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Neutrophil transmigration mediated by the neutrophil-specific antigen CD177 is influenced by the endothelial S536N dimorphism of platelet endothelial cell adhesion

molecule-1. J. Immunol. 184, 3889-3896.

Belcher J.D., Beckman J.D., Balla G., Balla J. and Vercellotti G. (2010). Heme

degradation and vascular injury. Antioxid. Redox Signal. 12, 233-248.

Bilban M., Bach F.H., Otterbein S.L., Ifedigbo E., d'Avila J.C., Esterbauer H., Chin B.Y., Usheva A., Robson S.C., Wagner O. and Otterbein L.E. (2006). Carbon monoxide orchestrates a protective response through PPARgamma. Immunity. 24, 601-610.

Bonkovsky H.L., Healey J.F. and Pohl J. (1990). Purification and characterization of heme oxygenase from chick liver. Comparison of the avian and mammalian enzymes. Eur.

J. Biochem.189, 155–166.

Brouard S., Otterbein L.E., Anrather J., Tobiasch E., Bach F.H., Choi A.M. and Soares M.P. (2000). Carbon monoxide generated by heme oxygenase-1 suppresses endothelial cell apoptosis. J. Exp. Med. 192, 1015–1026.

Calay D. and Mason J.C. (2014). The multifunctional role and therapeutic potential of HO-1 in the vascular endothelium. Antioxid. Redox Signal. 20, 1789-1809.

Cepinskas G., Savickiene J., Ionescu C.V. and Kvietys P.R. (2003). PMN transendothelial migration decreases nuclear NFkappaB in IL-1beta-activated endothelial cells: role of PECAM-1. J. Cell Biol. 161, 641-651.

Choi A.M.K. and Alam J. (1996). Heme oxygenase-1: function, regulation, and implication of a novel stress-inducible protein in oxidant-induced lung injury. Am. J.

Respir. Cell Mol. Biol. 15, 9-19.

Cheng H.J., Lei H.Y., Lin C.F., Luo Y.H., Wan S.W., Liu H.S., Yeh T.M. and Lin Y.S.

(2009). Anti-dengue virus nonstructural protein 1 antibodies recognize protein disulfide isomerase on platelets and inhibit platelet aggregation. Mol. Immunol. 47, 398-406.

Colvin R.B. and Smith R.N. (2005). Antibody-mediated organ-allograft rejection. Nat.

Rev. Immunol. 5, 807-817.

Cruse I. and Maines M.D. (1988). Evidence suggesting that the two forms of heme oxygenase are products of different genes. J. Biol. Chem. 263, 3348-3353.

Dejana E., Orsenigo F., Lampugnani M.G. (2008). The role of adherens junctions and VE-cadherin in the control of vascular permeability. J. Cell Sci. 121, 2115-2122.

Djamali A., Kaufman D.B., Ellis T.M., Zhong W., Matas A. and Samaniego M. (2014).

Diagnosis and management of antibody-mediated rejection: current status and novel approaches. Am. J. Transplant. 14, 255-271.

Exner M., Minar E., Wagner O., Schillinger M. (2004). The role of heme oxygenase-1

promoter polymorphisms in human disease. Free Radic. Biol. Med. 37, 1097-1104.

Falconar A.K. (2007). Antibody responses are generated to immunodominant ELK/

KLE-type motifs on the nonstructural-1 glycoprotein during live dengue virus infections in mice and humans: implications for diagnosis, pathogenesis, and vaccine design. Clin.

Vaccine Immunol. 14, 493–504.

Gao C., Sun W., Christofidou-Solomidou M., Sawada M., Newman D.K., Bergom C., Albelda S.M., Matsuyama S. and Newman P.J. (2003). PECAM-1 functions as a specific and potent inhibitor of mitochondrial-dependent apoptosis. Blood 102, 169-179.

Garrido-Urbani S., Bradfield P.F. and Imhof B.A. (2014). Tight junction dynamics: the role of junctional adhesion molecules (JAMs). Cell Tissue Res. 355, 701-715.

George J.F, Braun A., Brusko T.M., Joseph R., Bolisetty S., Wasserfall C.H., Atkinson M.A., Agarwal A. and Kapturczak M.H. (2008). Suppression by CD4+CD25+ regulatory T cells is dependent on expression of heme oxygenase-1 in antigen-presenting cells. Am.

J. Pathol. 173, 154–160.

Gilmore T.D. (2006). Introduction to NF-kappaB: players, pathways, perspectives.

Oncogene. 25, 6680–6684.

Gozzelino R., Jeney V. and Soares M.P. (2010). Mechanisms of cell protection by heme oxygenase-1. Annu. Rev. Pharmacol. Toxicol. 50, 323-354.

Grosser N., Hemmerle A., Berndt G., Erdmann K., Hinkelmann U., Schurger S, Wijayanti N., Immenschuh S. and Schroder H. (2004). The antioxidant defense protein heme oxygenase 1 is a novel target for statins in endothelial cells. Free Radic. Biol. Med. 37, 2064-2071.

Haldane J.B. (1927). Carbon Monoxide as a Tissue Poison. Biochem. J. 21, 1068-1075.

Halstead S. B. (2007). Dengue Lancet. 370, 1644–1652.

Hayashi S., Takamiya R., Yamaguchi T., Matsumoto K., Tojo S.J., Tamatani T., Kitajima M., Makino N., Ishimura Y. and Suematsu M. (1999). Induction of heme oxygenase-1 suppresses venular leukocyte adhesion elicited by oxidative stress: role of bilirubin generated by the enzyme. Circ. Res. 85, 663–671.

