:57–69.
- Huang S, Bjornsti MA, Houghton PJ. Rapamycins: mechanism of action and cellular resistance. Cancer Biol Ther 2003;2:222–232.
- Lankat-Buttgereit B, Göke R. The tumour suppressor Pdcd4: recent advances in the elucidation of function and regulation. Biol Cell 2009;101:309–317.
- Hillard A, Hillard B, Zheng SJ, Sun H, Miwa T, Song W, et al. Translational regulation of autoimmune inflammation and lymphoma genesis by programmed cell death 4. J Immunol 2006;177:8095–8102.
- Sheedy FJ, Palsson-McDermott E, Hennessy EJ, Martin C, O’Leary JJ, Ruan Q et al. Negative regulation of TLR4 via targeting of the proinflammatory tumor suppressor PDCD4 by the microRNA miR-21. Nat Immunol 2010;11:141–147.
- Lankat-Buttgereit B, Müller S, Schmidt H, Parhofer KG, Gress TM, Göke R. Knockdown of Pdcd4 results in induction of proprotein convertase 1/3 and potent secretion of chromogranin A and secretogranin II in a neuroendocrine cell line. Biol Cell 2008;100:703–715.
- Yasuda M, Irie K, Murakami A. Inhibition by genistein of the lipopolysaccharide-induced down-regulation of programmed cell death 4 in RAW 264.7 mouse macrophages. Biosci Biotechnol Biochem 2010;74:1095–1097.
- Young MR, Santhanam AN, Yoshikawa N, Colburn NH. Have tumor suppressor PDCD4 and its counteragent oncogenic miR-21 gone rogue? Mol Interv 2010;10:76–79.
- Schmid T, Bajer MM, Blees JS, Eifler LK, Milke L, Rübsamen D et al. Inflammation-induced loss of Pdcd4 is mediated by phosphorylation-dependent degradation. Carcinogenesis 2011;32:1427–1433.
- Koumas L, Smith TJ, Phipps RP. Fibroblast subsets in the human orbit: Thy-1+ and Thy-1- subpopulations exhibit distinct phenotypes. Eur J Immunol 2002;32:477–485.
- Koumas L, Smith TJ, Feldon S, Blumberg N, Phipps RP. Thy-1 expression in human fibroblast subsets defines myofibroblastic or lipofibroblastic phenotypes. Am J Pathol 2003;163:1291–1300.
- Khoo TK, Coenen MJ, Schiefer AR, Kumar S, Bahn RS. Evidence for enhanced Thy-1 (CD90) expression in orbital fibroblasts of patients with Graves’ ophthalmopathy. Thyroid 2008;18:1291–1296.
- Göke A, Göke R, Knolle A, Trusheim H, Schmidt H, Wilmen A et al. DUG is a novel homologue of translation initiation factor 4G that binds eIF4A. Biochem Biophys Res Commun 2002;297:78–82.
- Yang HS, Jansen AP, Komar AA, Zheng X, Merrick WC, Costes S et al. The transformation suppressor Pdcd4 is a novel eukaryotic translation initiation factor 4A binding protein that inhibits translation. Mol Cell Biol 2003;23:26–37.
- Shiota M, Izumi H, Tanimoto A, Takahashi M, Miyamoto N, Kashiwagi E et al. Programmed cell death protein 4 down-regulates Y-box binding protein-1 expression via a direct interaction with Twist1 to suppress cancer cell growth. Cancer Res 2009;69:3148–3156.
- Yang HS, Jansen AP, Nair R, Shibahara K, Verma AK, Cmarik JL et al. A novel transformation suppressor, Pdcd4, inhibits AP-1 transactivation but not NF-kappaB or ODC transactivation. Oncogene 2001;20:669–676.
- Dumont FJ, Su Q. Mechanism of action of the immunosuppressant rapamycin. Life Sci 1996;58:373–395.
- Sehgal SN. Rapamune (RAPA, rapamycin, sirolimus): mechanism of action immunosuppressive effect results from blockade of signal transduction and inhibition of cell cycle progression. Clin Biochem 1998;31:335–340.
- Akselband Y, Harding MW, Nelson PA. Rapamycin inhibits spontaneous and fibroblast growth factor beta-stimulated proliferation of endothelial cells and fibroblasts. Transplant Proc 1991;23:2833–2836.
- Marx SO, Jayaraman T, Go LO, Marks AR. Rapamycin-FKBP inhibits cell cycle regulators of proliferation in vascular smooth muscle cells. Circ Res 1995;76:412–417.
- Zheng XX, Strom TB, Steele AW. Quantitative comparison of rapamycin and cyclosporine effects on cytokine gene expression studied by reverse transcriptase-competitive polymerase chain reaction. Transplantation 1994;58:87–92.
- Uthaisangsook S, Day NK, Hitchcock R, Lerner A, James-Yarish M, Good RA et al. Negative regulation of interleukin-12 production by a rapamycin-sensitive signaling pathway: a brief communication. Exp Biol Med (Maywood) 2003;228:1023–1027.
- Hoentjen F, Sartor RB, Ozaki M, Jobin C. STAT3 regulates NF-kappaB recruitment to the IL-12p40 promoter in dendritic cells. Blood 2005;105:689–696.