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Hormone dependence of the L and M isozymes of pyruvate kinase in isolated rat hepatocytes.

作者信息

Gali P, Broer Y, Rosselin G, Hartmann L

出版信息

Biol Cell. 1983;48(2-3):133-41. doi: 10.1111/j.1768-322x.1984.tb00207.x.

DOI:10.1111/j.1768-322x.1984.tb00207.x
PMID:6370353
Abstract

L Pyruvate kinase (LPK) is considered to be the major form in the liver. Two isozymes, LPK and MPK, have been localized in the isolated rat hepatocyte in vitro with an immunocytometric method. MPK is induced by insulin, which also creates a slight stimulation of LPK (at physiological doses) in both fed and fasted animals. Glucagon inhibits LPK in fed animals (the fasting rat is already in a situation of gluconeogenesis and this hormone is ineffective). MPK is insensitive to glucagon, regardless of the nutritional state of the animals. Each PK isozyme is thus controlled predominantly by one of the two hormones, corresponding to a sophisticated regulation of hepatic glycolysis and gluconeogenesis.

摘要

相似文献

1
Hormone dependence of the L and M isozymes of pyruvate kinase in isolated rat hepatocytes.
Biol Cell. 1983;48(2-3):133-41. doi: 10.1111/j.1768-322x.1984.tb00207.x.
2
[Immunocytometric study of pyruvate kinase L in isolated rat hepatocytes: effect of fasting and glucagon].
C R Seances Acad Sci III. 1982 Oct 11;295(5):341-4.
3
[Insulin dependence of pyruvate kinase M in isolated rat hepatocytes].
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Insulin dependence of M2 pyruvate kinase in primary culture of human liver.人肝脏原代培养中M2丙酮酸激酶的胰岛素依赖性
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J Biol Chem. 1976 Jun 25;251(12):3756-62.
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Insulin-like action of proinsulin on rat liver carbohydrate metabolism in vitro.胰岛素原对大鼠肝脏碳水化合物代谢的体外胰岛素样作用。
Diabetes. 1985 May;34(5):415-9. doi: 10.2337/diab.34.5.415.
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Hormonal regulation of L-type pyruvate kinase in rat liver cells in culture.
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