Renin-angiotensin system in human coronavirus pathogenesis

Future Virology

Volumn 5, Issue 2, 2010, Pages 145-161

  Wevers, Brigitte A ^a   Van Der Hoek, Lia ^b  

^a ACADEMIC MEDICAL CENTER   (Netherlands)

^b Center for Infection and Immunity Amsterdam   (Netherlands)

Author keywords

Aminopeptidase N; Angiotensin converting enzyme 2; Human coronavirus 229E; Human coronavirus NL63; Renin angiotensin system; SARS CoV; Virus host interactions

Indexed keywords

ANGIOTENSIN CONVERTING ENZYME 2; ANGIOTENSIN II; ANGIOTENSIN II [3-8]; CELL PROTEIN; MICROSOMAL AMINOPEPTIDASE; PROTEINASE;

ACUTE LUNG INJURY; ADULT RESPIRATORY DISTRESS SYNDROME; CORONAVIRUS INFECTION; ENZYME ACTIVITY; HUMAN; LIPID BILAYER; NONHUMAN; NULL ALLELE; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN EXPRESSION; RENIN ANGIOTENSIN ALDOSTERONE SYSTEM; REVIEW; SARS CORONAVIRUS; SEVERE ACUTE RESPIRATORY SYNDROME; SIGNAL TRANSDUCTION; TARGET CELL; VIRUS CELL INTERACTION; VIRUS ENTRY; VIRUS PATHOGENESIS; VIRUS STRAIN; VIRUS TRANSMISSION; VIRUS VIRULENCE;

EID: 77649299023     PISSN: 17460794     EISSN: None     Source Type: Journal    
DOI: 10.2217/fvl.10.4     Document Type: Review

References (189)

1. Gonzalez JM, Gomez-Puertas P, Cavanagh D, Gorbalenya AE, Enjuanes L: A comparative sequence analysis to revise the current taxonomy of the family Coronaviridae. Arch. Virol. 148(11), 2207-2235 (2003).
2. Weiss SR, Navas-Martin S: Coronavirus pathogenesis and the emerging pathogen severe acute respiratory syndrome coronavirus. Microbiol. Mol. Biol. Rev. 69(4), 635-664 (2005).
3. Bradburne AF, Bynoe ML, Tyrrell DA: Effects of a 'new' human respiratory virus in volunteers. Br. Med. J. 3(5568), 767-769 (1967).
4. van der Hoek L: Human coronaviruses: what do they cause? Antivir. Ther. 12(4 Pt B), 651-658 (2007).
5. Fouchier RA, Kuiken T, Schutten M et al.: Aetiology: Koch's postulates fulfilled for SARS virus. Nature 423(6937), 240 (2003).
6. Ksiazek TG, Erdman D, Goldsmith CS et al.: A novel coronavirus associated with severe acute respiratory syndrome. N. Engl. J. Med. 348(20), 1953-1966 (2003).
7. Kuiken T, Fouchier RA, Schutten M et al.: Newly discovered coronavirus as the primary cause of severe acute respiratory syndrome. Lancet 362(9380), 263-270 (2003).
8. Peiris JS, Lai ST, Poon LL et al.: Coronavirus as a possible cause of severe acute respiratory syndrome. Lancet 361(9366), 1319-1325 (2003).
9. Peiris JS, Guan Y, Yuen KY: Severe acute respiratory syndrome. Nat. Med. 10(Suppl. 12), S88-S97 (2004).
10. van der Hoek L, Pyrc K, Jebbink MF et al.: Identification of a new human coronavirus. Nat. Med. 10(4), 368-373 (2004).
11. Fouchier RA, Hartwig NG, Bestebroer TM et al.: A previously undescribed coronavirus associated with respiratory disease in humans. Proc. Natl Acad. Sci. USA 101(16), 6212-6216 (2004).
12. Woo PC, Lau SK, Chu CM et al.: Characterization and complete genome sequence of a novel coronavirus, coronavirus HKU1, from patients with pneumonia. J. Virol. 79(2), 884-895 (2005).
13. Garbino J, Crespo S, Aubert JD et al.: A prospective hospital-based study of the clinical impact of non-severe acute respiratory syndrome (non-SARS)-related human coronavirus infection. Clin. Infect. Dis. 43(8), 1009-1015 (2006).
14. Pyrc K, Berkhout B, van der Hoek L: The novel human coronaviruses NL63 and HKU1. J. Virol. 81(7), 3051-3057 (2007).
15. Helenius A: Virus entry and uncoating. In: Field's Virology. Knipe MD, Howley PM (Eds). Lippincott Williams & Wilkins, PA, USA 99-118 (2007).
16. Stoddart CA, Geleziunas R, Ferrell S et al.: Human immunodeficiency virus type 1 Nef-mediated downregulation of CD4 correlates with Nef enhancement of viral pathogenesis. J. Virol. 77(3), 2124-2133 (2003).
17. Michel N, Allespach I, Venzke S, Fackler OT, Keppler OT: The Nef protein of human immunodeficiency virus establishes superinfection immunity by a dual strategy to downregulate cell-surface CCR5 and CD4. Curr. Biol. 15(8), 714-723 (2005).
