Table.1 Genes Differentially Expressed in Hepg2-TIP30R106H And

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Table.1 Genes Differentially Expressed in Hepg2-TIP30R106H And Table.1 Genes differentially expressed in HepG2-TIP30R106H and HepG2-TIP30 ----------------------------------------------------------------------------------------------------------------------------------------------------------------- Gene Locus Accession Function Fold change -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Fifty-one genes up-regulated in HepG2-TIP30R106H Insulin-like growth factor binding protein 1 (IGFBP-1)(1) 7p13-p12 NM_000596 cell proliferation/ growth 30.0 Insulin-like growth factor binding protein 3(1) 7p13-p12 NM_000598 growth factor stabilizer 29.86 RGC32 protein 13q13.3 AF036549 regulation of CDK activity 14.93 Chondroitin sulfate proteoglycan 2 (CSPG2) 15q14.3 AF072892 cell proliferation & differentiation 6.96 S100 calcium-binding protein A4 (S100A4)(2) 1q21 NM_001961.2 metastasis 4.29 Cysteine-rich, angiogenic inducer, 61 (Cyr61; IGFBP10; CCN1)(3) 1p31.p22 NM_001554 cell proliferation & angiogenesis 4.0 Protein kinase-related oncogene (PIM1)(4) 6p21.2 BC001271 signal transduction 3.25 Histamine N-methyltransferase (HNMT) 2q22.1 NM_006895 acyltransferase, metabolism 3.25 CD 24 signal transducer 6q21 NM_013230 immune response 3.03 guanine nucleotide exchange factors for Rap; M-Ras-regulated GEF 7p15.3 NM_012294 signal transduction 2.83 matrix metalloproteinase 3 (MMP3)(5) 11q22.3 NM_002422 promote invasion and metastasis 2.64 acylphosphatase 1, erythrocyte (common) type (ACYP1) 14q24.3 XM_352906 acylphosphatase activity 2.64 Arginase II 14q24.1-q24.3 NM_001172 metabolism 2.64 Jagged 1 (HJ1; JAG1) 20p12.1-p11.3 NM_000214 signal transduction/angiogenesis 2.64 Annexin II 15q21-q22 NM_004039.1 fibrin homeostasis/neoangiogenesis 2.64 Methylthioadenosine phosphorylase (MTAP) 9p22-p21 NM_002451 polyamine metabolism 2.64 Immediate early response gene 3 (IER3; IEX1) 6p21.3 NM_003897 apoptosis 2.46 Dual specificity phosphatase 1 (DUSP1) 5q34 NM_004417 signal transduction 2.46 Ectonucleotide pyrophosphatase/phosphodiesterase 1(ENPP1) 6q22-q23 NM_006208.1 metabolism 2.46 Core 1 UDP-galactose:N-acetylgalactosamine-alpha-R beta 1,3- 7p14-p13 NM_020156.1 transferase activity 2.46 galactosyltransferase (C1GALT1) Insulin receptor substrate-1 (IRS-1) 2q36 NM_005544 signal transduction 2.30 LIS1-interacting protein NUDE1 16p13.11 NM_017668 mitosis 2.30 Tumor necrosis factor, alpha-induced protein (GG2-1) 5q23.1 NM_14350 anti-apoptosis 2.30 Annexin 2 (ANAX2) 15q21-q22 AK092006 calcium metabolism 2.30 CHST6 (carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 6) 16q22 NM_021615.2 transferase activity 2.30 N-cadherin (CDH2) (6) 18q11.2-q12.2 NM_001792 cell adhesion 2.30 procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), 10q21.3-q23.1 NM_000917 posttranslation 2.30 alpha polypeptide I (P4HA1) mucosa associated lymphoid tissue lymphoma translocation gene1 (MALT1) 18q21 NM_006785 apoptosis 2.14 Wee1 11p15.3 NM_003390 cell cycle, mitosis 2.0 thymosin, beta 10 (TMSB10) (7) 2p11.2 NM_021103 cytoskeleton 1.87 protein phosphatase 1, regulatory (inhibitor) subunit 2 (PPP1R2) 3q29 NM_006241 inhibitor subunit of PP1 1.87 interferon induced transmembrane protein 2 (1-8D) (IFITM2) 11p15.5 NM_006435 immune response 1.87 c-syn protooncogene (FYN) (8) 6q21 NM_002037 cell growth 1.87 epithelial V-like antigen 1 (EVA1) (9) 11q24 NM_005795 cell adhesion 1.87 CD24 antigen (small cell lung carcinoma cluster 4 antigen) 6q21 NM_013230 signal transduction 1.87 Crk-associated substrate -related protein Cas-L (pp105) 17p12 XM_225245 signal transduction 1.87 nuclear factor, interleukin 3 regulated (NFIL3) 9q22 NM_005384 transcription/antiapoptosis 1.87 Cell division cycle 2, G1 to S and G2 to M (CDC2) 10q21.1 NM_001786 cell cycle 1.87 serine/threonine protein kinase MASK (MST4) Xq26.2 NM_016542 cell death/ apoptosis 1.74 AXL receptor tyrosine kinase (10) 19q13.1 NM_021913 signal transduction 1.74 B-cell CLL/lymphoma 6 (zinc finger protein 51) (BCL6) 3q27 NM_001706 transcription 1.74 RAD17 homolog (S. pombe) 5q12-q13.1 