Skip to main content Accessibility help
×
Hostname: page-component-586b7cd67f-2plfb Total loading time: 0 Render date: 2024-11-26T10:31:16.443Z Has data issue: false hasContentIssue false

26 - Inflammation in Cardiovascular Diseases

from PART V - INFLAMMATORY DISEASES/HISTOLOGY

Published online by Cambridge University Press:  05 April 2014

Kenneth K. Wu
Affiliation:
University of Texas Health Science Center
Charles N. Serhan
Affiliation:
Harvard Medical School
Peter A. Ward
Affiliation:
University of Michigan, Ann Arbor
Derek W. Gilroy
Affiliation:
University College London
Get access

Summary

INTRODUCTION

Inflammation has emerged as a key pathophysiological event in vascular diseases and the consequent cardiac and cerebral ischemic injury. There is ample evidence that inflammation is intimately involved in atherosclerosis. It mediates the initiation of atherosclerosis, promotes progression of the atherosclerotic lesions, and regulates atheromatous plaque stability [1, 2]. There is also good evidence that inflammation plays a crucial role in ischemia-reperfusion cardiac and cerebral injury [3, 4].

Inflammation is a complex process involving multiple cellular and molecular components. It is triggered by diverse proinflammatory mediators (PIM) which are generated directly and indirectly by microbial invasion, endotoxins, immune complexes, and cytokines. Vascular endothelium is subjected to pro inflammatory insults, as it is in constant contact with circulating blood and along with it many environmental stressful factors. Fortunately, endothelium is endowed with potent anti-inflammatory molecules that confer resistance to damage by transient proinflammatory attacks. Once the insulting factors dissipate, endothelial cells return to its basal state. The mechanisms by which endothelial cells resist insults are likely to be very complex. One model is stress-coupled induction of anti-inflammatory and cytoprotective genes [5]. This mechanism allows for timely defense against transient insults. However, when insults by PIMs become persistent, this protective property wears out resulting in endothelial cell damage and functional defects and eventually endothelial apoptosis and necrosis.

Type
Chapter
Information
Publisher: Cambridge University Press
Print publication year: 2010

