Platelet-activating factor overturns the transcriptional repressor disposition of Sp1 in the expression of MMP-9 in human corneal epithelial cells

Investigative Ophthalmology and Visual Science

Volumn 48, Issue 5, 2007, Pages 1931-1941

  Taheri, Faramarz ^a   Bazan, Haydee E P ^a  

^a LOUISIANA STATE UNIVERSITY HEALTH SCIENCES CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; GELATINASE B; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 3; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR SP1; FLAVONOID; MAP2K1 PROTEIN, HUMAN; MAP2K2 PROTEIN, HUMAN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE KINASE 2; NF KAPPA B KINASE; NF-KAPPA B KINASE; PROTEIN KINASE (CALCIUM,CALMODULIN); PROTEIN SERINE THREONINE KINASE; REPRESSOR PROTEIN; THROMBOCYTE ACTIVATING FACTOR; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; CORNEA EPITHELIUM; DNA BINDING; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME LINKED IMMUNOSORBENT ASSAY; ENZYME PHOSPHORYLATION; EPITHELIUM CELL; GEL MOBILITY SHIFT ASSAY; GENE DELETION; GENE EXPRESSION; HUMAN; HUMAN CELL; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN MOTIF; TRANSCRIPTION REGULATION; UPREGULATION; WESTERN BLOTTING; ZYMOGRAPHY; CELL LINE; DRUG ANTAGONISM; DRUG EFFECT; ENZYMOLOGY; GENE EXPRESSION REGULATION; GENETIC TRANSFECTION; GENETICS; METABOLISM; PHOSPHORYLATION; PLASMID;

BLOTTING, WESTERN; CA(2+)-CALMODULIN DEPENDENT PROTEIN KINASE; CELL LINE; ELECTROPHORETIC MOBILITY SHIFT ASSAY; ENZYME-LINKED IMMUNOSORBENT ASSAY; EPITHELIUM, CORNEAL; FLAVONOIDS; GENE EXPRESSION REGULATION, ENZYMOLOGIC; HUMANS; MAP KINASE KINASE 1; MAP KINASE KINASE 2; MATRIX METALLOPROTEINASE 9; MITOGEN-ACTIVATED PROTEIN KINASE 1; MITOGEN-ACTIVATED PROTEIN KINASE 3; PHOSPHORYLATION; PLASMIDS; PLATELET ACTIVATING FACTOR; PROTEIN-SERINE-THREONINE KINASES; REPRESSOR PROTEINS; SP1 TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR AP-1; TRANSFECTION;

EID: 34250219975     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: 10.1167/iovs.06-1008     Document Type: Article

References (62)

