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Seric and hepatic NTPDase and 5′ nucleotidase activities of rats experimentally infected by Fasciola hepatica

Published online by Cambridge University Press:  01 March 2016

PEDRO H. DOLESKI ,
RICARDO E. MENDES ,
DANIELA B. R. LEAL ,
NATHIELI B. BOTTARI ,
MANOELA M. PIVA ,
ESTER S. DA SILVA ,
MATEUS E. GABRIEL ,
NEUBER J. LUCCA ,
CLAITON I. SCHWERTZ  and
PATRÍCIA GIACOMIM
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PEDRO H. DOLESKI
Affiliation:
Department of Microbiology and Parasitology, Universidade Federal de Santa Maria, RS, Brazil
RICARDO E. MENDES
Affiliation:
Laboratory of Veterinary Pathology, Instituto Federal Catarinense (IFC), Concórdia, SC, Brazil
DANIELA B. R. LEAL
Affiliation:
Department of Microbiology and Parasitology, Universidade Federal de Santa Maria, RS, Brazil
NATHIELI B. BOTTARI
Affiliation:
Department of Biochemistry and Molecular Biology, Universidade Federal de Santa Maria, RS, Brazil
MANOELA M. PIVA
Affiliation:
Laboratory of Veterinary Pathology, Instituto Federal Catarinense (IFC), Concórdia, SC, Brazil
ESTER S. DA SILVA
Affiliation:
Laboratory of Veterinary Pathology, Instituto Federal Catarinense (IFC), Concórdia, SC, Brazil
MATEUS E. GABRIEL
Affiliation:
Laboratory of Veterinary Pathology, Instituto Federal Catarinense (IFC), Concórdia, SC, Brazil
NEUBER J. LUCCA
Affiliation:
Laboratory of Veterinary Pathology, Instituto Federal Catarinense (IFC), Concórdia, SC, Brazil
CLAITON I. SCHWERTZ
Affiliation:
Laboratory of Veterinary Pathology, Instituto Federal Catarinense (IFC), Concórdia, SC, Brazil
PATRÍCIA GIACOMIM
Affiliation:
Laboratory of Veterinary Pathology, Instituto Federal Catarinense (IFC), Concórdia, SC, Brazil
VERA M. MORSCH
Affiliation:
Department of Biochemistry and Molecular Biology, Universidade Federal de Santa Maria, RS, Brazil
MARIA R. C. SCHETINGER
Affiliation:
Department of Biochemistry and Molecular Biology, Universidade Federal de Santa Maria, RS, Brazil
MATHEUS D. BALDISSERA
Affiliation:
Department of Microbiology and Parasitology, Universidade Federal de Santa Maria, RS, Brazil
ALEKSANDRO S. DA SILVA*
Affiliation:
Department of Biochemistry and Molecular Biology, Universidade Federal de Santa Maria, RS, Brazil Department of Animal Science, Universidade do Estado de Santa Catarina (UDESC), Chapecó, SC, Brazil
*
*Corresponding author. Department of Animal Science, Universidade do Estado de Santa Catarina (UDESC), Chapecó, SC, Brazil. E-mail: [email protected]
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Summary

The enzymatic activities of NTPDase and 5′nucleotidase are important to regulate the concentration of adenine nucleotides, known molecules involved in many physiological functions. Therefore, the objective of this study was to evaluate the activity of NTPDase and 5′nucleotidase in serum and liver tissue of rats infected by Fasciola hepatica. Rats were divided into two groups: uninfected control and infected. NTPDase activity for adenosine triphosphate (ATP) and ADP substrates in the liver was higher compared with the control group at 15 days post-infection (PI), while seric activity was lower. In addition, seric and hepatic samples did not show changes for 5′nucleotidase activity at this time. On the other hand, either NTPDase or 5′nucleotidase activities in liver homogenate and serum were higher at 87 days PI. Early in the infection, low NTPDase activity maintains an increase of ATP in the bloodstream in order to activate host immune response, while in hepatic tissue it decreases extracellular ATP to maintain a low inflammatory response in the tissue. As stated, higher NTPDase and 5′nucleotidase activities 87 days after infection in serum and tissue, probably results on an increased concentration of adenosine molecule which stimulates a Th2 immune response. Thus, it is possible to conclude that F. hepatica infections lead to different levels of nucleotide degradation when considering the two stages of infection studied, which influences the inflammatory and pathological processes developed by the purinergic system.

Keywords

ATPadenosineFasciolosisNTPDase5'nucleotidase
Type
Research Article
Information
Parasitology , Volume 143 , Issue 5 , April 2016 , pp. 551 - 556
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Copyright
Copyright © Cambridge University Press 2016 