18. Ross TM, Oran AE, Cullen BR: Inhibition of HIV-1 progeny virion release by cell-surface CD4 is relieved by expression of the viral Nef protein. Curr. Biol. 9(12), 613-621 (1999).
19. Aiken C, Konner J, Landau NR, Lenburg ME, Trono D: Nef induces CD4 endocytosis: requirement for a critical dileucine motif in the membrane-proximal CD4 cytoplasmic domain. Cell 76(5), 853-864 (1994).
20. Schneider-Schaulies J, Schnorr JJ, Brinckmann U et al.: Receptor usage and differential downregulation of CD46 by measles virus wild-type and vaccine strains. Proc. Natl Acad. Sci. USA 92(9), 3943-3947 (1995).
21. Marschall M, Meier-Ewert H, Herrler G, Zimmer G, Maassab HF: The cell receptor level is reduced during persistent infection with influenza C virus. Arch. Virol. 142(6), 1155-1164 (1997).
22. Santoro F, Kennedy PE, Locatelli G, Malnati MS, Berger EA, Lusso P: CD46 is a cellular receptor for human herpesvirus 6. Cell 99(7), 817-827 (1999).
23. Li W, Moore MJ, Vasilieva N et al.: Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature 426(6965), 450-454 (2003).
24. Kuba K, Imai Y, Rao S et al.: A crucial role of angiotensin converting enzyme 2 (ACE2) in SARS coronavirus-induced lung injury. Nat. Med. 11(8), 875-879 (2005).
25. Hofmann H, Pyrc K, van der Hoek L, Geier M, Berkhout B, Pohlmann S: Human coronavirus NL63 employs the severe acute respiratory syndrome coronavirus receptor for cellular entry. Proc. Natl Acad. Sci. USA 102(22), 7988-7993 (2005).
26. Yeager CL, Ashmun RA, Williams RK et al.: Human aminopeptidase N is a receptor for human coronavirus 229E. Nature 357(6377), 420-422 (1992).
27. Gallagher TM, Buchmeier MJ: Coronavirus spike proteins in viral entry and pathogenesis. Virology 279(2), 371-374 (2001).
28. Marsh M, Helenius A: Virus entry: open sesame. Cell 124(4), 729-740 (2006).
29. Delmas B, Gelfi J, Sjostrom H, Noren O, Laude H: Further characterization of aminopeptidase-N as a receptor for coronaviruses. Adv. Exp. Med. Biol. 342, 293-298 (1993).
30. Tresnan DB, Levis R, Holmes KV: Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I. J. Virol. 70(12), 8669-8674 (1996).
31. Li BX, Ge JW, Li YJ: Porcine aminopeptidase N is a functional receptor for the PEDV coronavirus. Virology 365(1), 166-172 (2007).
32. Lendeckel U, Kahne T, Riemann D, Neubert K, Arndt M, Reinhold D: Review: the role of membrane peptidases in immune functions. Adv. Exp. Med. Biol. 477, 1-24 (2000).
33. Look AT, Ashmun RA, Shapiro LH, Peiper SC: Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N. J. Clin. Invest. 83(4), 1299-1307 (1989).
34. Sjostrom H, Noren O, Olsen J: Structure and function of aminopeptidase N. Adv. Exp. Med. Biol. 477, 25-34 (2000).
35. Mina-Osorio P: The moonlighting enzyme CD13: old and new functions to target. Trends Mol. Med. 14(8), 361-371 (2008).
36. Riemann D, Kehlen A, Langner J: CD13 - not just a marker in leukemia typing. Immunol. Today 20(2), 83-88 (1999).
37. Bhagwat SV, Petrovic N, Okamoto Y, Shapiro LH: The angiogenic regulator CD13/APN is a transcriptional target of Ras signaling pathways in endothelial morphogenesis. Blood 101(5), 1818-1826 (2003).
38. Wang G, Deering C, Macke M et al.: Human coronavirus 229E infects polarized airway epithelia from the apical surface. J. Virol. 74(19), 9234-9239 (2000).
39. Wentworth DE, Tresnan DB, Turner BC et al.: Cells of human aminopeptidase N (CD13) transgenic mice are infected by human coronavirus-229E in vitro, but not in vivo. Virology 335(2), 185-197 (2005).
40. Kolb AF, Hegyi A, Siddell SG: Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N. J. Gen. Virol. 78(Pt 11), 2795-2802 (1997).
41. Breslin JJ, Mork I, Smith MK et al.: Human coronavirus 229E: receptor binding domain and neutralization by soluble receptor at 37°C. J. Virol. 77(7), 4435-4438 (2003).
42. Nomura R, Kiyota A, Suzaki E et al.: Human coronavirus 229E binds to CD13 in rafts and enters the cell through caveolae. J. Virol. 78(16), 8701-8708 (2004).
43. Kawase M, Shirato K, Matsuyama S, Taguchi F: Protease-mediated entry via endosome of human coronavirus 229E. J. Virol. 83(2), 712-721 (2008).
