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Reduced protein kinase C activity and endogenous protein phosphorylation in ethionine-induced fatty liver in cows

  • Biochemistry
  • Published:
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Abstract

Protein kinase C (PKC) activity was evaluated and the phosphorylation of its endogenous substrates was explored in fatty liver induced by administration of ethionine (an analogue of methionine) to cows in order to assess the relevance of PKC-dependent phosphorylation in the development of fatty liver. PKC activity was decreased in both the cytosolic and the total particulate fractions from fatty livers, compared to the corresponding fractions from control liver. The mode of activation by the PKC cofactors (1-oleoyl-2-acetyl-sn-glycerol, 12-O-tetradecanoylphorbol-13-acetate, phosphatidylserine and Ca2+) was similar in both control and fatty livers, suggesting a quantitative but not a qualitative change in PKC in fatty liver. At least three substrate proteins (34 kDa, 26 kDa and 19 kDa) were found in the cytosolic fraction and their phosphorylation was reduced in fatty liver. These results suggest that impairment of the signal transduction pathway mediated by PKC is involved in the pathogenesis of fatty liver in cows.

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Abbreviations

ATP:

adenosine triphosphate

EGTA:

ethylene glycol bis(β-aminoethylether)-N,N,N′,N′-tetraacetic acid

NEFA:

non-esterified fatty acid

OAG:

1-oleoyl-2-acetyl-sn-glycerol

PKC:

protein kinase C

PS:

phosphatidylserine

SDS-PAGE:

sodium dodecyl sulphate-polyacrylamide gel electrophoresis

TG:

triglyceride

TPA:

12-O-tetradecanoylphorbol-13-acetate

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  1. Laboratory of Biochemistry, National Institute of Animal Health, 305, Tsukuba, Ibaraki, Japan

    N. Katoh

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Katoh, N. Reduced protein kinase C activity and endogenous protein phosphorylation in ethionine-induced fatty liver in cows. Vet Res Commun 18, 423–432 (1994). https://doi.org/10.1007/BF01839418

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  • DOI: https://doi.org/10.1007/BF01839418

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