Vanin-1-/- mice show decreased NSAID- and Schistosoma-induced intestinal inflammation associated with higher gluthathione stores

Journal of Clinical Investigation

Volumn 113, Issue 4, 2004, Pages 591-597

  Martin, Florent ^a   Penet, Marie France ^a   Malergue, Fabrice ^a   Lepidi, Hubert ^b   Dessein, Alain ^a   Galland, Franck ^a   De Reggi, Max ^a   Naquet, Philippe ^a   Gharib, Bouchra ^a  

^a INSERM   (France)

^b CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; MEMBRANE ENZYME; MERCAPTAMINE; NONSTEROID ANTIINFLAMMATORY AGENT; PANTETHEINASE; PANTETHEINE; PANTOTHENIC ACID; THIOL GROUP; UNCLASSIFIED DRUG; VANIN 1; CELL ADHESION MOLECULE; CHEMOKINE; CYCLOOXYGENASE 1; CYCLOOXYGENASE 2; INDOMETACIN; INDUCIBLE NITRIC OXIDE SYNTHASE; ISOENZYME; MEMBRANE PROTEIN; MIP 2 PROTEIN, MOUSE; MIP-2 PROTEIN, MOUSE; NITRIC OXIDE SYNTHASE; PROSTAGLANDIN SYNTHASE; PTGS1 PROTEIN, MOUSE; VNN1 PROTEIN, MOUSE;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CELL ACTIVATION; CONTROLLED STUDY; DISEASE PREDISPOSITION; ENTERITIS; ENZYME ACTIVITY; INFLAMMATORY CELL; MOUSE; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTECTION; PROTEIN FUNCTION; SCHISTOSOMA; ANIMAL; BAGG ALBINO MOUSE; CHEMICALLY INDUCED DISORDER; CYTOLOGY; GENETICS; INFLAMMATION; INTESTINE; METABOLISM; MOUSE MUTANT; PARASITOLOGY; PATHOLOGY; SCHISTOSOMA MANSONI; SURVIVAL RATE;

ANIMALS; ANTI-INFLAMMATORY AGENTS, NON-STEROIDAL; CELL ADHESION MOLECULES; CHEMOKINES; CYCLOOXYGENASE 1; CYCLOOXYGENASE 2; CYSTEAMINE; GLUTAMATE-CYSTEINE LIGASE; GLUTATHIONE; INDOMETHACIN; INFLAMMATION; INTESTINES; ISOENZYMES; MEMBRANE PROTEINS; MICE; MICE, INBRED BALB C; MICE, KNOCKOUT; NITRIC OXIDE SYNTHASE; NITRIC OXIDE SYNTHASE TYPE II; PROSTAGLANDIN-ENDOPEROXIDE SYNTHASES; SCHISTOSOMA MANSONI; SCHISTOSOMIASIS MANSONI; SURVIVAL RATE;

EID: 1642275597     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI200419557     Document Type: Article

References (53)