44. Parton RG, Simons K: The multiple faces of caveolae. Nat. Rev. Mol. Cell Biol. 8(3), 185-194 (2007).
45. Riemann D, Hansen GH, Niels-Christiansen L et al.: Caveolae/lipid rafts in fibroblast-like synoviocytes: ectopeptidase-rich membrane microdomains. Biochem. J. 354(Pt 1), 47-55 (2001).
46. Delacour D, Jacob R: Apical protein transport. Cell. Mol. Life Sci. 63(21), 2491-2505 (2006).
47. Han DP, Penn-Nicholson A, Cho MW: Identification of critical determinants on ACE2 for SARS-CoV entry and development of a potent entry inhibitor. Virology 350(1), 15-25 (2006).
48. Tipnis SR, Hooper NM, Hyde R, Karran E, Christie G, Turner AJ: A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase. J. Biol. Chem. 275(43), 33238-33243 (2000).
49. Donoghue M, Hsieh F, Baronas E et al.: A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9. Circ. Res. 87(5), E1-E9 (2000).
50. Vickers C, Hales P, Kaushik V et al.: Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase. J. Biol. Chem. 277(17), 14838-14843 (2002).
51. Guy JL, Lambert DW, Warner FJ, Hooper NM, Turner AJ: Membrane-associated zinc peptidase families: comparing ACE and ACE2. Biochim. Biophys. Acta 1751(1), 2-8 (2005).
52. Nie Y, Wang P, Shi X et al.: Highly infectious SARS-CoV pseudotyped virus reveals the cell tropism and its correlation with receptor expression. Biochem. Biophys. Res. Commun. 321(4), 994-1000 (2004).
53. Ren X, Glende J, Al-Falah M et al.: Analysis of ACE2 in polarized epithelial cells: surface expression and function as receptor for severe acute respiratory syndrome-associated coronavirus. J. Gen. Virol. 87(Pt 6), 1691-1695 (2006).
54. Hamming I, Timens W, Bulthuis ML, Lely AT, Navis GJ, van Goor H: Tissue distribution of ACE2 protein, the functional receptor for SARS coronavirus. A first step in understanding SARS pathogenesis. J. Pathol. 203(2), 631-637 (2004).
55. Harmer D, Gilbert M, Borman R, Clark KL: Quantitative mRNA expression profiling of ACE 2, a novel homologue of angiotensin converting enzyme. FEBS Lett. 532(1-2), 107-110 (2002).
56. Guo Y, Korteweg C, McNutt MA, Gu J: Pathogenetic mechanisms of severe acute respiratory syndrome. Virus Res. 133(1), 4-12 (2008).
57. Oudit GY, Kassiri Z, Jiang C et al.: SARS-coronavirus modulation of myocardial ACE2 expression and inflammation in patients with SARS. Eur. J. Clin. Invest. 39(7), 618-625 (2009).
58. Lambert DW, Yarski M, Warner FJ et al.: Tumor necrosis factor-α convertase (ADAM17) mediates regulated ectodomain shedding of the severe-acute respiratory syndrome-coronavirus (SARS-CoV) receptor, angiotensin-converting enzyme-2 (ACE2). J. Biol. Chem. 280(34), 30113-30119 (2005).
59. Jia HP, Look DC, Tan P et al.: Ectodomain shedding of angiotensin converting enzyme 2 in human airway epithelia. Am. J. Physiol. Lung Cell Mol. Physiol. 297(1), L84-L96 (2009).
60. Warner FJ, Lew RA, Smith AI, Lambert DW, Hooper NM, Turner AJ: Angiotensin-converting enzyme 2 (ACE2), but not ACE, is preferentially localized to the apical surface of polarized kidney cells. J. Biol. Chem. 280(47), 39353-39362 (2005).
61. Rice GI, Jones AL, Grant PJ, Carter AM, Turner AJ, Hooper NM: Circulating activities of angiotensin-converting enzyme, its homolog, angiotensin- converting enzyme 2, and neprilysin in a family study. Hypertension 48(5), 914-920 (2006).
62. Lambert DW, Hooper NM, Turner AJ: Angiotensin-converting enzyme 2 and new insights into the renin-angiotensin system. Biochem. Pharmacol. 75(4), 781-786 (2008).
63. Pyrc K, Dijkman R, Deng L et al.: Mosaic structure of human coronavirus NL63, one thousand years of evolution. J. Mol. Biol. 364(5), 964-973 (2006).
64. Li W, Sui J, HuAng IC et al.: The S proteins of human coronavirus NL63 and severe acute respiratory syndrome coronavirus bind overlapping regions of ACE2. Virology 367(2), 367-374 (2007).
65. Wu K, Li W, Peng G, Li F: Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor. Proc. Natl Acad. Sci. USA 106(47), 19970-19974 (2009).
66. Simmons G, Gosalia DN, Rennekamp AJ, Reeves JD, Diamond SL, Bates P: Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry. Proc. Natl Acad. Sci. USA 102(33), 11876-11881 (2005).
