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Mercury chloride increases hepatic alanine aminotransferase and glucose 6-phosphatase activities in newborn rats in vivo
Lucélia Moraes‑Silva*, Tania Maria Bueno*, Carina Franciscato*, Cláudia Sirlene de Oliveira†, Nilce Coelho Peixoto* and Maria Ester Pereira*†1
*Programa de PsGraduao em Cincias Biolgicas, Bioqumica Toxicolgica, Universidade Federal de Santa Maria, 97105900, Santa Maria, RS, Brasil, and †Departamento de Qumica, Centro de Cincias Naturais e Exatas, Universidade Federal de Santa Maria, 97105900, Santa Maria, RS, Brasil
This work investigated the in vivo and in vitro effects of HgCl2 and ZnCl2 on metabolic enzymes from tissues of young rats to verify whether the physiological and biochemical alterations induced by mercury and prevented by zinc are related to hepatic and renal glucose metabolism. Wistar rats received (subcutaneous) saline or ZnCl2 (27 mg/kg/day) from 3 to 7 days old and saline or HgCl2 (5.0 mg/kg/day) from 8 to 12 days old. Mercury exposure increased the hepatic alanine aminotransferase (∼6-fold) and glucose 6-phosphatase (75%) activity; zinc pre-exposure prevented totally and partially these mercury alterations respectively. In vitro, HgCl2 inhibited the serum (22%, 10 μM) and liver (54%, 100 μM) alanine aminotransferase, serum (53%) and liver (64%) lactate dehydrogenase (10 μM), and liver (53%) and kidney (41%) glucose 6-phosphatase (100 μM) from 10- to 13-day-old rats. The results show that mercury induces distinct alterations in these enzymes when tested in vivo or in vitro as well as when different sources were used. The increase of both hepatic alanine aminotransferase and glucose 6-phosphatase activity suggests that the mercury-exposed rats have increased gluconeogenic activity in the liver. Zinc prevents the in vivo effects on metabolic changes induced by mercury.
Key words: alanine aminotransferase, gluconeogenesis, glucose-6-phosphatase, lactate dehydrogenase, mercuric chloride, young rats, zinc chloride
Abbreviations: ALT, alanine aminotransferase, G6Pase, glucose 6-phosphatase, LDH, lactate dehydrogenase, PBG-synthase, porphobilinogen synthase, Pi, inorganic phosphorus
1To whom correspondence should be addressed (email email@example.com).
Received 30 June 2010/18 January 2012; accepted 14 March 2012
Published as Cell Biology International Immediate Publication 14 March 2012, doi:10.1042/CBI20100475
© The Author(s) Journal compilation © 2012 International Federation for Cell Biology