Broad regulation of matrix and adhesion molecules in THP-1 human macrophages by nitroglycerin

Nitric Oxide - Biology and Chemistry

Volumn 22, Issue 1, 2010, Pages 11-17

  Krishnatry, Anu Shilpa ^a   Brazeau, Daniel A ^a   Fung, Ho Leung ^a  

^a UNIVERSITY AT BUFFALO   (United States)

Author keywords

Cell adhesion molecules; Extracellular matrix proteases; Matrix metalloproteinase 9; Microarrays; Nitroglycerin; Testican 1

Indexed keywords

ALPHA1 INTEGRIN; CELL PROTEIN; FIBRONECTIN; GELATINASE B; GLYCERYL TRINITRATE; MATRIX METALLOPROTEINASE 26; TESTICAN 1; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DNA MICROARRAY; ENZYME ACTIVATION; EXTRACELLULAR MATRIX; GENE EXPRESSION REGULATION; HUMAN; HUMAN CELL; IMMUNOREGULATION; LEUKOCYTE ADHERENCE; MACROPHAGE ACTIVATION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; REAL TIME POLYMERASE CHAIN REACTION;

BETA CATENIN; CELL ADHESION MOLECULES; CELLS, CULTURED; EXTRACELLULAR MATRIX PROTEINS; FIBRONECTINS; GENE EXPRESSION REGULATION; HUMANS; MACROPHAGES; MATRIX METALLOPROTEINASES; NITROGLYCERIN; OLIGONUCLEOTIDE ARRAY SEQUENCE ANALYSIS; PROTEOGLYCANS; RECOMBINANT PROTEINS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; THROMBOSPONDINS; VASCULAR CELL ADHESION MOLECULE-1;

EID: 73149086384     PISSN: 10898603     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.niox.2009.10.004     Document Type: Article

References (59)