67. Huang IC, Bosch BJ, Li F et al.: SARS coronavirus, but not human coronavirus NL63, utilizes cathepsin L to infect ACE2-expressing cells. J. Biol. Chem. 281(6), 3198-3203 (2006).
68. Bosch BJ, Bartelink W, Rottier PJ: Cathepsin L functionally cleaves the severe acute respiratory syndrome coronavirus class I fusion protein upstream of rather than adjacent to the fusion peptide. J. Virol. 82(17), 8887-8890 (2008).
69. Haga S, Yamamoto N, Nakai-Murakami C et al.: Modulation of TNF-α-converting enzyme by the spike protein of SARS-CoV and ACE2 induces TNF-α production and facilitates viral entry. Proc. Natl Acad. Sci. USA 105(22), 7809-7814 (2008).
70. Glowacka I, Bertram S, Herzog P et al.: Differential downregulation of ACE2 by the spike proteins of SARS-coronavirus and human coronavirus NL63. J. Virol. 84(2), 1198-1205 (2009).
71. Wang S, Guo F, Liu K et al.: Endocytosis of the receptor-binding domain of SARS-CoV spike protein together with virus receptor ACE2. Virus Res. 136(1-2), 8-15 (2008).
72. Wang H, Yang P, Liu K et al.: SARS coronavirus entry into host cells through a novel clathrin- and caveolae-independent endocytic pathway. Cell Res. 18(2), 290-301 (2008).
73. Le Roy C, Wrana JL: Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling. Nat. Rev. Mol. Cell Biol. 6(2), 112-126 (2005).
74. Hansen GH, Delmas B, Besnardeau L et al.: The coronavirus transmissible gastroenteritis virus causes infection after receptor-mediated endocytosis and acid-dependent fusion with an intracellular compartment. J. Virol. 72(1), 527-534 (1998).
75. Kurdi M, De Mello WC, Booz GW: Working outside the system: an update on the unconventional behavior of the renin-angiotensin system components. Int. J. Biochem. Cell Biol. 37(7), 1357-1367 (2005).
76. Zimmerman BG, Dunham EW: Tissue renin-angiotensin system: a site of drug action? Annu. Rev. Pharmacol. Toxicol. 37, 53-69 (1997).
77. Nicholls MG, Richards AM, Agarwal M: The importance of the renin-angiotensin system in cardiovascular disease. J. Hum. Hypertens. 12(5), 295-299 (1998).
78. Warner FJ, Lubel JS, McCaughan GW, Angus PW: Liver fibrosis: a balance of ACEs? Clin. Sci. (Lond.) 113(3), 109-118 (2007).
79. Fleming I, Kohlstedt K, Busse R: The tissue renin-angiotensin system and intracellular signalling. Curr. Opin. Nephrol. Hypertens. 15(1), 8-13 (2006).
80. Batenburg WW, Jan Danser AH: The (pro) renin receptor: a new addition to the renin-angiotensin system? Eur. J. Pharmacol. 585(2-3), 320-324 (2008).
81. Hackenthal E, Paul M, Ganten D, Taugner R: Morphology, physiology, and molecular biology of renin secretion. Physiol. Rev. 70(4), 1067-1116 (1990).
82. Paul M, Poyan Mehr A, Kreutz R: Physiology of local renin-angiotensin systems. Physiol. Rev. 86(3), 747-803 (2006).
83. Unger T, Li J: The role of the renin-angiotensin-aldosterone system in heart failure. J. Renin Angiotensin Aldosterone Syst. 5(Suppl. 1), S7-S10 (2004).
84. Fyhrquist F, Saijonmaa O: Renin-angiotensin system revisited. J. Intern. Med. 264(3), 224-236 (2008).
85. Lindberg BF, Gyllstedt E, Andersson KE: Conversion of angiotensin I to angiotensin II by chymase activity in human pulmonary membranes. Peptides 18(6), 847-853 (1997).
86. Goodfriend TL, Elliott ME, Catt KJ: Angiotensin receptors and their antagonists. N. Engl. J. Med. 334(25), 1649-1654 (1996).
87. Higuchi S, Ohtsu H, Suzuki H, Shirai H, Frank GD, Eguchi S: Angiotensin II signal transduction through the AT1 receptor: novel insights into mechanisms and pathophysiology. Clin. Sci. (Lond.) 112(8), 417-428 (2007).
88. Suzuki Y, Ruiz-Ortega M, Lorenzo O, Ruperez M, Esteban V, Egido J: Inflammation and angiotensin II. Int. J. Biochem. Cell Biol. 35(6), 881-900 (2003).
89. Dragun D, Muller DN, Brasen JH et al.: Angiotensin II type 1-receptor activating antibodies in renal-allograft rejection. N. Engl. J. Med. 352(6), 558-569 (2005).
90. Guzik TJ, Hoch NE, Brown KA et al.: Role of the T cell in the genesis of angiotensin II induced hypertension and vascular dysfunction. J. Exp. Med. 204(10), 2449-2460 (2007).
91. Stegbauer J, Lee DH, Seubert S et al.: Role of the renin-angiotensin system in autoimmune inflammation of the central nervous system. Proc. Natl Acad. Sci. USA 106(35), 14942-14947 (2009).