1. Bazan HE. Cellular and molecular events in corneal wound healing: significance of lipid signalling. Exp Eye Res. 2005;80:453-463.
2. Woessner JF Jr. MMPs and TIMPs - an historical perspective. Mol Biotechnol. 2002;22:33-49.
3. Turpeenniemi-Hujanen T. Gelatinases (MMP-2 and -9) and their natural inhibitors as prognostic indicators in solid cancers. Biochimie (Paris). 2005;87:287-297.
4. Chakraborti S, Mandal M, Das S, et al. Regulation of matrix metalloproteinases: an overview. Mol Cell Biochem. 2003;253: 269-285.
5. Nagase H, Woessner JF Jr. Matrix metalloproteinases. J Biol Chem. 1999;274:21491-21494.
6. Vu TH. Don't mess with the matrix. Nat Genet. 2001;28:202-203.
7. Massova I, Kotra LP, Fridman R, Mobashery S. Matrix metalloproteinases: structures, evolution, and diversification. FASEB J. 1998;12:1075-1095.
8. Vu TH, Werb Z. Matrix metalloproteinases: effectors of development and normal physiology. Genes Dev. 2000;14:2123-2133.
9. Sivak JM, Mohan R, Rinehart WB, et al. Pax-6 expression and activity are induced in the reepithelializing cornea and control activity of the transcriptional promoter for matrix metalloproteinase gelatinase B. Dev Biol. 2000;222:41-54.
10. Matsubara M, Zieske JD, Fini ME. Mechanism of basement membrane dissolution preceding corneal ulceration. Invest Ophthalmol Vis Sci. 1991;32:3221-3237.
11. Matsubara M, Girard MT, Kublin CL, et al. Differential roles for two gelatinolytic enzymes of the matrix metalloproteinase family in the remodelling cornea. Dev Biol. 1991;147:425-439.
12. Leppert D, Waubant E, Galardy R, et al. T cell gelatinases mediate basement membrane transmigration in vitro. J Immunol. 1995; 154:4379-4389.
13. Okada S, Kita H, George TJ, et al. Migration of eosinophils through basement membrane components in vitro: role of matrix metalloproteinase-9. Am J Respir Cell Mol Biol. 1997;17:519-528.
14. Fini ME, Parks WC, Rinehart WB, et al. Role of matrix metalloproteinases in failure to re-epithelialize after corneal injury. Am J Pathol. 1996;149:1287-1302.
15. Gay JC. Mechanism and regulation of neutrophil priming by platelet-activating factor. J Cell Physiol. 1993;156:189-197.
16. Shukla SD. Platelet-activating factor receptor and signal transduction mechanisms. FASEB J. 1992;6:2296-2301.
17. Buttke TM, Sandstrom PA. Redox regulation of programmed cell death in lymphocytes. Free Radic Res. 1995;22:389-397.
18. Braquet P, Touqui L, Shen TY, Vargaftig BB. Perspectives in platelet-activating factor research. Pharmacol Rev. 1987;39:97-145.
19. Bazan HE, Reddy ST, Lin N. Platelet-activating factor (PAF) accumulation correlates with injury in the cornea. Exp Eye Res. 1991; 52:481-491.
20. Chandrasekher G, Ma X, Lallier TE, Bazan HE. Delay of corneal epithelial wound healing and induction of keratocyte apoptosis by platelet-activating factor. Invest Ophthalmol Vis Sci. 2002;43: 1422-1428.
21. Tao Y, Bazan HE, Bazan NG. Platelet-activating factor induces the expression of metalloproteinases-1 and -9, but not -2 or -3, in the corneal epithelium. Invest Ophthalmol Vis Sci. 1995;36:345-354.
22. Ottino P, Bazan HE. Corneal stimulation of MMP-1, -9 and uPA by platelet-activating factor is mediated by cyclooxygenase-2 metabolites. Curr Eye Res. 2001;23:77-85.
23. Ottino P, Taheri F, Bazan HE. Platelet-activating factor induces the gene expression of TIMP-1, -2, and PAI-1: imbalance between the gene expression of MMP-9 and TIMP-1 and -2. Exp Eye Res. 2002;74:393-402.
24. Huhtala P, Tuuttila A, Chow LT, et al. Complete structure of the human gene for 92-kDa type IV collagenase: divergent regulation of expression for the 92- and 72-kilodalton enzyme genes in HT-1080 cells. J Biol Chem. 1991;266:16485-16490.
25. Sato H, Seiki M. Regulatory mechanism of 92 kDa type IV collagenase gene expression which is associated with invasiveness of tumor cells. Oncogene. 1993;8:395-405.
26. Sato H, Kita M, Seiki M. v-Src activates the expression of 92-kDa type IV collagenase gene through the AP-1 site and the GT box homologous to retinoblastoma control elements: a mechanism regulating gene expression independent of that by inflammatory cytokines. J Biol Chem. 1993;268:23460-23468.
27. Bazan HE, Varner L. A mitogen-activated protein kinase (MAP-kinase) cascade is stimulated by platelet activating factor (PAF) in corneal epithelium. Curr Eye Res. 1997;16:372-379.
28. Gum R, Lengyel E, Juarez J, et al. Stimulation of 92-kDa gelatinase B promoter activity by ras is mitogen-activated protein kinase kinase 1-independent and requires multiple transcription factor binding sites including closely spaced PEA3/ets and AP-1 sequences. J Biol Chem. 1996;271:10672-10680.
29. Himelstein BP, Lee EJ, Sato H, et al. Transcriptional activation of the matrix metalloproteinase-9 gene in an H-ras and v-myc transformed rat embryo cell line. Oncogene. 1997;14:1995-1998.
30. Yan C, Wang H, Boyd DD. KiSS-1 represses 92-kDa type IV collagenase expression by down-regulating NF-κB binding to the promoter as a consequence of IκBα-induced block of p65/p50 nuclear translocation. J Biol Chem. 2001;276:1164-1172.
31. Crowe DL, Brown TN. Transcriptional inhibition of matrix metalloproteinase 9 (MMP-9) activity by a c-fos/estrogen receptor fusion protein is mediated by the proximal AP-1 site of the MMP-9 promoter and correlates with reduced tumor cell invasion. Neoplasia. 1999;1:368-372.
