Interspecies differences in hepatic Ca2+ -ATPase activity and the effect of cold preservation on porcine liver Ca2+ -ATPase function

Piotr Janicki, Paul E. Wise, Andrey E. Belous, C. Wright Pinson

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The accumulation of intracellular calcium ([Ca2+]i) caused by ischemia-reperfusion during liver transplantation has been implicated as a factor leading to primary graft nonfunction. Plasma membrane (PM) and endoplasmic reticulum (ER) Ca2+ -adenosinetriphosphatases (ATPases) are the primary transporters that maintain [Ca2+]i homeostasis in the liver. We hypothesized that the porcine liver is better than the rat liver as a model for the study of human liver Ca2+ -ATPase activity. We also hypothesized that cold preservation would depress Ca2+ -ATPase activity in the porcine liver. Pig and rat livers were harvested, and human liver samples were obtained from surgical resection specimens. All were preserved with University of Wisconsin solution, and porcine livers were also preserved on ice for 2 to 18 hours. Ca2+ -ATPase activity was measured after incubation with45Ca2+ and adenosine triphosphate in the presence of specific Ca2+ -ATPase inhibitors. Porcine PM and ER Ca2+ -ATPase activities were 0.47 ± 0.03 and 1.57 ± 0.10 nmol of Ca2+/mg of protein/min, respectively. This was not significantly different from human liver, whereas rat liver was significantly greater at 2.60 ± 0.03 and 9.2 ± 0.9 nmol of Ca2+/mg of protein/min, respectively. We conclude that the Ca2+ -ATPase activity in the pig liver is equivalent to that of human liver, and thus, the pig liver is a better model than the rat liver. Cold preservation studies showed a significant decrease in porcine hepatic PM Ca2+ -ATPase activity after 4 hours of storage and near-total inhibition after 12 hours. Porcine hepatic ER Ca2+ -ATPase activity showed a 45% decrease in activity by 12 hours and a 69% decrease by 18 hours. We conclude that cold ischemia at clinically relevant times depresses PM Ca2+ -ATPase more than ER Ca2+ -ATPase activity in pig liver homogenates.

Original languageEnglish (US)
Pages (from-to)132-139
Number of pages8
JournalLiver Transplantation
Volume7
Issue number2
DOIs
StatePublished - Jan 1 2001

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Calcium-Transporting ATPases
Swine
Liver
Endoplasmic Reticulum
Cell Membrane
Cold Ischemia
Ice

All Science Journal Classification (ASJC) codes

  • Surgery
  • Hepatology
  • Transplantation

Cite this

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title = "Interspecies differences in hepatic Ca2+ -ATPase activity and the effect of cold preservation on porcine liver Ca2+ -ATPase function",
abstract = "The accumulation of intracellular calcium ([Ca2+]i) caused by ischemia-reperfusion during liver transplantation has been implicated as a factor leading to primary graft nonfunction. Plasma membrane (PM) and endoplasmic reticulum (ER) Ca2+ -adenosinetriphosphatases (ATPases) are the primary transporters that maintain [Ca2+]i homeostasis in the liver. We hypothesized that the porcine liver is better than the rat liver as a model for the study of human liver Ca2+ -ATPase activity. We also hypothesized that cold preservation would depress Ca2+ -ATPase activity in the porcine liver. Pig and rat livers were harvested, and human liver samples were obtained from surgical resection specimens. All were preserved with University of Wisconsin solution, and porcine livers were also preserved on ice for 2 to 18 hours. Ca2+ -ATPase activity was measured after incubation with45Ca2+ and adenosine triphosphate in the presence of specific Ca2+ -ATPase inhibitors. Porcine PM and ER Ca2+ -ATPase activities were 0.47 ± 0.03 and 1.57 ± 0.10 nmol of Ca2+/mg of protein/min, respectively. This was not significantly different from human liver, whereas rat liver was significantly greater at 2.60 ± 0.03 and 9.2 ± 0.9 nmol of Ca2+/mg of protein/min, respectively. We conclude that the Ca2+ -ATPase activity in the pig liver is equivalent to that of human liver, and thus, the pig liver is a better model than the rat liver. Cold preservation studies showed a significant decrease in porcine hepatic PM Ca2+ -ATPase activity after 4 hours of storage and near-total inhibition after 12 hours. Porcine hepatic ER Ca2+ -ATPase activity showed a 45{\%} decrease in activity by 12 hours and a 69{\%} decrease by 18 hours. We conclude that cold ischemia at clinically relevant times depresses PM Ca2+ -ATPase more than ER Ca2+ -ATPase activity in pig liver homogenates.",
author = "Piotr Janicki and Wise, {Paul E.} and Belous, {Andrey E.} and Pinson, {C. Wright}",
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Interspecies differences in hepatic Ca2+ -ATPase activity and the effect of cold preservation on porcine liver Ca2+ -ATPase function. / Janicki, Piotr; Wise, Paul E.; Belous, Andrey E.; Pinson, C. Wright.