1. Aurrand-Lions, M., et al. 1996. Vanin-1, a novel GPI-linked perivascular molecule involved in thymus homing. Immunity. 5:391-405.
2. Granjeaud, S., Naquet, P., and Galland, F. 1999. An ESTs description of the new Vanin gene family conserved from fly to human. Immunogenetics. 49:964-972.
3. Galland, F., et al. 1998. Two human genes related to murine vanin-1 are located on the long arm of human chromosome 6. Genomics. 53:203-213.
4. Martin, F., et al. 2001. Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and encode isoforms of pantetheinase ectoenzymes. Immunogenetics. 53:296-306.
5. Mazas, B., Barra, D., Dupre, S., and Pitari, G. 1999. Is pantetheinase the actual identity of mouse and human vanin-1 proteins? FEBS Lett. 461:149-152.
6. Pitari, G., et al. 2000. Pantetheinase activity of membrane-bound Vanin-1: lack of free cysteamine in tissues of Vanin-1 deficient mice. FEBS Lett. 483:149-154.
7. Dupre, S., Graziani, M.T., Rosei, M.A., Fabi, A., and Del Grosso, E. 1970. The enzymatic breakdown of pantethine to pantothenic acid and cystamine. Eur. J. Biochem. 16:571-578.
8. Miller, S.L., and Schlesinger, G. 1993. Prebiotic syntheses of vitamin coenzymes. I. Cysteamine and 2-mercaptoethanesulfonic acid (coenzyme M). J. Mol. Evol. 36:302-307.
9. Garcia, R.A., Hirschberger, L.L., and Stipanuk, M.H. 1988. Measurement of cyst(e)amine in physiological samples by high performance liquid chromatography. Anal. Biochem. 170:432-440.
10. Ida, S., Tanaka, Y., Ohkuma, S., and Kuriyama, K. 1984. Determination of cystamine by high-performance liquid chromatography. Anal. Biochem. 136:352-356.
11. Kataoka, H., Imamura, Y., Tanaka, H., and Makita, M. 1993. Determination of cysteamine and cystamine by gas chromatography with flame photometric detection. J. Pharm. Biomed. Anal. 11:963-969.
12. Ricci, G., Nardini, M., Chiaraluce, R., Dupre, S., and Cavallini, D. 1983. Detection and determination of cysteamine at the nanomole level. J. Appl. Biochem. 5:320-329.
13. 2+-induced cross-linking of membrane proteins in intact human erythrocytes. Biochemistry. 17:2598-2604.
14. Pontremoli, S., Traniello, S., Enser, M., Shapiro, S., and Horecker, B.L. 1967. Regulation of fructose diphosphatase activity by disulfide exchange. Proc. Natl. Acad. Sci. U. S. A. 58:286-293.
15. Namboodiri, M.A., Weller, J.L., and Klein, D.C. 1980. Rapid and reversible activation of aceryl CoA hydrolase in intact pineal cells by disulfide exchange. Biochem. Biophys. Res. Commun. 96:188-195.
16. Ernest, M.J., and Kim, K.H. 1973. Regulation of rat liver glycogen synthetase. Reversible inactivation of glycogen synthetase D by sulfhydryl-disulfide exchange. J. Biol. Chem. 248:1550-1555.
17. Beamer, R.L., Griffith, O.W., Gass, J.D., Anderson, M.E., and Meister, A. 1980. Interaction of L- and D-3-amino-1-chloro-2-pentanone with gamma-glutamylcysteine synthetase. J. Biol. Chem. 255:11732-11736.
18. Lebo, R.V., and Kredich, N.M. 1978. Inactivation of human gamma-glutamylcysteine synthetase by cystamine. Demonstration and quantification of enzyme-ligand complexes. J. Biol. Chem. 253:2615-2623.
19. Griffith, O.W., Larsson, A., and Meister, A. 1977. Inhibition of gamma-glutamylcysteine synthetase by cystamine: an approach to a therapy of 5-oxoprolinuria (pyroglutamic aciduria). Biochem. Biophys. Res. Commun. 79:919-925.
20. Griffith, O.W., and Mulcahy, R.T. 1999. The enzymes of glutathione synthesis: gamma-glutamylcysteine synthetase. Adv. Enzymol. Relat. Areas Mol. Biol. 73:209-267.
21. Troyer, K.L., et al. 2001. Growth retardation, duodenal lesions, and aberrant ileum architecture in triple null mice lacking EGF, amphiregulin, and TGF-alpha. Gastroenterology. 121:68-78.
22. Dessein, A.J., et al. 1999. Severe hepatic fibrosis in Schistosoma mansoni infection is controlled by a major locus that is closely linked to the interferon-gamma receptor gene. Am. J. Hum. Genet. 65:709-721.
23. Lambertucci, J.R., et al. 2000. Schistosoma mansoni: assessment of morbidity before and after control. Acta Trop. 77:101-109.
24. Beck, P.L., et al. 2000. Mechanisms of NSAID-induced gastrointestinal injury defined using mutant mice. Gastroenterology. 119:699-705.
25. Abdallahi, O.M., Hanna, S., De Reggi, M., and Gharib, B. 1999. Visualization of oxygen radical production in mouse liver in response to infection with Schistosoma mansoni. Liver. 19:495-500.
26. Gharib, B., Abdallahi, O.M., Dessein, H., and De Reggi, M. 1999. Development of eosinophil peroxidase activity and concomitant alteration of the antioxidant defenses in the liver of mice infected with Schistosoma mansoni. J. Hepatol. 30:594-602.