32. Bond M, Fabunmi RP, Baker AH, Newby AC. Synergistic upregulation of metalloproteinase-9 by growth factors and inflammatory cytokines: an absolute requirement for transcription factor NF-κB. FEBS Lett. 1998;435:29-34.
33. Esteve PO, Chicoine E, Robledo O, et al. Protein kinase C-zeta regulates transcription of the matrix metalloproteinase-9 gene induced by IL-1 and TNF-alpha in glioma cells via NF-kappa B. J Biol Chem. 2002;277:35150-35155.
34. Sivak JM, West-Mays JA, Yee A, et al. Transcription factors Pax6 and AP-2α interact to coordinate corneal epithelial repair by controlling expression of matrix metalloproteinase gelatinase B. Mol Cell Biol. 2004;24:245-257.
35. Philipsen S, Suske G. A tale of three fingers: the family of mammalian Sp/XKLF transcription factors. Nucleic Acids Res. 1999;27: 2991-3000.
36. Kaczynski J, Cook T, Urrutia R. Sp1- and Kruppel-like transcription factors. Genome Biol. 2003;4:206.
37. Bouwman P, Philipsen S. Regulation of the activity of Sp1-related transcription factors. Mol Cell Endocrinol. 2002;195:27-38.
38. Lin SY, Black AR, Kostic D, et al. Cell cycle-regulated association of E2F1 and Sp1 is related to their functional interaction. Mol Cell Biol. 1996;16:1668-1675.
39. Lee DK, Suh D, Edenberg HJ, Hur MW. POZ domain transcription factor, FBI-1, represses transcription of ADH5/FDH by interacting with the zinc finger and interfering with DNA binding activity of Sp1. J Biol Chem. 2002;277:26761-26768.
40. Doetzlhofer A, Rotheneder H, Lagger G, et al. Histone deacetylase 1 can repress transcription by binding to Sp1. Mol Cell Biol. 1999;19:5504-5511.
41. Zaid A, Hodny Z, Li R, Nelson BD. Sp1 acts as a repressor of the human adenine nucleotide translocase-2 (ANT2) promoter. Eur J Biochem. 2001;268:5497-5503.
42. Ogra Y, Suzuki K, Gong P, et al. Negative regulatory role of Sp1 in metal responsive element-mediated transcriptional activation. J Biol Chem. 2001;276:16534-16539.
43. Li L, He S, Sun JM, Davie JR. Gene regulation by Sp1 and Sp3. Biochem Cell Biol. 2004;82:460-471.
44. Briggs MR, Kadonaga JT, Bell SP, Tjian R. Purification and biochemical characterization of the promoter-specific transcription factor, Sp1. Science. 1986;234:47-52.
45. Lomberk G, Urrutia R. The family feud: turning off Sp1 by Sp1-like KLF proteins. Biochem J. 2005;392:1-11.
46. Kadonaga JT, Carner KR, Masiarz FR, Tjian R. Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain. Cell. 1987;51:1079-1090.
47. Suzuki T, Kimura A, Nagai R, Horikoshi M. Regulation of interaction of the acetyltransferase region of p300 and the DNA-binding domain of Sp1 on and through DNA binding. Genes Cells. 2000; 5:29-41.
48. Hagen G, Muller S, Beato M, Suske G. Sp1-mediated transcriptional activation is repressed by Sp3. EMBO J. 1994;13:3843-3851.
49. Dennig J, Hagen G, Beato M, Suske G. Members of the Sp transcription factor family control transcription from the uteroglobin promoter. J Biol Chem. 1995;270:12737-12744.
50. Kwon HS, Kim MS, Edenberg HJ, Hur MW. Sp3 and Sp4 can repress transcription by competing with Sp1 for the core cis-elements on the human ADH5/FDH minimal promoter. J Biol Chem. 1999;274:20-28.
51. Shou Y, Baron S, Poncz M. An Sp1-binding silencer element is a critical negative regulator of the megakaryocyte-specific αIIb gene. J Biol Chem. 1998;273:5716-5726.
52. Murata Y, Kim HG, Rogers KT, et al. Negative regulation of Sp1 trans-activation is correlated with the binding of cellular proteins to the amino terminus of the Sp1 trans-activation domain. J Biol Chem. 1994;269:20674-20681.
53. Huynh KD, Fischle W, Verdin E, Bardwell VJ. BCoR, a novel corepressor involved in BCL-6 repression. Genes Dev. 2000;14: 1810-1823.
54. Chen JD, Evans RM. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature. 1995;377:454-457.
55. Zamir I, Dawson J, Lavinsky RM, et al. Cloning and characterization of a corepressor and potential component of the nuclear hormone receptor repression complex. Proc Natl Acad Sci USA. 1997;94: 14400-14405.
56. Lee JA, Suh DC, Kang JE, et al. Transcriptional activity of Sp1 is regulated by molecular interactions between the zinc finger DNA binding domain and the inhibitory domain with corepressors, and this interaction is modulated by MEK. J Biol Chem. 2005;280: 28061-28071.
57. Milanini J, Vinals F, Pouyssegur J, Pages G. p42/p44 MAP kinase module plays a key role in the transcriptional regulation of the vascular endothelial growth factor gene in fibroblasts. J Biol Chem. 1998;273:18165-18172.
58. Merchant JL, Du M, Todisco A. Sp1 phosphorylation by Erk 2 stimulates DNA binding. Biochem Biophys Res Commun. 1999; 254:454-461.
59. Milanini-Mongiat J, Pouyssegur J, Pages G. Identification of two Sp1 phosphorylation sites for p42/p44 mitogen-activated protein kinases: their implication in vascular endothelial growth factor gene transcription. J Biol Chem. 2002;277:20631-20639.
60. Turner J, Crossley M. Mammalian Kruppel-like transcription factors: more than just a pretty finger. Trends Biochem Sci. 1999; 24:236-240.
61. Black AR, Black JD, Azizkhan-Clifford J. Sp1 and Kruppel-like factor family of transcription factors in cell growth regulation and cancer. J Cell Physiol. 2001;188:143-160.
62. Cook T, Gebelein B, Urrutia R. Sp1 and its likes: biochemical and functional predictions for a growing family of zinc finger transcription factors. Ann NY Acad Sci. 1999;880:94-102.