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Gene Review

mlt-7  -  Protein MLT-7

Caenorhabditis elegans

 
 
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Disease relevance of peroxidase

 

High impact information on peroxidase

  • A topology model predicts that the enzyme will utilize cytosolic NADPH to generate reactive oxygen, but the function of the ecto peroxidase domain was unknown [4].
  • Although in insects the evidence indicates that the cross-reaction results from the presence of core alpha1,3-fucosylated N-glycans, the molecular basis for anti-horseradish peroxidase staining in nematodes has been unresolved to date [5].
  • In this study, pressure injection of horseradish peroxidase or nickel lysine into inhibitory motor neurons revealed numerous spines projecting from the main neuronal process toward the neuromuscular surface that then branched and extended fine, longitudinal processes up to 130 microm in length [6].
  • On electron micrographs, the basophilic cells in these clusters appeared to be late-stage basophilic myelocytes, ie, having an increased number of granules, a less-conspicuous Golgi apparatus and rough endoplasmic reticulum, a horseshoe-shaped-to-lobulated nucleus, and reduced peroxidase activity [7].
  • Isoelectrofocusing (IEF) isozyme analysis revealed that peroxidase, esterase and superoxide dismutase activity increased after nematode infection, in roots of resistant lines in comparison with their susceptible parents [8].
 

Anatomical context of peroxidase

 

Associations of peroxidase with chemical compounds

 

Other interactions of peroxidase

  • The enhanced peroxidase and esterase activities may play a role in the lignification of cell walls, which assists in the resistance to penetration by the nematode [17].
  • The effect of Cereal cyst nematode (Heterodera avenae) infection on the expression of putative root defence-related enzymes, peroxidase (PER), esterase (EST) and superoxide dismutase (SOD), was studied in roots of a wheat/Aegilops triuncialis introgression line TR-3531 carrying the Cre7 resistance gene [17].
 

Analytical, diagnostic and therapeutic context of peroxidase

References

  1. Comparative serial analysis of gene expression of transcript profiles of tomato roots infected with cyst nematode. Uehara, T., Sugiyama, S., Masuta, C. Plant Mol. Biol. (2007) [Pubmed]
  2. Relationships among peripheral eosinophilia, eosinophil peroxidase activity, interleukin-5 concentration and faecal nematode egg count during natural, mixed gastrointestinal nematode infection. Doligalska, M., Moskwa, B., Stear, M.J. Vet. Immunol. Immunopathol. (1999) [Pubmed]
  3. Evaluation of "crude" antigen prepared from Taenia saginata for the serological diagnosis of T. saginata cysticercosis in cattle using the enzyme-linked immunosorbent assay (ELISA). Craig, P.S., Rickard, M.D. Zeitschrift für Parasitenkunde (Berlin, Germany) (1980) [Pubmed]
  4. Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox. Edens, W.A., Sharling, L., Cheng, G., Shapira, R., Kinkade, J.M., Lee, T., Edens, H.A., Tang, X., Sullards, C., Flaherty, D.B., Benian, G.M., Lambeth, J.D. J. Cell Biol. (2001) [Pubmed]
  5. Molecular basis of anti-horseradish peroxidase staining in Caenorhabditis elegans. Paschinger, K., Rendic, D., Lochnit, G., Jantsch, V., Wilson, I.B. J. Biol. Chem. (2004) [Pubmed]
  6. The number of morphological synapses between neurons does not predict the strength of their physiological synaptic interactions: a study of dendrites in the nematode Ascaris suum. Angstadt, J.D., Donmoyer, J.E., Stretton, A.O. J. Comp. Neurol. (2001) [Pubmed]
  7. Development of basophils in Mongolian gerbils: formation of basophilic cell clusters in the bone marrow after Nippostrongylus brasiliensis infection. Okada, M., Nawa, Y., Horii, Y., Kitamura, T., Arizono, N. Lab. Invest. (1997) [Pubmed]
  8. Biochemical and genetic studies of two Heterodera avenae resistance genes transferred from Aegilops ventricosa to wheat. Montes, M.J., López-Braña, I., Romero, M.D., Sin, E., Andrés, M.F., Martín-Sánchez, J.A., Delibes, A. Theor. Appl. Genet. (2003) [Pubmed]
  9. Immunization of sheep against parasitic nematodes leads to elevated levels of globule leukocytes in the small intestine lumen. Stankiewicz, M., Pernthaner, A., Cabaj, W., Jonas, W.E., Douch, P.G., Bisset, S.A., Rabel, B., Pfeffer, A., Green, R.S. Int. J. Parasitol. (1995) [Pubmed]
  10. The distribution of concanavalin A binding sites on the intestinal epithelium of the nematodes Ascaris suum and Parascaris equorum. Trimble, J.J., Thompson, S.A. Cell Tissue Res. (1976) [Pubmed]
  11. Immunological detection of alkaline-diaminobenzidine-negativeperoxisomes of the nematode Caenorhabditis elegans purification and unique pH optima of peroxisomal catalase. Togo, S.H., Maebuchi, M., Yokota, S., Bun-Ya, M., Kawahara, A., Kamiryo, T. Eur. J. Biochem. (2000) [Pubmed]
  12. Physiology of two strains of Trichostrongylus colubriformis resistant and susceptible to thiabendazole and mucosal response of experimentally infected rabbits. Mallet, S., Hoste, H. Int. J. Parasitol. (1995) [Pubmed]
  13. The role of dityrosine formation in the crosslinking of CUT-2, the product of a second cuticlin gene of Caenorhabditis elegans. Lassandro, F., Sebastiano, M., Zei, F., Bazzicalupo, P. Mol. Biochem. Parasitol. (1994) [Pubmed]
  14. Metabolism of lipid peroxidation products by the gastro-intestinal nematodes Necator americanus, Ancylostoma ceylanicum and Heligmosomoides polygyrus. Brophy, P.M., Pritchard, D.I. Int. J. Parasitol. (1992) [Pubmed]
  15. Glutathione S-transferases from the gastrointestinal nematode Heligmosomoides polygyrus and mammalian liver compared. Brophy, P.M., Ben-Smith, A., Brown, A., Behnke, J.M., Pritchard, D.I. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (1994) [Pubmed]
  16. Peroxide-supported in-vitro cytochrome P450 activities in Haemonchus contortus. Kotze, A.C. Int. J. Parasitol. (1999) [Pubmed]
  17. Root enzyme activities associated with resistance to Heterodera avenae conferred by gene Cre7 in a wheat/Aegilops triuncialis introgression line. Montes, M.J., López-Braña, I., Delibes, A. J. Plant Physiol. (2004) [Pubmed]
 
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