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

1. Ross, R.A., Monteith, P.R., and McAdam, J.G. 1993. Case report: polymorphous haemangioendothelioma, a rare cause of persistent lymphadenopathy. J R Nav Med Serv 79:80–82.Google ScholarPubMed
2. Libby, P. 2002. Inflammation in atherosclerosis. Nature 420:868–874.CrossRefGoogle ScholarPubMed
3. Frangogiannis, N.G., Smith, C.W., and Entman, M.L. 2002. The inflammatory response in myocardial infarction. Cardiovasc Res 53:31–47.CrossRefGoogle ScholarPubMed
4. del Zoppo., G., Ginis, I., Hallenbeck, J.M., Iadecola, C., Wang, X., and Feuerstein, G.Z. 2000. Inflammation and stroke: putative role for cytokines, adhesion molecules and iNOS in brain response to ischemia. Brain Pathol 10:95–112.Google ScholarPubMed
5. Wu, K.K. 1998. Injury-coupled induction of endothelial eNOS and COX-2 genes: a paradigm for thromboresistant gene therapy. Proc Assoc Am Physicians 110:163–170.Google ScholarPubMed
6. Dittman, W.A., and Majerus, P.W. 1990. Structure and function of thrombomodulin: a natural anticoagulant. Blood 75:329–336.Google ScholarPubMed
7. Sadler, J.E. 1997. Thrombomodulin structure and function. Thromb Haemost 78:392–395.Google ScholarPubMed
8. Esmon, C.T. 1995. Thrombomodulin as a model of molecular mechanisms that modulate protease specificity and function at the vessel surface. FASEB J 9:946–955.CrossRefGoogle ScholarPubMed
9. Wu, K.K., and Liou, J.Y. 2005. Cellular and molecular biology of prostacyclin synthase. Biochem Biophys Res Commun 338:45–52.CrossRefGoogle ScholarPubMed
10. Smith, W.L., Garavito, R.M., and DeWitt, D.L. 1996. Prostaglandin endoperoxide H synthases (cyclooxygenases)-1 and -2. J Biol Chem 271:33157–33160.CrossRefGoogle ScholarPubMed
11. McAdam, B.F., Catella-Lawson, F., Mardini, I.A., Kapoor, S., Lawson, J.A., and FitzGerald, G.A. 1999. Systemic biosynthesis of prostacyclin by cyclooxygenase (COX)-2: the human pharmacology of a selective inhibitor of COX-2. Proc Natl Acad Sci USA 96:272–277.CrossRefGoogle ScholarPubMed
12. Belton, O., Byrne, D., Kearney, D., Leahy, A., and Fitzgerald, D.J. 2000. Cyclooxygenase-1 and -2-dependent prostacyclin formation in patients with atherosclerosis. Circulation 102:840–845.CrossRefGoogle ScholarPubMed
13. Liou, J.Y., Lee, S., Ghelani, D., Matijevic-Aleksic, N., and Wu, K.K. 2006. Protection of endothelial survival by peroxisome proliferator-activated receptor-delta mediated 14–3–3 upregulation. Arterioscler Thromb Vasc Biol 26:1481–1487.CrossRefGoogle ScholarPubMed
14. Liou, J.Y., Ghelani, D., Yeh, S., and Wu, K.K. 2007. Nonsteroidal anti-inflammatory drugs induce colorectal cancer cell apoptosis by suppressing 14–3–3epsilon. Cancer Res 67:3185–3191.CrossRefGoogle ScholarPubMed
15. Liou, J.Y., Ellent, D.P., Lee, S., et al. 2007. Cyclooxygenase-2-derived prostaglandin e2 protects mouse embryonic stem cells from apoptosis. Stem Cells 25:1096–1103.CrossRefGoogle ScholarPubMed
16. Herschman, H.R. 1996. Prostaglandin synthase 2. Biochim Biophys Acta 1299:125–140.Google ScholarPubMed
17. Wu, K.K. 1995. Inducible cyclooxygenase and nitric oxide synthase. Adv Pharmacol 33:179–207.Google ScholarPubMed
18. Wu, K.K., Liou, J.Y., and Cieslik, K. 2005. Transcriptional Control of COX-2 via C/EBPbeta. Arterioscler Thromb Vasc Biol 25:679–685.CrossRefGoogle ScholarPubMed
19. Schroer, K., Zhu, Y., Saunders, M.A., et al. 2002. Obligatory role of cyclic adenosine monophosphate response element in cyclooxygenase-2 promoter induction and feedback regulation by inflammatory mediators. Circulation 105:2760–2765.CrossRefGoogle ScholarPubMed
20. Saunders, M.A., Sansores-Garcia, L., Gilroy, D.W., and Wu, K.K. 2001. Selective suppression of CCAAT/enhancer-binding protein beta binding and cyclooxygenase-2 promoter activity by sodium salicylate in quiescent human fibroblasts. J Biol Chem 276:18897–18904.CrossRefGoogle ScholarPubMed
21. Zhu, Y., Saunders, M.A., Yeh, H., Deng, W.G., and Wu, K.K. 2002. Dynamic regulation of cyclooxygenase-2 promoter activity by isoforms of CCAAT/enhancer-binding proteins. J Biol Chem 277:6923–6928.CrossRefGoogle ScholarPubMed
22. Tazawa, R., Xu, X.M., Wu, K.K., and Wang, L.H. 1994. Characterization of the genomic structure, chromosomal location and promoter of human prostaglandin H synthase-2 gene. Biochem Biophys Res Commun 203:190–199.CrossRefGoogle ScholarPubMed
23. Deng, W.G., Zhu, Y., and Wu, K.K. 2003. Up-regulation of p300 binding and p50 acetylation in tumor necrosis factor-alpha-induced cyclooxygenase-2 promoter activation. J Biol Chem 278:4770–4777.CrossRefGoogle ScholarPubMed