NM_133338 cell cycle 1.74 Member RAS oncogene family (RAB1) 2p14 NM_004161 signal transduction 1.74 Peroxisome proliferative activated receptor, gamma, coactivator 1 5q33.1 NM_133263 transcription 1.74 Integrin, alpha 6 (ITGA6)(11) 2q22-q31 NM_000210 metastasis 1.74 Laminin beta-1 chain precursor (LAMB1) 7q22.1 NM_002291 attachment & migration 1.74 Highly expressed in cancer, rich in leucine heptad repeats (HEC) 18p11.31 NM_006101 mitosis 1.74 Pituitary tumor-transforming gene 1(PTTG1)(12) 5q35.1 NM_004219 angiogenesis/mitogenesis 1.74 Meningioma expressed antigen 5 (MGEA5) 10q24.1-q24.3NM_012215 enzyme 1.74 Proteasome (prosome, macropain) 26S subunit, ATPase, 6 (PSMC6) 14q22.1 NM_002806 protein degradation 1.74 Signal transducing adaptor molecule (SH3 domain and ITAM motif) 1 10p14-p13 NM-005843 signal transduction 1.74 Twenty-five genes down-regulated in HepG2-TIP30R106H Cell division control protein, septin D1 (septin 9) (13) 17q25.3 NM_006640 cell cycle -1.74 Cathepsin D (lysosomal aspartyl protease (CTSD) 11p15.5 NM_001909 metastasis -1.74 A kinase (PRKA) anchor protein 1 (SAKAP84) 17q21-q23 NM_003488 signal transduction -1.74 Pre-mRNA splicing factor (PRP16) 16q21-q22.3 NM_014003 RNA splicing -1.74 Bladder cancer associated protein (BLCAP) 20q11.2-q12 NM_006698 unknown -1.74 Glucocorticoid receptor DNA binding factor 1(GRLF1) 19q13.3 NM_024342 nuclear receptor -1.74 Coagulation factor VIII-associated (intronic transcript) (F8A) Xq28 NM_012151 unknown -1.74 Tumour Protein P53 (TP53) 17p13.1 NM_000546 transcription -1.74 Protein tyrosine phosphatase, non-receptor type substrate 1 (PTPNS1) 20p13 NM_080792 signal transduction -1.87 prostatic binding protein (PBP; RKIP) 12q24.23 NM_002567 metastasis suppressor -1.87 RNA binding protein; AT-rich element binding factor (SPM300; SRRM2) 16p13.3 NM_016333 RNA splicing -1.87 Argininosuccinate synthetase (ASS) 9q34.13 NM_054012 enzyme -1.87 Non-lens member of the beta-gamma crystalline like protein (AIM1)(14) 6q21 NM_016180 mitosis -1.87 MYC-associated zinc finger protein (purine-binding transcription factor) 16p11.2 NM_002383 transcription -2.0 Fibroblast growth factor receptor 4 (FGFR4) 5q35.3 NM_002011 signal growth factor -2.0 Claudin 6 (CLDN6) 16p13.3 NM_021195.2 adhesion -2.0 ladinin 1 (LAD1) 1q35.1-q32.3 NM_005558 cell organization -2.0 Zyxin (ZYX) 7q32 NM_003461 cell sion -2.14 Chromobox homolog 4 (Pc class homolog, Drosophila) (CBX4) 17q25.3 NM_003655 repressor of proto-oncognes -2.30 Cell death-inducing DFFA-like effector b (CIDEB) 14q11.2 NM_014430.1 apoptosis -2.30 Calreticulin (CALR) 19p13.3-p13.2 NM_004343 calcium ion binding -2.64 Talin (TLN) 9p13 NM_011602 cell adhesion / mobility -2.64 Zinc finger protein 144 (Mel-18) (ZNF144) (PCGF2)(15) 17q21.2 NM_007144 transcription -3.0 Rho GDP dissociation inhibitor (GDI) alpha 17q25.3 NM_004309 signal transduction -3.5 Insulin-like growth factor 2 (somatomedin A) (IGF2) 11p15.5 NM_000612 growth factor -5.66 -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- References: 1. D. E. Hansel et al., Clin Cancer Res 10, 6152 (Sep 15, 2004). 2. E. J. Kim, D. M. Helfman, J Biol Chem 278, 30063 (Aug 8, 2003). 3. J. A. Menendez, I. Mehmi, D. W. Griggs, R. Lupu, Endocr Relat Cancer 10, 141 (Jun, 2003). 4. M. van Lohuizen et al., cell 56, 673 (Feb 24, 1989). 5. J. Mercapide, R. Lopez De Cicco, J. S. Castresana, A. J. Klein-Szanto, Int J Cancer 106, 676 (Sep 20, 2003). 6. R. B. Hazan, R. Qiao, R. Keren, I. Badano, K. Suyama, Ann N Y Acad Sci 1014, 155 (Apr, 2004). 7. G. Chiappetta et al., Oncol Rep 12, 239 (Aug, 2004). 8. K. Semba et al., Proc Natl Acad Sci U S A 83, 5459 (Aug, 1986). 9. M. Guttinger et al., J Cell Biol 141, 1061 (May 18, 1998). 10. J. P. O'Bryan et al., Mol Cell Biol 11, 5016 (Oct, 1991). 11. S. J. Leu et al., J Biol Chem 278, 33801 (Sep 5, 2003). 12. X. Zhang et al., Mol Endocrinol 13, 156 (Jan, 1999). 13. S. E. Russell et al., Cancer Res 60, 4729 (Sep 1, 2000). 14. M. E. Ray, G. Wistow, Y. A. Su, P. S. Meltzer, J. M. Trent, Proc Natl Acad Sci U S A 94, 3229 (Apr 1, 1997). 15. F. Matsuo et al., Breast Cancer 9, 33 (2002). .
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