92. Jones ES, Vinh A, McCarthy CA, Gaspari TA, Widdop RE: AT2 receptors: functional relevance in cardiovascular disease. Pharmacol. Ther. 120(3), 292-316 (2008).
93. AbdAlla S, Lother H, Abdel-tawab AM, Quitterer U: The angiotensin II AT2 receptor is an AT1 receptor antagonist. J. Biol. Chem. 276(43), 39721-39726 (2001).
94. Li J, Culman J, Hortnagl H et al.: Angiotensin AT2 receptor protects against cerebral ischemia-induced neuronal injury. FASEB J. 19(6), 617-619 (2005).
95. Dinh DT, Frauman AG, Johnston CI, Fabiani ME: Angiotensin receptors: distribution, signalling and function. Clin. Sci. (Lond.) 100(5), 481-492 (2001).
96. Braun-Menendez E, Fasciolo JC, Leloir LF, Munoz JM: The substance causing renal hypertension. J. Physiol. 98(3), 283-298 (1940).
97. Smith AI, Turner AJ: What's new in the renin-angiotensin system? Cell. Mol. Life Sci. 61(21), 2675-2676 (2004).
98. Reudelhuber TL: The renin-angiotensin system: peptides and enzymes beyond angiotensin II. Curr. Opin. Nephrol. Hypertens. 14(2), 155-159 (2005).
99. Hamming I, Cooper ME, Haagmans BL et al.: The emerging role of ACE2 in physiology and disease. J. Pathol. 212(1), 1-11 (2007).
100. Peach MJ: Renin-angiotensin system: biochemistry and mechanisms of action. Physiol. Rev. 57(2), 313-370 (1977).
101. Nicholls MG, Robertson JI: The renin-angiotensin system in the year 2000. J. Hum. Hypertens. 14(10-11), 649-666 (2000).
102. Ferrario CM, Trask AJ, Jessup JA: Advances in biochemical and functional roles of angiotensin-converting enzyme 2 and angiotensin-(1-7) in regulation of cardiovascular function. Am. J. Physiol. Heart Circ. Physiol. 289(6), H2281-H2290 (2005).
103. Danilczyk U, Eriksson U, Crackower MA, Penninger JM: A story of two ACEs. J. Mol. Med. 81(4), 227-234 (2003).
104. Rice GI, Thomas DA, Grant PJ, Turner AJ, Hooper NM: Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolism. Biochem. J. 383(Pt 1), 45-51 (2004).
105. Varagic J, Trask AJ, Jessup JA, Chappell MC, Ferrario CM: New angiotensins. J. Mol. Med. 86(6), 663-671 (2008).
106. Welches WR, Santos RA, Chappell MC, Brosnihan KB, Greene LJ, Ferrario CM: Evidence that prolyl endopeptidase participates in the processing of brain angiotensin. J. Hypertens. 9(7), 631-638 (1991).
107. Ferrario CM: Commentary on Tikellis et al.: there is more to discover about angiotensin-converting enzyme. Hypertension 41(3), 390-391 (2003).
108. Santos RA, Simoes e Silva AC, Maric C et al.: Angiotensin-(1-7) is an endogenous ligand for the G protein-coupled receptor Mas. Proc. Natl Acad. Sci. USA 100(14), 8258-8263 (2003).
109. Walters PE, Gaspari TA, Widdop RE: Angiotensin-(1-7) acts as a vasodepressor agent via angiotensin II type 2 receptors in conscious rats. Hypertension 45(5), 960-966 (2005).
110. Santos RA, Campagnole-Santos MJ, Andrade SP: Angiotensin-(1-7): an update. Regul. Pept. 91(1-3), 45-62 (2000).
111. Santos RA, Ferreira AJ, Simoes ESAC: Recent advances in the angiotensin-converting enzyme 2-angiotensin(1-7)-Mas axis. Exp. Physiol. 93(5), 519-527 (2008).
112. Crackower MA, Sarao R, Oudit GY et al.: Angiotensin-converting enzyme 2 is an essential regulator of heart function. Nature 417(6891), 822-828 (2002).
113. Gurley SB, Allred A, Le TH et al.: Altered blood pressure responses and normal cardiac phenotype in ACE2-null mice. J. Clin. Invest. 116(8), 2218-2225 (2006).
114. Yamamoto K, Ohishi M, Katsuya T et al.: Deletion of angiotensin-converting enzyme 2 accelerates pressure overload-induced cardiac dysfunction by increasing local angiotensin II. Hypertension 47(4), 718-726 (2006).
115. Ardaillou R, Chansel D: Synthesis and effects of active fragments of angiotensin II. Kidney Int. 52(6), 1458-1468 (1997).
116. Banegas I, Prieto I, Vives F et al.: Brain aminopeptidases and hypertension. J. Renin Angiotensin Aldosterone Syst. 7(3), 129-134 (2006).
117. Healy DP, Wilk S: Localization of immunoreactive glutamyl aminopeptidase in rat brain. II. Distribution and correlation with angiotensin II. Brain Res. 606(2), 295-303 (1993).