24. Deng, W.G., Zhu, Y., and Wu, K.K. 2004. Role of p300 and PCAF in regulating cyclooxygenase-2 promoter activation by inflammatory mediators. Blood 103:2135–2142.CrossRefGoogle ScholarPubMed
25. Rockwell, P., Yuan, H., Magnusson, R., Figueiredo-Pereira, M. E. 2000. Proteasome inhibition in neuronal cells induces a proinflammatory response manifested by upregulation of cyclooxygenase-2, its accumulation as ubiquitin conjugates, and production of the prostaglan-din PGE(2). Arch Biochem Biophys 374:325–333.CrossRefGoogle Scholar
26. Mbonye, U.R., Wada, M., Rieke, C.J., Tang, H.Y., Dewitt, D.L., and Smith, W.L. 2006. The 19-amino acid cassette of cyclooxygenase-2 mediates entry of the protein into the endoplasmic reticulum-associated degradation system. J Biol Chem 281:35770–35778.CrossRefGoogle ScholarPubMed
27. Moore, K.L., Andreoli, S.P., Esmon, N.L., Esmon, C.T., and Bang, N.U. 1987. Endotoxin enhances tissue factor and suppresses thrombomodulin expression of human vascular endothelium in vitro. J Clin Invest 79:124–130.CrossRefGoogle ScholarPubMed
28. Ishii, H., and Majerus, P.W. 1985. Thrombomodulin is present in human plasma and urine. J Clin Invest 76:2178–2181.CrossRefGoogle ScholarPubMed
29. Salomaa, V., Matei, C., Aleksic, N., et al. 1999. Soluble thrombomodulin as a predictor of incident coronary heart disease and symptomless carotid artery atherosclerosis in the Atherosclerosis Risk in Communities (ARIC) Study: a case-cohort study. Lancet 353:1729–1734.CrossRefGoogle ScholarPubMed
30. Suen, D.F., Norris, K.L., and Youle, R.J. 2008. Mitochondrial dynamics and apoptosis. Genes Dev 22: 1577–1590.CrossRefGoogle ScholarPubMed
31. Cybulsky, M.I., Iiyama, K., Li, H., et al. 2001. A major role for VCAM-1, but not ICAM-1, in early atherosclerosis. J Clin Invest 107:1255–1262.CrossRefGoogle Scholar
32. Boring, L., Gosling, J., Cleary, M., and Charo, I.F. 1998. Decreased lesion formation in CCR2-/- mice reveals a role for chemokines in the initiation of atherosclerosis. Nature 394:894–897.CrossRefGoogle Scholar
33. Mach, F., Sauty, A., Iarossi, A.S., et al. 1999. Differential expression of three T lymphocyte-activating CXC chemokines by human atheroma-associated cells. J Clin Invest 104:1041–1050.CrossRefGoogle Scholar
34. Clinton, S.K., Underwood, R., Hayes, L., Sherman, M.L., Kufe, D.W., and Libby, P. 1992. Macrophage colony-stimulating factor gene expression in vascular cells and in experimental and human atherosclerosis. Am J Pathol 140: 301–316.Google ScholarPubMed
35. Doran, A.C., Meller, N., and McNamara, C.A. 2008. Role of smooth muscle cells in the initiation and early progression of atherosclerosis. Arterioscler Thromb Vasc Biol 28:812–819.CrossRefGoogle ScholarPubMed
36. Wu, K.K., and Matijevic-Aleksic, N. 2005. Molecular aspects of thrombosis and antithrombotic drugs. Crit Rev Clin Lab Sci 42:249–277.CrossRefGoogle ScholarPubMed
37. Dirnagl, U., Iadecola, C., and Moskowitz, M.A. 1999. Pathobiology of ischemic stroke: an integrated view. Trends Neurosci 22:391–397.CrossRefGoogle Scholar
38. Frangogiannis, N.G. 2008. The immune system and cardiac repair. Pharmacol Res. 58(2):88–111.CrossRefGoogle ScholarPubMed
39. Willems, I.E., Havenith, M.G., De Mey, J.G., and Daemen, M.J. 1994. The alpha-smooth muscle actin-positive cells in healing human myocardial scars. Am J Pathol 145:868–875.Google ScholarPubMed
40. Tomasek, J.J., Gabbiani, G., Hinz, B., Chaponnier, C., and Brown, R.A. 2002. Myofibroblasts and mechano-regulation of connective tissue remodelling. Nat Rev Mol Cell Biol 3:349–363.CrossRefGoogle ScholarPubMed
41. Ogryzko, V.V., Schiltz, R.L., Russanova, V., Howard, B.H., and Nakatani, Y. 1996. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87:953–959.CrossRefGoogle ScholarPubMed
42. Boyes, J., Byfield, P., Nakatani, Y., and Ogryzko, V. 1998. Regulation of activity of the transcription factor GATA-1 by acetylation. Nature 396:594–598.CrossRefGoogle ScholarPubMed
43. Furia, B., Deng, L., Wu, K., et al. 2002. Enhancement of nuclear factor-kappa B acetylation by coactivator p300 and HIV-1 Tat proteins. J Biol Chem 277:4973–4980.CrossRefGoogle ScholarPubMed
44. Karin, M. 1999. The beginning of the end: IkappaB kinase (IKK) and NF-kappaB activation. J Biol Chem 274:27339–27342.CrossRefGoogle Scholar
45. Chen, L.F., Mu, Y., and Greene, W.C. 2002. Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB. EMBO J 21:6539–6548.CrossRefGoogle ScholarPubMed