Hess J., Angel P. and Schorpp-Kistner M. (2004). AP-1 subunits: quarrel and harmony among siblings. J. Cell Sci. 117, 5965–5973.

Hirohashi T., Uehara S., Chase C.M., DellaPelle P., Madsen J.C., Russell P.S. and Colvin R.B. (2010). Complement independent antibody-mediated endarteritis and transplant arteriopathy in mice. Am. J. Transplant. 10, 510-517.

Igarashi K. and Sun J. (2006). The heme-Bach1 pathway in the regulation of oxidative

stress response and erythroid differentiation. Antioxid. Redox Signal. 8, 107–118.

Igarashi K. and Watanabe-Matsui M. (2014). Wearing red for signaling: the heme-bach axis in heme metabolism, oxidative stress response and iron immunology. Tohoku J. Exp.

Med. 232, 229-253.

Immenschuh S., and Ramadori G. (2000). Gene regulation of heme oxygenase-1 as a therapeutic target. Biochem. Pharmacol. 60, 1121-1128.

Immenschuh S. and Schroder H. (2006). Heme oxygenase-1 and cardiovascular disease.

Histol. Histopathol. 21, 679–685.

Immenschuh S., Baumgart-Vogt E., Tan M., Iwahara S., Ramadori G. and Fahimi H.D.

(2003). Differential cellular and subcellular localization of heme-binding protein 23/peroxiredoxin I and heme oxygenase-1 in rat liver. J. Histochem. Cytochem. 51, 1621-1631.

Immenschuh S., Rahayu P., Bayat B., Saragih H., Rachman A. and Santoso S. (2013).

Antibodies against dengue virus nonstructural protein-1 induce heme oxygenase-1 via a redox-dependent pathway in human endothelial cells. Free Radic. Biol. Med. 54, 85-92.

Iwasaki K., Miwa Y., Haneda M., Uchida K., Nakao A. and Kobayashi T. (2010).

Significance of HLA class I antibody-induced antioxidant gene expression for endothelial cell protection against complement attack. Biochem. Biophys. Res. Commun. 391, 1210–1215

Iwasaki K., Miwa Y., Ogawa H., Yazaki S., Iwamoto M., Furusawa T., Onishi A., Kuzuya T., Haneda M., Watarai Y., Uchida K. and Kobayashi T. (2012). Comparative study on signal transduction in endothelial cells after anti-a/b and human leukocyte antigen antibody reaction: implication of accommodation. Transplantation. 93, 390-397.

Kadl A., Pontiller J., Exner M. and Leitinger N. (2007). Single bolus injection of bilirubin improves the clinical outcome in a mouse model of endotoxemia. Shock. 28, 582-588.

Kapitulnik J. and Maines M.D. (2012). The role of bile pigments in health and disease:

effects on cell signaling, cytotoxicity, and cytoprotection. Front. Pharmacol. 3, 136.

Kapturczak M.H., Wasserfall C., Brusko T., Campbell-Thompson M., Ellis T.M., Atkinson M.A., Aqarwal A. (2004). Heme oxygenase-1 modulates early inflammatory responses: evidence from the heme oxygenase-1-deficient mouse. Am. J. Pathol. 165, 1045–1053.

Kawashima A., Oda Y., Yachie A., Koizumi S. and Nakanishi I. (2002). Heme

oxygenase-1 deficiency: the first autopsy case. Hum. Pathol. 33, 125.

Keshavan P., Deem T.L., Schwemberger S.J., Babcock G.F., Cook-Mills J.M. and Zucker S.D. (2005). Unconjugated bilirubin inhibits VCAM-1-mediated transendothelial leukocyte migration. J. Immunol. 174, 3709–3718.

Keyse S.M., Applegate L.A., Tromvoukis Y. and Tyrrell R.M. (1990). Oxidant stress leads to transcriptional activation of the human heme oxygenase gene in cultured skin fibroblasts. Mol. Cell Biol. 10, 4967–4969.

Kim H.P., Ryter S.W. and Choi A.M. (2006). CO as a cellular signaling molecule. Annu.

Rev. Pharmacol. Toxicol. 46, 411–449.

Kirino Y., Takeno M., Murakami S., Kobayashi M., Kobayashi H., Miura K., Ideguchi H., Ohno S., Ueda A. and Ishigatsubo Y. (2007). Tumor necrosis factor alpha acceleration of inflammatory responses by down-regulating heme oxygenase 1 in human peripheral monocytes. Arthritis Rheum. 56, 464-475.

Kittleson M.M. and Kobashigawa J.A. (2012). Antibody-mediated rejection. Curr. Opin.

Organ Transplant. 17, 551-557.

Kobayashi M. and Yamamoto M. (2005). Molecular mechanisms activating the Nrf2–

Keap1 pathway of antioxidant gene regulation. Antioxid. Redox Signal. 7, 385–394.

Koyasu S. (2003). The role of PI3K in immune cells. Nat. Immunol. 4, 313-319.

Kuckleburg C.J., Tilkens S.B., Santoso S., Newman P.J. (2012). Proteinase 3 contributes to transendothelial migration of NB1-positive neutrophils. J. Immunol. 188, 2419-2426.

Larsen R., Gozzelino R., Jeney V., Tokaji L., Bozza F.A., Japiassú A.M., Bonaparte D., Cavalcante M.M., Chora A., Ferreira A., Marguti I., Cardoso S., Sepúlveda N., Smith A.

and Soares M.P. (2010). A central role for free heme in the pathogenesis of severe sepsis.Sci. Transl. Med. 2, 51ra71.

Laurindo F. R.. Fernandes D. C., Amanso A. M., Lopes L. R. and Santos C. X. (2008).