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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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