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References

REFERENCES

Baldissera, M. D., Mendes, R. E. and Da Silva, A. S. (2015). Activity of cholinesterases, pyruvate kinase and adenosine deaminase in rats experimentally infected by Fasciola hepatica: influences of these enzymes on inflammatory response and pathological findings. Pathology Research and Practice 211, 871–876.CrossRefGoogle ScholarPubMed
Barankiewicz, J., Dosch, H. M. and Cohen, A. (1988). Extracellular nucleotide catabolism in human B and T lymphocytes. The source of adenosine production. Journal of Biological Chemistry 263, 7094–7098.CrossRefGoogle Scholar
Borowiec, A., Lechward, K., Tkacz-Stachowska, K. and Skladanowski, A. C. (2006). Adenosine as a metabolic regulator of tissue function: production of adenosine by cytoplasmic 5'-nucleotidases. Acta Biochimica Polonica 53, 269–278.CrossRefGoogle ScholarPubMed
Bours, M., Swennen, E., Di Virgilio, F., Cronstein, B. N. and Dagnelie, P. C. (2006). Adenosine 5′triphosphate and adenosine as endogenous signaling molecules in immunity and inflammation. Pharmacology and Therapeutics 112, 358–404.CrossRefGoogle ScholarPubMed
Bradford, M. M. (1976). A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein–dye binding. Analytical Biochemistry 72, 248–254.CrossRefGoogle Scholar
Burnstock, G. and Verkhratsky, A. (2010). Long-term (trophic) purinergic signaling: purinoceptors control cell proliferation, differentiation and death. Cell Death Disease 1, e9.CrossRefGoogle ScholarPubMed
Chan, K. M., Delfert, D. and Junger, K. D. (1986). A direct colorimetric assay for the Ca2+ – ATPase activity. Analytical Biochemistry 157, 375–380.CrossRefGoogle Scholar
Corriden, R. and Insel, P. A. (2010). Basal release of ATP: an autocrine–paracrine mechanism for cell regulation. Science Signaling 3, re1.CrossRefGoogle ScholarPubMed
Fausther, M., Lecka, J., Soliman, E., Kauffestein, G., Pelletier, J., Sheung, N., Dranoff, J. A. and Sévigny, J. (2011). Coexpression of ecto-5=−nucleotidase/CD73 with specific NTPDases differentially regulates adenosine formation in the rat liver. American Journal Physiology Gastrointestinal Liver Physiology 302, G447–G459.CrossRefGoogle ScholarPubMed
Flynn, R. J., Mulcahy, G. and Elsheikha, H. M. (2010). Coordinating innate and adaptive immunity in Fasciola hepatica infection: implications for control. Veterinary Parasitology 169, 235–240.CrossRefGoogle ScholarPubMed
Gressler, L. T., Da Silva, A. S., Oliveira, C. B., Schafer, A. S., Aires, A. R., Rocha, J. F. X., Tonin, A. A., Schirmbeck, G. H., Casali, E. A., Lopes, S. T. A., Leal, M. L. R. and Monteiro, S. G. (2014). Experimental infection by Haemonchus contortus in lambs: influence of disease on purine levels in serum. Parasitology 141, 898–903.CrossRefGoogle ScholarPubMed
Guasconi, L., Chiappelo, L. S. and Masih, D. T. (2015). Fasciola hepatica excretory–secretory products induce CD4+T cell anergy via selective up-regulation of PD-L2 expression on macrophages in a Dectin-1 dependent way. Immunobiology 220, 934–939.CrossRefGoogle Scholar
Junger, W. G. (2011). Immune cell regulation by autocrine purinergic signalling. Nature Reviews 11, 201.Google ScholarPubMed
Mas-Coma, S., Bargues, M. D. and Valero, M. A. (2005). Fascioliasis and other plant-borne trematode zoonoses. International Journal for Parasitology 35, 1255–1278.CrossRefGoogle ScholarPubMed
Mendes, E. A., Mendes, T. A. O., Santos, S. L., Menezes-Souza, D., Bartholomeu, D. C., Martins, I. V. F., Silva, L. M. and Lima, W. S. L. (2013). Expression of IL-4, IL-10 and IFN- in the liver tissue of cattle that are naturally infected with Fasciola hepatica . Veterinary Parasitology 195, 177–182.CrossRefGoogle ScholarPubMed
Nyindo, M. and Lukambagire, A. (2015). Fascioliasis: an ongoing zoonotic trematode infection. BioMed Research International 2015, 786195.CrossRefGoogle ScholarPubMed
Oses, J. P., Cardoso, C. M., Germano, R. A., Kirst, I. B., Rucker, B., Furstenau, C. R., Wink, M. R., Bonan, C. D., Battastini, A. M. and Sarkis, J. J. (2004). Soluble NTPDase: an additional system of nucleotide hydrolysis in rat blood serum. Life Sciences 74, 3275–3284.CrossRefGoogle ScholarPubMed
Ralevic, V. and Burnstock, G. (1998). Receptors for purines and pyrimidines. Pharmacology Review 50, 413–492.Google ScholarPubMed
Rosemberg, D. B., Rico, E. P., Langoni, A. S., Spinelli, J. T., Pereira, T. C., Dias, R. D., Souza, D. O., Bonan, C. D. and Bogo, M. R. (2010). NTPDase family in zebrafish: nucleotide hydrolysis, molecular identification and gene expression profiles in brain, liver and heart. Comparative Biochemistry and Physiology B 155, 230–240.CrossRefGoogle ScholarPubMed
Trautmann, A. (2009). Extracellular ATP in the immune system: more than just a “danger signal”. Science Signaling 2, e6.CrossRefGoogle ScholarPubMed
Zimmermman, H. (2000). Extracellular metabolism of ATP and others nucleotides. Naunyn-Schmiedeberg's Archives of Pharmacology 362, 299–309.CrossRefGoogle Scholar