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Titolo:
Lipopolysaccharide alters ecto-ATP-diphosphohydrolase and causes relocation of its reaction product in experimental intrahepatic cholestasis
Autore:
Zinchuk, VS; Okada, T; Seguchi, H;
Indirizzi:
Kochi Med Sch, Dept Anat & Cell Biol, Nanko Ku, Kochi 7838505, Japan KochiMed Sch Kochi Japan 7838505 l Biol, Nanko Ku, Kochi 7838505, Japan
Titolo Testata:
CELL AND TISSUE RESEARCH
fascicolo: 1, volume: 304, anno: 2001,
pagine: 103 - 109
SICI:
0302-766X(200104)304:1<103:LAEACR>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMA-MEMBRANE VESICLES; SALT EXPORT PUMP; RAT-LIVER; CANALICULAR MEMBRANE; ACID-TRANSPORT; HEPATOCYTE; ENDOTOXIN; APYRASE; INACTIVATION; EXPRESSION;
Keywords:
endotoxin; ecto-apyrase; experimental cholestasis; hepatocyte; rat (Sprague Dawley);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Zinchuk, VS Kochi Med Sch, Dept Anat & Cell Biol, Nanko Ku, Okoh Cho, Kochi 7838505, Japan Kochi Med Sch Okoh Cho Kochi Japan 7838505 chi 7838505, Japan
Citazione:
V.S. Zinchuk et al., "Lipopolysaccharide alters ecto-ATP-diphosphohydrolase and causes relocation of its reaction product in experimental intrahepatic cholestasis", CELL TIS RE, 304(1), 2001, pp. 103-109

Abstract

Lipopolysaccharide (LPS), a bacterial endotoxin, exerts profound inflammatory actions toward various tissues and cells. We induced intrahepatic cholestasis in rats by administration of LPS and followed ecto-ATP-diphosphohydrolase (ecto-apyrase) activity in the liver. The activity of the enzyme had decreased to 77% 2 h after injection compared with the activity in control animals. The maximum decrease was detected 24 h after administration. The activity was found to have partially recovered 1 week after injection, but had yet to reach control levels. In contrast to the decrease in ecto-apyraseactivity, there were increases in alkaline phosphatase activity and bilirubin concentration, markers of cholestasis. In response to LPS. the reactionproduct of ecto-apyrase was found to relocate from the canalicular domain of the plasma membrane of hepatocytes, its predominant localization in the liver of intact animals, to the basolateral and sinusoidal domains. The pattern of histochemical reaction indicated modulation of the enzyme activity and changes in trafficking of intracellular proteins. Taken together, our findings showed that LPS administration alters ecto-apyrase and causes relocation of its reaction product from the canalicular domain of the plasma membrane of hepatocytes in the rat. It is suggested that relocation of the reaction product may be a protective mechanism to enable the hepatocytes to withstand the cytokine-induced metabolic perturbations.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/07/20 alle ore 06:22:44