118. 125I] angiotensins in rat. J. Neurochem. 46(4), 1292-1297 (1986).
119. Ruiz-Ortega M, Lorenzo O, Egido J: Angiotensin III increases MCP-1 and activates NF-κB and AP-1 in cultured mesangial and mononuclear cells. Kidney Int. 57(6), 2285-2298 (2000).
120. Wright JW, Yamamoto BJ, Harding JW: Angiotensin receptor subtype mediated physiologies and behaviors: new discoveries and clinical targets. Prog. Neurobiol. 84(2), 157-181 (2008).
121. Ahmad S, Ward PE: Role of aminopeptidase activity in the regulation of the pressor activity of circulating angiotensins. J. Pharmacol. Exp. Ther. 252(2), 643-650 (1990).
122. Chai SY, Fernando R, Peck G et al.: The angiotensin IV/AT4 receptor. Cell. Mol. Life Sci. 61(21), 2728-2737 (2004).
123. Ruiz-Ortega M, Esteban V, Egido J: The regulation of the inflammatory response through nuclear factor-κB pathway by angiotensin IV extends the role of the renin angiotensin system in cardiovascular diseases. Trends Cardiovasc. Med. 17(1), 19-25 (2007).
124. Mustafa T, Lee JH, Chai SY, Albiston AL, McDowall SG, Mendelsohn FA: Bioactive angiotensin peptides: focus on angiotensin IV. J. Renin Angiotensin Aldosterone Syst. 2(4), 205-210 (2001).
125. Vanderheyden PM: From angiotensin IV binding site to AT(4) receptor. Mol. Cell Endocrinol. 302(2) 159-166 (2008).
126. Esteban V, Ruperez M, Sanchez-Lopez E et al.: Angiotensin IV activates the nuclear transcription factor-κB and related proinflammatory genes in vascular smooth muscle cells. Circ. Res. 96(9), 965-973 (2005).
127. Veerappan A, Reid AC, Estephan R et al.: Mast cell renin and a local renin-angiotensin system in the airway: role in bronchoconstriction. Proc. Natl Acad.
128. Boyce JA: The role of mast cells in asthma. Prostaglandins Leukot. Essent. Fatty Acids 69(2-3), 195-205 (2003).
129. Andersson CK, Mori M, Bjermer L, Lofdahl CG, Erjefalt JS: Novel site-specific mast cell subpopulations in the human lung. Thorax 64(4), 297-305 (2009).
130. Campbell DJ, Habener JF: Angiotensinogen gene is expressed and differentially regulated in multiple tissues of the rat. J. Clin. Invest. 78(1), 31-39 (1986).
131. Ohkubo H, Nakayama K, Tanaka T, Nakanishi S: Tissue distribution of rat angiotensinogen mRNA and structural analysis of its heterogeneity. J. Biol. Chem. 261(1), 319-323 (1986).
132. Studdy PR, Lapworth R, Bird R: Angiotensin-converting enzyme and its clinical significance - a review. J. Clin. Pathol. 36(8), 938-947 (1983).
133. Bullock GR, Steyaert I, Bilbe G et al.: Distribution of type-1 and type-2 angiotensin receptors in the normal human lung and in lungs from patients with chronic obstructive pulmonary disease. Histochem. Cell Biol. 115(2), 117-124 (2001).
134. Wang R, Zagariya A, Ibarra-Sunga O et al.: Angiotensin II induces apoptosis in human and rat alveolar epithelial cells. Am. J. Physiol. 276(5 Pt 1), L885-L889 (1999).
135. Papp M, Li X, Zhuang J, Wang R, Uhal BD: Angiotensin receptor subtype AT(1) mediates alveolar epithelial cell apoptosis in response to ANG II. Am. J. Physiol. Lung Cell Mol. Physiol. 282(4), L713-L718 (2002).
136. Kuba K, Imai Y, Penninger JM: Angiotensin-converting enzyme 2 in lung diseases. Curr. Opin. Pharmacol. 6(3), 271-276 (2006).
137. Orte C, Polak JM, Haworth SG, Yacoub MH, Morrell NW: Expression of pulmonary vascular angiotensin-converting enzyme in primary and secondary plexiform pulmonary hypertension. J. Pathol. 192(3), 379-384 (2000).
138. Csaszar A, Halmos B, Palicz T, Szalai C, Romics L: Interpopulation effect of ACE I/D polymorphism on serum concentration of ACE in diagnosis of sarcoidosis. Lancet 350(9076), 518 (1997).
139. Specks U, Martin WJ, 2nd, Rohrbach MS: Bronchoalveolar lavage fluid angiotensin-converting enzyme in interstitial lung diseases. Am. Rev. Respir. Dis. 141(1), 117-123 (1990).
140. Idell S, Kueppers F, Lippmann M, Rosen H, Niederman M, Fein A: Angiotensin converting enzyme in bronchoalveolar lavage in ARDS. Chest 91(1), 52-56 (1987).