1. Nitroglycerin: a blast from the past remains a trusted standby. Nitrates offer quick, effective relief from a common heart disease symptom, often for just pennies per dose. Harv. Heart Lett. 15 (2005) 3.
2. Munzel T., Wenzel P., and Daiber A. Do we still need organic nitrates?. J. Am. Coll. Cardiol. 49 (2007) 1296-1298
3. Fung H.L. Biochemical mechanism of nitroglycerin action and tolerance: is this old mystery solved?. Annu. Rev. Pharmacol. Toxicol. 44 (2004) 67-85
4. Anon. GISSI-3: effects of lisinopril and transdermal glyceryl trinitrate singly and together on 6-week mortality and ventricular function after acute myocardial infarction. Gruppo Italiano per lo Studio della Sopravvivenza nell'infarto Miocardico. Lancet 343 (1994) 1115-1122
5. Anon. ISIS-4: a randomised factorial trial assessing early oral captopril, oral mononitrate, and intravenous magnesium sulphate in 58,050 patients with suspected acute myocardial infarction. ISIS-4 (Fourth International Study of Infarct Survival) Collaborative Group. Lancet 345 (1995) 669-685
6. Nagao K., Kanmatsuse K., Ooiwa K., Satou K., Watanabe I., Yamasita M., and Kikushima K. The effects of long-acting nitrates on 5-year cardiac events of patients with coronary thrombolytic therapy for acute myocardial infarction. Int. Med. 39 (2000) 877-884
7. Yamauchi T., Hagiwara N., Kasanuki H., Koyanagi R., and Ogawa H. Long-term nitrate use in acute myocardial infarction (the Heart Institute of Japan, Department of Cardiology Nitrate Evaluation Program). Cardiovasc. Drugs Ther. 22 (2008) 177-184
8. Kanamasa K., Hayashi T., Kimura A., Ikeda A., and Ishikawa K. Long-term, continuous treatment with both oral and transdermal nitrates increases cardiac events in healed myocardial infarction patients. Angiology 53 (2002) 399-408
9. Nakamura Y., Moss A.J., Brown M.W., Kinoshita M., and Kawai C. Long-term nitrate use may be deleterious in ischemic heart disease: a study using the databases from two large-scale postinfarction studies. Multicenter Myocardial Ischemia Research Group. Am. Heart J. 138 (1999) 577-585
10. Ishikawa K., Kanamasa K., Ogawa I., Takenaka T., Naito T., Kamata N., Yamamoto T., Nakai S., Hama J., Oyaizu M., Kimura A., Yamamoto K., Aso N., Arai M., Yabushita H., and Katori Y. Long-term nitrate treatment increases cardiac events in patients with healed myocardial infarction. Secondary Prevention Group. Jpn. Circ. J. 60 (1996) 779-788
11. Ishikawa K., Yamamoto T., Kanamasa K., Hayashi T., Takenaka T., Kimura A., Miyataka M., Yabushita H., and Kitayama K. Intermittent nitrate therapy for prior myocardial infaraction does not induce rebound angina nor reduce cardiac events. Int. Med. 39 (2000) 1020-1026
12. Death A.K., Nakhla S., McGrath K.C., Martell S., Yue D.K., Jessup W., and Celermajer D.S. Nitroglycerin upregulates matrix metalloproteinase expression by human macrophages. J. Am. Coll. Cardiol. 39 (2002) 1943-1950
13. Nagase H., and Woessner Jr. J.F. Matrix metalloproteinases. J. Biol. Chem. 274 (1999) 21491-21494
14. Newby A.C. Dual role of matrix metalloproteinases (matrixins) in intimal thickening and atherosclerotic plaque rupture. Physiol. Rev. 85 (2005) 1-31
15. Chakraborti S., Mandal M., Das S., Mandal A., and Chakraborti T. Regulation of matrix metalloproteinases: an overview. Mol. Cell. Biochem. 253 (2003) 269-285
16. Ram M., Sherer Y., and Shoenfeld Y. Matrix metalloproteinase-9 and autoimmune diseases. J. Clin. Immunol. 26 (2006) 299-307
17. Lendon C.L., Davies M.J., Born G.V., and Richardson P.D. Atherosclerotic plaque caps are locally weakened when macrophages density is increased. Atherosclerosis 87 (1991) 87-90
18. Galis Z.S., Sukhova G.K., Lark M.W., and Libby P. Increased expression of matrix metalloproteinases and matrix degrading activity in vulnerable regions of human atherosclerotic plaques. J. Clin. Invest. 94 (1994) 2493-2503
19. Gough P.J., Gomez I.G., Wille P.T., and Raines E.W. Macrophage expression of active MMP-9 induces acute plaque disruption in apoE-deficient mice. J. Clin. Invest. 116 (2006) 59-69
20. Kai H., Ikeda H., Yasukawa H., Kai M., Seki Y., Kuwahara F., Ueno T., Sugi K., and Imaizumi T. Peripheral blood levels of matrix metalloproteases-2 and -9 are elevated in patients with acute coronary syndromes. J. Am. Coll. Cardiol. 32 (1998) 368-372