46. Deng, W.G., and Wu, K.K. 2003. Regulation of inducible nitric oxide synthase expression by p300 and p50 acetylation. J Immunol 171:6581–6588.CrossRefGoogle ScholarPubMed
47. Wedel, A., and Ziegler-Heitbrock, H. W. 1995. The C/EBP family of transcription factors. Immunobiology 193:171–185.CrossRefGoogle Scholar
48. Akira, S., and Kishimoto, T. 1997. NF-IL6 and NF-kappa B in cytokine gene regulation. Adv Immunol 65:1–46.Google ScholarPubMed
49. Nakajima, T., Kinoshita, S., Sasagawa, T., et al. 1993. Phosphorylation at threonine-235 by a ras-dependent mitogen-activated protein kinase cascade is essential for transcription factor NF-IL6. Proc Natl Acad Sci USA 90:2207–2211.CrossRefGoogle ScholarPubMed
50. Trautwein, C., Caelles, C., van der Geer, P., Hunter, T., Karin, M., and Chojkier, M. 1993. Transactivation by NF-IL6/LAP is enhanced by phosphorylation of its activation domain. Nature 364:544–547.CrossRefGoogle ScholarPubMed
51. Buck, M., Poli, V., van der Geer, P., Chojkier, M., and Hunter, T. 1999. Phosphorylation of rat serine 105 or mouse threonine 217 in C/EBP beta is required for hepatocyte proliferation induced by TGF alpha. Mol Cell 4:1087–1092.CrossRefGoogle Scholar
52. Wegner, M., Cao, Z., and Rosenfeld, M.G. 1992. Calcium-regulated phosphorylation within the leucine zipper of C/EBP beta. Science 256:370–373.CrossRefGoogle ScholarPubMed
53. Dlaska, M., and Weiss, G. 1999. Central role of transcription factor NF-IL6 for cytokine and iron-mediated regulation of murine inducible nitric oxide synthase expression. J Immunol 162:6171–6177.Google ScholarPubMed
54. Fitzgerald, G.A. 2004. Coxibs and cardiovascular disease. N Engl J Med 351:1709–1711.CrossRefGoogle ScholarPubMed
55. Cipollone, F., Prontera, C., Pini, B., et al. 2001. Overexpression of functionally coupled cyclooxygenase-2 and prostaglandin E synthase in symptomatic atherosclerotic plaques as a basis of prostaglandin E(2)-dependent plaque instability. Circulation 104:921–927.CrossRefGoogle ScholarPubMed
56. Mukherjee, D., Nissen, S.E., and Topol, E.J. 2001. Risk of cardiovascular events associated with selective COX-2 inhibitors. JAMA 286:954–959.CrossRefGoogle ScholarPubMed
57. Schonbeck, U., Sukhova, G.K., Graber, P., Coulter, S., and Libby, P. 1999. Augmented expression of cyclooxygenase-2 in human atherosclerotic lesions. Am J Pathol 155:1281–1291.CrossRefGoogle ScholarPubMed
58. Wu, K.K. 2006. Transcription-based COX-2 inhibition: a therapeutic strategy. Thromb Haemost 96:417–422.Google ScholarPubMed
59. Cieslik, K., Zhu, Y., and Wu, K.K. 2002. Salicylate suppresses macrophage nitric-oxide synthase-2 and cyclo-oxygenase-2 expression by inhibiting CCAAT/enhancer-binding protein-beta binding via a common signaling pathway. J Biol Chem 277:49304–49310.CrossRefGoogle Scholar
Libby, P. 2002. Inflammation in atherosclerosis. Nature 420:868–874.CrossRefGoogle ScholarPubMed
Liou, J.Y., Lee, S., Ghelani, D., Matijevic-Aleksic, N., and Wu, K.K. 2006. Protection of endothelial survival by peroxisome proliferator-activated receptor-delta mediated 14–3–3 upregulation. Arterioscler Thromb Vasc Biol 26:1481–1487.CrossRefGoogle ScholarPubMed
Wu, K.K. 2006. Transcription-based COX-2 inhibition: a therapeutic strategy. Thromb Haemost 96:417–422.Google ScholarPubMed
Wu, K.K., Liou, J.Y., and Cieslik, K. 2005. Transcriptional control of COX-2 via C/EBPbeta. Arterioscler Thromb Vasc Biol 25:679–685.CrossRefGoogle ScholarPubMed

Save book to Kindle

To save this book to your Kindle, first ensure [email protected] is added to your Approved Personal Document E-mail List under your Personal Document Settings on the Manage Your Content and Devices page of your Amazon account. Then enter the ‘name’ part of your Kindle email address below. Find out more about saving to your Kindle.

Note you can select to save to either the @free.kindle.com or @kindle.com variations. ‘@free.kindle.com’ emails are free but can only be saved to your device when it is connected to wi-fi. ‘@kindle.com’ emails can be delivered even when you are not connected to wi-fi, but note that service fees apply.

Find out more about the Kindle Personal Document Service.

Available formats
×

Save book to Dropbox

To save content items to your account, please confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account. Find out more about saving content to Dropbox.

Available formats
×

Save book to Google Drive

To save content items to your account, please confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account. Find out more about saving content to Google Drive.

Available formats
×