Abstract
Helicobacter pylori is a Gram-negative bacteria that infects the human stomach of half of the world’s Âpopulation. Colonization is followed by infiltration of the gastric mucosa by lymphocytes and myeloid cells. These cells are activated by various bacterial factors, causing them to produce immune/inflammatory mediators, including reactive nitrogen species and polyamines that contribute to cellular damage and the pathogenesis of H. pylori-associated gastric cancer. In vitro experiments have revealed that H. pylori induces macrophage polyamine production by upregulation of the arginase 2/ornithine decarboxylase (ODC) metabolic pathway and enhances hydrogen peroxide synthesis through the activity of spermidine oxidase (SMO). In this chapter, we present a survey of the methods used to analyze the induction and the role of the enzymes related to polyamine metabolism, i.e., arginase, ODC, and SMO in H. pylori-infected macrophages.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Cover TL, Blaser MJ (2009) Helicobacter pylori in health and disease. Gastroenterology 136:1863–1873
Wilson KT, Crabtree JE (2007) Immunology of Helicobacter pylori: insights into the failure of the immune response and perspectives on vaccine studies. Gastroenterology 133:288–308
Gobert AP, McGee DJ, Akhtar M, Mendz GL, Newton JC, Cheng Y, Mobley HL, Wilson KT (2001) Helicobacter pylori arginase inhibits nitric oxide production by eukaryotic cells: a strategy for bacterial survival. Proc Natl Acad Sci U S A 98:13844–13849
Gobert AP, Cheng Y, Akhtar M, Mersey BD, Blumberg DR, Cross RK, Chaturvedi R, Drachenberg CB, Boucher JL, Hacker A, Casero RA Jr, Wilson KT (2004) Protective role of arginase in a mouse model of colitis. J Immunol 173:2109–2117
Gobert AP, Cheng Y, Wang JY, Boucher JL, Iyer RK, Cederbaum SD, Casero RA Jr, Newton JC, Wilson KT (2002) Helicobacter pylori induces macrophage apoptosis by activation of arginase II. J Immunol 168:4692–4700
Chaturvedi R, Cheng Y, Asim M, Bussiere FI, Xu H, Gobert AP, Hacker A, Casero RA Jr, Wilson KT (2004) Induction of polyamine oxidase 1 by Helicobacter pylori causes macrophage apoptosis by hydrogen peroxide release and mitochondrial membrane depolarization. J Biol Chem 279:40161–40173
Cheng Y, Chaturvedi R, Asim M, Bussiere FI, Scholz A, Xu H, Casero RA Jr, Wilson KT (2005) Helicobacter pylori-induced macrophage apoptosis requires activation of ornithine decarboxylase by c-Myc. J Biol Chem 280:22492–22496
Bussiere FI, Chaturvedi R, Cheng Y, Gobert AP, Asim M, Blumberg DR, Xu H, Kim PY, Hacker A, Casero RA Jr, Wilson KT (2005) Spermine causes loss of innate immune response to Helicobacter pylori by inhibition of inducible nitric-oxide synthase translation. J Biol Chem 280:2409–2412
Chaturvedi R, Asim M, Lewis ND, Algood HM, Cover TL, Kim PY, Wilson KT (2007) L-arginine availability regulates inducible nitric oxide synthase-dependent host defense against Helicobacter pylori. Infect Immun 75:4305–4315
Xu H, Chaturvedi R, Cheng Y, Bussiere FI, Asim M, Yao MD, Potosky D, Meltzer SJ, Rhee JG, Kim SS, Moss SF, Hacker A, Wang Y, Casero RA Jr, Wilson KT (2004) Spermine oxidation induced by Helicobacter pylori results in apoptosis and DNA damage: implications for gastric carcinogenesis. Cancer Res 64:8521–8525
Wilson KT, Ramanujam KS, Mobley HL, Musselman RF, James SP, Meltzer SJ (1996) Helicobacter pylori stimulates inducible nitric oxide synthase expression and activity in a murine macrophage cell line. Gastroenterology 111:1524–1533
Gobert AP, Mersey BD, Cheng Y, Blumberg DR, Newton JC, Wilson KT (2002) Cutting edge: urease release by Helicobacter pylori stimulates macrophage inducible nitric oxide synthase. J Immunol 168:6002–6006
Corraliza IM, Campo ML, Soler G, Modolell M (1994) Determination of arginase activity in macrophages: a micromethod. J Immunol Methods 174:231–235
Acknowledgements
This work was supported by R01 DK053620, R01 AT004821, P01 CA116087, P01 CA028842, P30 DK058404 (Vanderbilt Digestive Disease Center), and a Merit Review Grant from the Office of Medical Research, Department of Veterans Affairs. APG is also supported by a grant from Philippe Foundation.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2011 Springer Science+Business Media, LLC
About this protocol
Cite this protocol
Gobert, A.P., Chaturvedi, R., Wilson, K.T. (2011). Methods to Evaluate Alterations in Polyamine Metabolism Caused by Helicobacter pylori Infection. In: Pegg, A., Casero, Jr., R. (eds) Polyamines. Methods in Molecular Biology, vol 720. Humana Press. https://doi.org/10.1007/978-1-61779-034-8_26
Download citation
DOI: https://doi.org/10.1007/978-1-61779-034-8_26
Published:
Publisher Name: Humana Press
Print ISBN: 978-1-61779-033-1
Online ISBN: 978-1-61779-034-8
eBook Packages: Springer Protocols