21. Van Wart H.E., and Birkedal-Hansen H. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl. Acad. Sci. USA 87 (1990) 5578-5582
22. Elkins P.A., Ho Y.S., Smith W.W., Janson C.A., D'Alessio K.J., McQueney M.S., Cummings M.D., and Romanic A.M. Structure of the C-terminally truncated human ProMMP9, a gelatin-binding matrix metalloproteinase. Acta Crystallogr. D Biol. Crystallogr. 58 (2002) 1182-1192
23. Tsou P.S., Addanki V., Haas J.A., Page N.A., and Fung H.L. Role of glutaredoxin-mediated protein S-glutathionylation in cellular nitroglycerin tolerance. J. Pharmacol. Exp. Ther. (2009)
24. Rival Y., Beneteau N., Chapuis V., Taillandier T., Lestienne F., Dupont-Passelaigue E., Patoiseau J.F., Colpaert F.C., and Junquero D. Cardiovascular drugs inhibit MMP-9 activity from human THP-1 macrophages. DNA Cell Biol. 23 (2004) 283-292
25. Vandesompele J., De Preter K., Pattyn F., Poppe B., Van Roy N., De Paepe A., and Speleman F. Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol. 3 (2002) Research0034.1-Research0034.11
26. Wang E.Q., Lee W.I., Brazeau D., and Fung H.L. CDNA microarray analysis of vascular gene expression after nitric oxide donor infusions in rats: implications for nitrate tolerance mechanisms. AAPS PharmSci. 4 (2002) E10
27. Excoffier L., Smouse P.E., and Quattro J.M. Analysis of molecular variance inferred from metric distances among DNA haplotypes: application to human mitochondrial DNA restriction data. Genetics 131 (1992) 479-491
28. Carpenter J., and Bithell J. Bootstrap confidence intervals: when, which, what? A practical guide for medical statisticians. Stat. Med. 19 (2000) 1141-1164
29. Zharkikh A., and Li W.H. Estimation of confidence in phylogeny: the complete-and-partial bootstrap technique. Mol. Phylogenet. Evol. 4 (1995) 44-63
30. Rekhter M. Vulnerable atherosclerotic plaque: emerging challenge for animal models. Curr. Opin. Cardiol. 17 (2002) 626-632
31. Tsuchiya S., Yamabe M., Yamaguchi Y., Kobayashi Y., Konno T., and Tada K. Establishment and characterization of a human acute monocytic leukemia cell line (THP-1). Int. J. Cancer 26 (1980) 171-176
32. Tsuchiya S., Kobayashi Y., Goto Y., Okumura H., Nakae S., Konno T., and Tada K. Induction of maturation in cultured human monocytic leukemia cells by a phorbol diester. Cancer Res. 42 (1982) 1530-1536
33. Pi X., Yan C., Kim D., Chen J., and Berk B.C. Differential expression of genes from nitrate-tolerant rat aorta. J. Vasc. Res. 39 (2002) 304-310
34. Cybulsky M.I., Iiyama K., Li H., Zhu S., Chen M., Iiyama M., Davis V., Gutierrez-Ramos J.C., Connelly P.W., and Milstone D.S. A major role for VCAM-1, but not ICAM-1, in early atherosclerosis. J. Clin. Invest. 107 (2001) 1255-1262
35. Dansky H.M., Barlow C.B., Lominska C., Sikes J.L., Kao C., Weinsaft J., Cybulsky M.I., and Smith J.D. Adhesion of monocytes to arterial endothelium and initiation of atherosclerosis are critically dependent on vascular cell adhesion molecule-1 gene dosage. Arterioscler. Thromb. Vasc. Biol. 21 (2001) 1662-1667
36. Yakubenko V.P., Lobb R.R., Plow E.F., and Ugarova T.P. Differential induction of gelatinase B (MMP-9) and gelatinase A (MMP-2) in T lymphocytes upon alpha(4)beta(1)-mediated adhesion to VCAM-1 and the CS-1 peptide of fibronectin. Exp. Cell. Res. 260 (2000) 73-84
37. Takahashi M., Tsunoda T., Seiki M., Nakamura Y., and Furukawa Y. Identification of membrane-type matrix metalloproteinase-1 as a target of the beta-catenin/Tcf4 complex in human colorectal cancers. Oncogene 21 (2002) 5861-5867
38. Nishida Y., Miyamori H., Thompson E.W., Takino T., Endo Y., and Sato H. Activation of matrix metalloproteinase-2 (MMP-2) by membrane type 1 matrix metalloproteinase through an artificial receptor for proMMP-2 generates active MMP-2. Cancer Res. 68 (2008) 9096-9104
39. Edgell C.J., BaSalamah M.A., and Marr H.S. Testican-1: a differentially expressed proteoglycan with protease inhibiting activities. Int. Rev. Cytol. 236 (2004) 101-122
40. Roll S., Seul J., Paulsson M., and Hartmann U. Testican-1 is dispensable for mouse development. Matrix Biol. (2006)
41. Bocock J.P., Edgell C.J., Marr H.S., and Erickson A.H. Human proteoglycan testican-1 inhibits the lysosomal cysteine protease cathepsin l. Eur. J. Biochem. 270 (2003) 4008-4015