In: Liver Transplantation, Vol. 7, No. 2, 01.01.2001, p. 132-139.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Interspecies differences in hepatic Ca2+ -ATPase activity and the effect of cold preservation on porcine liver Ca2+ -ATPase function

AU - Janicki, Piotr

AU - Wise, Paul E.

AU - Belous, Andrey E.

AU - Pinson, C. Wright

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N2 - The accumulation of intracellular calcium ([Ca2+]i) caused by ischemia-reperfusion during liver transplantation has been implicated as a factor leading to primary graft nonfunction. Plasma membrane (PM) and endoplasmic reticulum (ER) Ca2+ -adenosinetriphosphatases (ATPases) are the primary transporters that maintain [Ca2+]i homeostasis in the liver. We hypothesized that the porcine liver is better than the rat liver as a model for the study of human liver Ca2+ -ATPase activity. We also hypothesized that cold preservation would depress Ca2+ -ATPase activity in the porcine liver. Pig and rat livers were harvested, and human liver samples were obtained from surgical resection specimens. All were preserved with University of Wisconsin solution, and porcine livers were also preserved on ice for 2 to 18 hours. Ca2+ -ATPase activity was measured after incubation with45Ca2+ and adenosine triphosphate in the presence of specific Ca2+ -ATPase inhibitors. Porcine PM and ER Ca2+ -ATPase activities were 0.47 ± 0.03 and 1.57 ± 0.10 nmol of Ca2+/mg of protein/min, respectively. This was not significantly different from human liver, whereas rat liver was significantly greater at 2.60 ± 0.03 and 9.2 ± 0.9 nmol of Ca2+/mg of protein/min, respectively. We conclude that the Ca2+ -ATPase activity in the pig liver is equivalent to that of human liver, and thus, the pig liver is a better model than the rat liver. Cold preservation studies showed a significant decrease in porcine hepatic PM Ca2+ -ATPase activity after 4 hours of storage and near-total inhibition after 12 hours. Porcine hepatic ER Ca2+ -ATPase activity showed a 45% decrease in activity by 12 hours and a 69% decrease by 18 hours. We conclude that cold ischemia at clinically relevant times depresses PM Ca2+ -ATPase more than ER Ca2+ -ATPase activity in pig liver homogenates.

AB - The accumulation of intracellular calcium ([Ca2+]i) caused by ischemia-reperfusion during liver transplantation has been implicated as a factor leading to primary graft nonfunction. Plasma membrane (PM) and endoplasmic reticulum (ER) Ca2+ -adenosinetriphosphatases (ATPases) are the primary transporters that maintain [Ca2+]i homeostasis in the liver. We hypothesized that the porcine liver is better than the rat liver as a model for the study of human liver Ca2+ -ATPase activity. We also hypothesized that cold preservation would depress Ca2+ -ATPase activity in the porcine liver. Pig and rat livers were harvested, and human liver samples were obtained from surgical resection specimens. All were preserved with University of Wisconsin solution, and porcine livers were also preserved on ice for 2 to 18 hours. Ca2+ -ATPase activity was measured after incubation with45Ca2+ and adenosine triphosphate in the presence of specific Ca2+ -ATPase inhibitors. Porcine PM and ER Ca2+ -ATPase activities were 0.47 ± 0.03 and 1.57 ± 0.10 nmol of Ca2+/mg of protein/min, respectively. This was not significantly different from human liver, whereas rat liver was significantly greater at 2.60 ± 0.03 and 9.2 ± 0.9 nmol of Ca2+/mg of protein/min, respectively. We conclude that the Ca2+ -ATPase activity in the pig liver is equivalent to that of human liver, and thus, the pig liver is a better model than the rat liver. Cold preservation studies showed a significant decrease in porcine hepatic PM Ca2+ -ATPase activity after 4 hours of storage and near-total inhibition after 12 hours. Porcine hepatic ER Ca2+ -ATPase activity showed a 45% decrease in activity by 12 hours and a 69% decrease by 18 hours. We conclude that cold ischemia at clinically relevant times depresses PM Ca2+ -ATPase more than ER Ca2+ -ATPase activity in pig liver homogenates.

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