141. Imai Y, Kuba K, Rao S et al.: Angiotensin-converting enzyme 2 protects from severe acute lung failure. Nature 436(7047), 112-116 (2005).
142. Ware LB, Matthay MA: The acute respiratory distress syndrome. N. Engl. J. Med. 342(18), 1334-1349 (2000).
143. Rubenfeld GD, Caldwell E, Peabody E et al.: Incidence and outcomes of acute lung injury. N. Engl. J. Med. 353(16), 1685-1693 (2005).
144. Raiden S, Nahmod K, Nahmod V et al.: Nonpeptide antagonists of AT1 receptor for angiotensin II delay the onset of acute respiratory distress syndrome. J. Pharmacol. Exp. Ther. 303(1), 45-51 (2002).
145. Nicholls J, Peiris M: Good ACE, bad ACE do battle in lung injury, SARS. Nat. Med. 11(8), 821-822 (2005).
146. Greene LJ, Spadaro AC, Martins AR, Perussi De Jesus WD, Camargo AC: Brain endo-oligopeptidase B: a post-proline cleaving enzyme that inactivates angiotensin I and II. Hypertension 4(2), 178-184 (1982).
147. Marshall RP, Webb S, Bellingan GJ et al.: Angiotensin converting enzyme insertion/deletion polymorphism is associated with susceptibility and outcome in acute respiratory distress syndrome. Am. J. Respir. Crit. Care Med. 166(5), 646-650 (2002).
148. Jerng JS, Yu CJ, Wang HC, Chen KY, Cheng SL, Yang PC: Polymorphism of the angiotensin-converting enzyme gene affects the outcome of acute respiratory distress syndrome. Crit. Care Med. 34(4), 1001-1006 (2006).
149. Lew TW, Kwek TK, Tai D et al.: Acute respiratory distress syndrome in critically ill patients with severe acute respiratory syndrome. JAMA 290(3), 374-380 (2003).
150. Imai Y, Kuba K, Penninger JM: The discovery of angiotensin-converting enzyme 2 and its role in acute lung injury in mice. Exp. Physiol. 93(5), 543-548 (2008).
151. Frieman M, Baric R: Mechanisms of severe acute respiratory syndrome pathogenesis and innate immunomodulation. Microbiol. Mol. Biol. Rev. 72(4), 672-685 (2008).
152. Chiu RW, Tang NL, Hui DS et al.: ACE2 gene polymorphisms do not affect outcome of severe acute respiratory syndrome. Clin. Chem. 50(9), 1683-1686 (2004).
153. Itoyama S, Keicho N, Hijikata M et al.: Identification of an alternative 5′-untranslated exon and new polymorphisms of angiotensin-converting enzyme 2 gene: lack of association with SARS in the Vietnamese population. Am. J. Med. Genet. A 136(1), 52-57 (2005).
154. Lo AW, Tang NL, To KF: How the SARS coronavirus causes disease: host or organism? J. Pathol. 208(2), 142-151 (2006).
155. Lin HX, Feng Y, Wong G et al.: Identification of residues in the receptor-binding domain (RBD) of the spike protein of human coronavirus NL63 that are critical for the RBD-ACE2 receptor interaction. J. Gen. Virol. 89(Pt 4), 1015-1024 (2008).
156. Mathewson AC, Bishop A, Yao Y et al.: Interaction of severe acute respiratory syndrome-coronavirus and NL63 coronavirus spike proteins with angiotensin converting enzyme-2. J. Gen. Virol. 89(Pt 11), 2741-2745 (2008).
157. Narayanan K, Huang C, Makino S: SARS coronavirus accessory proteins. Virus Res. 133(1), 113-121 (2008).
158. Weidmann P, De Myttenaere-Bursztein S, Maxwell MH, de Lima J: Effect on aging on plasma renin and aldosterone in normal man. Kidney Int. 8(5), 325-333 (1975).
159. Corman B, Barrault MB, Klingler C et al.: Renin gene expression in the aging kidney: effect of sodium restriction. Mech. Ageing Dev. 84(1), 1-13 (1995).
160. Nicholls JM, Peiris JS, Chan KH, Poon LM, Beh SL: Occult respiratory viral infections in coronial autopsies: a pilot project. Hong Kong Med. J. 15(3), S13-15 (2009).
161. Bastien N, Anderson K, Hart L et al.: Human coronavirus NL63 infection in Canada. J. Infect. Dis. 191(4), 503-506 (2005).
162. Cameron MJ, Bermejo-Martin JF, Danesh A, Muller MP, Kelvin DJ: Human immunopathogenesis of severe acute respiratory syndrome (SARS). Virus Res. 133(1), 13-19 (2008).
163. Myint S, Johnston S, Sanderson G, Simpson H: Evaluation of nested polymerase chain methods for the detection of human coronaviruses 229E and OC43. Mol. Cell Probes 8(5), 357-364 (1994).
164. Arbour N, Day R, Newcombe J, Talbot PJ: Neuroinvasion by human respiratory coronaviruses. J. Virol. 74(19), 8913-8921 (2000).
