| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
* Laboratoire de Parasitologie, Université Victor Ségalen, Bordeaux, France;
Laboratoire de Physique des Interactions Ondes-Matière, Centre National de la Recherche Scientifique, Ecole Nationale Superieure de Chimie et Physique de Bordeaux, piom, Unité Mixte de Recherche 5501, Talence, France;
Laboratoire de Chimie et Biochimie Pharmacologiques, Unité Mixte de Recherche 8601, Centre National de la Recherche Scientifique, Université René Descartes, Paris, France;
Department of Medicine, Division of Gastroenterology, University of Maryland School of Medicine, and Veterans Affairs Maryland Health Care System, Baltimore, MD 21201; and
¶
Unité de Microbiologie, Institut National de la Recherche Agronomique, Saint-Genès-Champanelle, France
We previously reported that macrophage arginase inhibits NO-dependent trypanosome killing in vitro and in vivo. BALB/c and C57BL/6 mice are known to be susceptible and resistant to trypanosome infection, respectively. Hence, we assessed the expression and the role of inducible NO synthase (iNOS) and arginase in these two mouse strains infected with Trypanosoma brucei brucei. Arginase I and arginase II mRNA expression was higher in macrophages from infected BALB/c compared with those from C57BL/6 mice, whereas iNOS mRNA was up-regulated at the same level in both phenotypes. Similarly, arginase activity was more important in macrophages from infected BALB/c vs infected C57BL/6 mice. Moreover, increase of arginase I and arginase II mRNA levels and of macrophage arginase activity was directly induced by trypanosomes, with a higher level in BALB/c compared with C57BL/6 mice. Neither iNOS expression nor NO production was stimulated by trypanosomes in vitro. The high level of arginase activity in T. brucei brucei-infected BALB/c macrophages strongly inhibited macrophage NO production, which in turn resulted in less trypanosome killing compared with C57BL/6 macrophages. NO generation and parasite killing were restored to the same level in BALB/c and C57BL/6 macrophages when arginase was specifically inhibited with N
-hydroxy-nor-L-arginine. In conclusion, host arginase represents a marker of resistance/susceptibility to trypanosome infections.
This article has been cited by other articles:
|
|
 |
|
  K. Ramey, F. O. Eko, W. E. Thompson, H. Armah, J. U. Igietseme, and J. K. Stiles Immunolocalization and Challenge Studies Using a Recombinant Vibrio cholerae Ghost Expressing Trypanosoma brucei Ca2+ ATPase (TBCA2) Antigen Am J Trop Med Hyg, September 1, 2009; 81(3): 407 - 415. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Jubault, C. Hamon, A. Gravot, C. Lariagon, R. Delourme, A. Bouchereau, and M. J. Manzanares-Dauleux Differential Regulation of Root Arginine Catabolism and Polyamine Metabolism in Clubroot-Susceptible and Partially Resistant Arabidopsis Genotypes Plant Physiology, April 1, 2008; 146(4): 2008 - 2019. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. F. Storz, M. Baze, J. L. Waite, F. G. Hoffmann, J. C. Opazo, and J. P. Hayes Complex Signatures of Selection and Gene Conversion in the Duplicated Globin Genes of House Mice Genetics, September 1, 2007; 177(1): 481 - 500. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. M. Hempe, J. Ory-Ascani, and D. Hsia Genetic Variation in Mouse Beta Globin Cysteine Content Modifies Glutathione Metabolism: Implications for the Use of Mouse Models Experimental Biology and Medicine, March 1, 2007; 232(3): 437 - 444. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. Chen, B. C. McCaig, M. Melotto, S. Y. He, and G. A. Howe Regulation of Plant Arginase by Wounding, Jasmonate, and the Phytotoxin Coronatine J. Biol. Chem., October 29, 2004; 279(44): 45998 - 46007. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