27. Pascal, M., et al. 2000. Hyaluronate levels and markers of oxidative stress in the serum of Sudanese subjects at risk of infection with Schistosoma mansoni. Trans. R. Soc. Trop. Med. Hyg. 94:66-70.
28. La Flamme, A.C., Patton, E.A., Bauman, B., and Pearce, E.J. 2001. IL-4 plays a crucial role in regulating oxidative damage in the liver during schistosomiasis. J. Immunol. 166:1903-1911.
29. Wynn, T.A., et al. 1998. IL-10 regulates liver pathology in acute murine Schistosomiasis mansoni but is not required for immune down-modulation of chronic disease. J. Immunol. 160:4473-4480.
30. Naspetti, M., et al. 2000. A novel anti-Ep-CAM antibody to analyze the organization of thymic medulla in autoimmunity. Curr. Top. Microbiol. Immunol. 251:109-117.
31. Liaudet, L., et al. 2000. Protection against hemorrhagic shock in mice genetically deficient in poly(ADP-ribose)polymerase. Proc. Natl. Acad. Sci. U. S. A. 97:10203-10208.
32. Lyons, C.R., Orloff, G.J., and Cunningham, J.M. 1992. Molecular cloning and functional expression of an inducible nitric oxide synthase from a murine macrophage cell line. J. Biol. Chem. 267:6370-6374.
33. Ballou, L.R., Botting, R.M., Goorha, S., Zhang, J., and Vane, J.R. 2000. Nociception in cyclooxygenase isozyme-deficient mice. Proc. Natl. Acad. Sci. U. S. A. 97:10272-10276.
34. Scott, D.J., et al. 2001. Lack of inducible nitric oxide synthase promotes intestinal tumorigenesis in the Apc(Min/+) mouse. Gastroenterology. 121:889-899.
35. Neumann, B., et al. 1999. Mechanisms of acute inflammatory lung injury induced by abdominal sepsis. Int. Immunol. 11:217-227.
36. Konecki, D.S., Brennand, J., Fuscoe, J.C., Caskey, C.T., and Chinault, A.C. 1982. Hypoxanthine-guanine phosphoribosyltransferase genes of mouse and Chinese hamster: construction and sequence analysis of cDNA recombinants. Nucleic Acids Res. 10:6763-6775.
37. Kinoshita, T., Imamura, J., Nagai, H., and Shimotohno, K. 1992. Quantification of gene expression over a wide range by the polymerase chain reaction. Anal. Biochem. 206:231-235.
38. Seelig, G.F., and Meister, A. 1984. Gamma-glutamylcysteine synthetase from erythrocytes. Anal. Biochem. 141:510-514.
39. Tietze, F. 1969. Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal. Biochem. 27:502-522.
40. Cheever, A.W. 1985. Schistosoma japonicum: the pathology of experimental infection. Exp. Parasitol. 59:1-11.
41. Amiri, P., et al. 1992. Tumour necrosis factor alpha restores granulomas and induces parasite egg-laying in schistosome-infected SCID mice. Nature. 356:604-607.
42. Wallace, J.L., et al. 1998. Cyclooxygenase 1 contributes to inflammatory responses in rats and mice: implications for gastrointestinal toxicity. Gastroenterology. 115:101-109.
43. Tanaka, A., Araki, H., Hase, S., Komoike, Y., and Takeuchi, K. 2002. Upregulation of COX-2 by inhibition of COX-1 in the rat: a key to NSAID-induced gastric injury. Aliment. Pharmacol. Ther. 16:90-101.
44. Wolpe, S.D., and Cerami, A. 1989. Macrophage inflammatory proteins 1 and 2: members of a novel superfamily of cytokines. FASEB J. 3:2565-2573.
45. Suzuki, K., et al. 1999. A novel glycosylphosphatidyl inositol-anchored protein on human leukocytes: a possible role for regulation of neutrophil adherence and migration. J. Immunol. 162:4277-4284.
46. Lu, S.C. 1999. Regulation of hepatic glutathione synthesis: current concepts and controversies. FASEB J. 13:1169-1183.
47. Will, Y., et al. 2000. Gamma-glutamyltranspeptidase-deficient knockout mice as a model to study the relationship between glutathione status, mitochondrial function, and cellular function. Hepatology. 32:740-749.
48. Rana, S.V., Allen, T., and Singh, R. 2002. Inevitable glutathione, then and now. Indian J. Exp. Biol. 40:706-716.
49. Lieberman, M.W., et al. 1996. Growth retardation and cysteine deficiency in gamma-glutamyl transpeptidase-deficient mice. Proc. Natl. Acad. Sci. U. S. A. 93:7923-7926.
50. LeGrand, T.S., and Aw, T.Y. 1996. Chronic hypoxia and glutathione-dependent detoxication in rat small intestine. Am. J. Physiol. 270:G725-G729.
51. Griffith, O.W., and Meister, A. 1979. Glutathione: interorgan translocation, turnover, and metabolism. Proc. Natl. Acad. Sci. U. S. A. 76:5606-5610.
52. Huang, C.S., Moore, W.R., and Meister, A. 1988. On the active site thiol of gamma-glutamylcysteine synthetase: relationships to catalysis, inhibition, and regulation. Proc. Natl. Acad. Sci. U. S. A. 85:2464-2468.
53. Karpuj, M.V., et al. 2002. Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine. Nat. Med. 8:143-149.