165. Arbour N, Ekande S, Cote G et al.: Persistent infection of human oligodendrocytic and neuroglial cell lines by human coronavirus 229E. J. Virol. 73(4), 3326-3337 (1999).
166. Reaux A, de Mota N, Zini S et al.: PC18, a specific aminopeptidase N inhibitor, induces vasopressin release by increasing the half-life of brain angiotensin III. Neuroendocrinology 69(5), 370-376 (1999).
167. Ruiz-Ortega M, Lorenzo O, Ruperez M et al.: Role of the renin-angiotensin system in vascular diseases: expanding the field. Hypertension 38(6), 1382-1387 (2001).
168. Wolf G: Renal injury due to renin-angiotensin-aldosterone system activation of the transforming growth factor-β pathway. Kidney Int. 70(11), 1914-1919 (2006).
169. Ruiz-Ortega M, Lorenzo O, Egido J: Angiotensin III up-regulates genes involved in kidney damage in mesangial cells and renal interstitial fibroblasts. Kidney Int. Suppl. 68, S41-S45 (1998).
170. Border WA, Noble NA: Transforming growth factor b in tissue fibrosis. N. Engl. J. Med. 331(19), 1286-1292 (1994).
171. Marshall RP, McAnulty RJ, Laurent GJ: Angiotensin II is mitogenic for human lung fibroblasts via activation of the type 1 receptor. Am. J. Respir. Crit. Care Med. 161(6), 1999-2004 (2000).
172. Li X, Molina-Molina M, Abdul-Hafez A, Uhal V, Xaubet A, Uhal BD: Angiotensin converting enzyme-2 is protective but downregulated in human and experimental lung fibrosis. Am. J. Physiol. Lung Cell Mol. Physiol. 295(1), L178-L185 (2008).
173. Uhal BD, Kim JK, Li X, Molina-Molina M: Angiotensin-TGF-β1 crosstalk in human idiopathic pulmonary fibrosis: autocrine mechanisms in myofibroblasts and macrophages. Curr. Pharm. Des. 13(12), 1247-1256 (2007).
174. Weber KT: Fibrosis, a common pathway to organ failure: angiotensin II and tissue repair. Semin. Nephrol. 17(5), 467-491 (1997).
175. Wynn TA: Cellular and molecular mechanisms of fibrosis. J. Pathol. 214(2), 199-210 (2008).
176. Thomas WG, Mendelsohn FA: Angiotensin receptors: form and function and distribution. Int. J. Biochem. Cell Biol. 35(6), 774-779 (2003).
177. Li YD, Block ER, Patel JM: Activation of multiple signaling modules is critical in angiotensin IV-induced lung endothelial cell proliferation. Am. J. Physiol. Lung Cell Mol. Physiol. 283(4), L707-L716 (2002).
178. Patel JM, Martens JR, Li YD, Gelband CH, Raizada MK, Block ER: Angiotensin IV receptor-mediated activation of lung endothelial NOS is associated with vasorelaxation. Am. J. Physiol. 275(6 Pt 1), L1061-L1068 (1998).
179. Rangel R, Sun Y, Guzman-Rojas L et al.: Impaired angiogenesis in aminopeptidase N-null mice. Proc. Natl Acad. Sci. USA 104(11), 4588-4593 (2007).
180. Danziger RS: Aminopeptidase N in arterial hypertension. Heart Fail. Rev. 13(3), 293-298 (2008).
181. Kuhlmann UC, Chwieralski CE, van den Brule S et al.: Modulation of cytokine production and silica-induced lung fibrosis by inhibitors of aminopeptidase N and of dipeptidyl peptidase-IV-related proteases. Life Sci. 84(1-2), 1-11 (2008).
182. Tani K, Ogushi F, Huang L et al.: CD13/aminopeptidase N, a novel chemoattractant for T lymphocytes in pulmonary sarcoidosis. Am. J. Respir. Crit. Care Med. 161(5), 1636-1642 (2000).
183. Heikkinen T, Jarvinen A: The common cold. Lancet 361(9351), 51-59 (2003).
184. Turner RB, Weingand KW, Yeh CH, Leedy DW: Association between interleukin-8 concentration in nasal secretions and severity of symptoms of experimental rhinovirus colds. Clin. Infect. Dis. 26(4), 840-846 (1998).
185. Zhu Z, Tang W, Ray A et al.: Rhinovirus stimulation of interleukin-6 in vivo and in vitro. Evidence for nuclear factor κB-dependent transcriptional activation. J. Clin. Invest. 97(2), 421-430 (1996).
186. Perlman S, Dandekar AA: Immunopathogenesis of coronavirus infections: implications for SARS. Nat. Rev. Immunol. 5(12), 917-927 (2005).
187. Colten HR, Krause JE: Pulmonary inflammation - a balancing act. N. Engl. J. Med. 336(15), 1094-1096 (1997).
188. Cole JM, Khokhlova N, Sutliff RL et al.: Mice lacking endothelial ACE: normal blood pressure with elevated angiotensin II. Hypertension 41(2), 313-321 (2003).
189. Taylor A: Aminopeptidases: structure and function. FASEB J. 7(2), 290-298 (1993).