42. Hausser H.J., Decking R., and Brenner R.E. Testican-1, an inhibitor of pro-MMP-2 activation, is expressed in cartilage. Osteoarthritis Cartilage 12 (2004) 870-877
43. Chen X., Su Y., Fingleton B., Acuff H., Matrisian L.M., Zent R., and Pozzi A. Increased plasma MMP9 in integrin alpha1-null mice enhances lung metastasis of colon carcinoma cells. Int. J. Cancer 116 (2005) 52-61
44. Adams J.C., and Lawler J. The thrombospondins. Int. J. Biochem. Cell. Biol. 36 (2004) 961-968
45. Irizarry R.A., Warren D., Spencer F., Kim I.F., Biswal S., Frank B.C., Gabrielson E., Garcia J.G., Geoghegan J., Germino G., Griffin C., Hilmer S.C., Hoffman E., Jedlicka A.E., Kawasaki E., Martinez-Murillo F., Morsberger L., Lee H., Petersen D., Quackenbush J., Scott A., Wilson M., Yang Y., Ye S.Q., and Yu W. Multiple-laboratory comparison of microarray platforms. Nat. Methods 2 (2005) 345-350
46. Snider J.V., Wechser M.A., and Lossos I.S. Human disease characterization: real-time quantitative PCR analysis of gene expression. Drug Discov. Today 6 (2001) 1062-1067
47. Marcet-Palacios M., Ulanova M., Duta F., Puttagunta L., Munoz S., Gibbings D., Radomski M., Cameron L., Mayers I., and Befus A.D. The transcription factor Wilms tumor 1 regulates matrix metalloproteinase-9 through a nitric oxide-mediated pathway. J. Immunol. 179 (2007) 256-265
48. Lianxu C., Hongti J., and Changlong Y. NF-kappaBp65-specific siRNA inhibits expression of genes of COX-2, NOS-2 and MMP-9 in rat IL-1beta-induced and TNF-alpha-induced chondrocytes. Osteoarthritis Cartilage 14 (2006) 367-376
49. Knipp B.S., Ailawadi G., Ford J.W., Peterson D.A., Eagleton M.J., Roelofs K.J., Hannawa K.K., Deogracias M.P., Ji B., Logsdon C., Graziano K.D., Simeone D.M., Thompson R.W., Henke P.K., Stanley J.C., and Upchurch Jr. G.R. Increased MMP-9 expression and activity by aortic smooth muscle cells after nitric oxide synthase inhibition is associated with increased nuclear factor-kappaB and activator protein-1 activity. J. Surg. Res. 116 (2004) 70-80
50. Kang J.L., Lee K., and Castranova V. Nitric oxide up-regulates DNA-binding activity of nuclear factor-kappaB in macrophages stimulated with silica and inflammatory stimulants. Mol. Cell. Biochem. 215 (2000) 1-9
51. Ho T.Y., and Bagnell C.A. Relaxin induces matrix metalloproteinase-9 through activation of nuclear factor kappa B in human THP-1 cells. Ann. NY Acad. Sci. 1041 (2005) 314-316
52. Kim G.M., Jin K.S., and Chung C.S. Differential effects of corticosteroids on the expression of cyclooxygenase-2, tumour necrosis factor-alpha and matrix metalloproteinase-9 in an animal model of migraine. Cephalalgia 28 (2008) 1179-1187
53. Gu Z., Kaul M., Yan B., Kridel S.J., Cui J., Strongin A., Smith J.W., Liddington R.C., and Lipton S.A. S-nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death. Science 297 (2002) 1186-1190
54. Okamoto T., Akaike T., Sawa T., Miyamoto Y., van der Vliet A., and Maeda H. Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation. J. Biol. Chem 276 (2001) 29596-29602
55. Zaki M.H., Fujii S., Okamoto T., Islam S., Khan S., Ahmed K.A., Sawa T., and Akaike T. Cytoprotective function of heme oxygenase 1 induced by a nitrated cyclic nucleotide formed during murine salmonellosis. J. Immunol. 182 (2009) 3746-3756
56. Sawa T., Zaki M.H., Okamoto T., Akuta T., Tokutomi Y., Kim-Mitsuyama S., Ihara H., Kobayashi A., Yamamoto M., Fujii S., Arimoto H., and Akaike T. Protein S-guanylation by the biological signal 8-nitroguanosine 3′,5′-cyclic monophosphate. Nat. Chem. Biol. 3 (2007) 727-735
57. McCarthy S.M., Bove P.F., Matthews D.E., Akaike T., and van der Vliet A. Nitric oxide regulation of MMP-9 activation and its relationship to modifications of the cysteine switch. Biochemistry 47 (2008) 5832-5840
58. Ridnour L.A., Windhausen A.N., Isenberg J.S., Yeung N., Thomas D.D., Vitek M.P., Roberts D.D., and Wink D.A. Nitric oxide regulates matrix metalloproteinase-9 activity by guanylyl-cyclase-dependent and -independent pathways. Proc. Natl. Acad. Sci. USA 104 (2007) 16898-16903
59. Umansky V., Hehner S.P., Dumont A., Hofmann T.G., Schirrmacher V., Droge W., and Schmitz M.L. Co-stimulatory effect of nitric oxide on endothelial NF-kappaB implies a physiological self-amplifying mechanism. Eur. J. Immunol. 28 (1998) 2276-2282