Hormonal control of glycogenolysis in parenchymal liver cells by Kupffer and endothelial liver cells.

Casteleijn, Eric; Kuiper, Johan; Rooij, H C van; Kamps, Jan A. A. M.; Koster, J.F.; Berkel, Theo J van

doi:10.1016/s0021-9258(18)69124-0

Cited by 93 publications

(2 citation statements)

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“…Maximal inactivation of glycogen synthase occurred at about 5 min, and activation of phosphorylase reached a peak at about 2 min, indicating a rapid response of the glycogenolytic process. The halfmaximal concentration of prostaglandins affecting both enzymes was 1 ,UM, in agreement with the concentrations of prostaglandins reported to stimulate glucose output in perfused rat livers and hepatocytes [3][4][5][6][7]. This concentration seems rather high for a biological effect.…”

Section: Discussionsupporting

confidence: 86%

“…It has been shown recently that prostaglandins are able to stimulate glycogenolysis in perfused rat liver [3][4][5] or in parenchymal liver cells [5][6][7]. Moreover, it has been proposed that prostaglandins may be the mediators of the effects of several agents, such as 4,f-phorbol 12,/-myristate 13a-acetate and platelet-activating factor [5,[8][9][10] on hepatic glucose metabolism through an intercellular communication mechanism.…”

Section: Introductionmentioning

confidence: 99%

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Prostaglandins E2 and F2α affect glycogen synthase and phosphorylase in isolated hepatocytes

Gómèz-Foix

Rodríguez‐Gil

Guinovart

et al. 1989

Biochemical Journal

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Prostaglandin E2 (PGE2) and prostaglandin F2 alpha (PGF2 alpha) inactivated glycogen synthase and activated glycogen phosphorylase in rat hepatocytes in a dose- and time-dependent manner. These effects were dependent on the presence of Ca2+ in the incubation medium. When glycogen synthase was immunoprecipitated from cells incubated with [32P]Pi and then treated with PGE2 or PGF2 alpha, there was increased phosphorylation of the 88 kDa subunit of the enzyme. This phosphorylation affected two CNBr fragments of the glycogen synthase, CB-1 and CB-2, the same fragments that are phosphorylated by different glycogenolytic hormones. No phosphorylation of glycogen synthase by prostaglandins was observed in the absence of Ca2+. Thus the effect of PGE2 and PGF2 alpha on these glycogen-metabolizing enzymes supports a role for regulation by prostaglandins of glucose metabolism in parenchymal liver cells.

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Section: Discussionsupporting

confidence: 86%

Section: Introductionmentioning

confidence: 99%

Prostaglandins E2 and F2α affect glycogen synthase and phosphorylase in isolated hepatocytes

Gómèz-Foix

Rodríguez‐Gil

Guinovart

et al. 1989

Biochemical Journal

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Primary role of Kupffer cell–hepatocyte communication in the expression of oxidative stress in the post-ischaemic liver

Cutrìn

Llesuy

Boveris

1998

Cell Biochem. Funct.

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It has been reported that hepatocyte metabolism and function can be modulated by the activated Kupffer cell through the release of different biomolecules like cytokines, eicosanoids, oxygen free radicals and enzymes. In relation to these paracrine factors involved in circuits of intercellular communication, the existence of a hepatic oxygen sensor located in the Kupffer cell has been postulated. According to this postulate the oxygen metabolism of the liver parenchymal cells could be under the control of the Kupffer cells. In order to study the role of the Kupffer cell in the reperfusion syndrome of the liver, a lobular ischaemia-reperfusion model was performed in rats with or without previous treatment with gadolinium chloride to block Kupffer cell function. Spontaneous chemiluminescence of the liver surface, oxygen uptake by tissue slices and tertbutyl hydroperoxide-initiated chemiluminescence determinations were performed to evaluate the oxygen metabolism and the oxy-radical generation by the liver. The lower basal photoemission, in parallel with a lower basal oxygen uptake registered in the hepatic lobes from the animals pretreated with gadolinium chloride clearly indicates that the gadolinium chloride-dependent functional inhibition of Kupffer cell leads to a downregulation of oxygen metabolism by the liver. Moreover, the intensity of oxidative stress exhibited by the postischaemic lobes appears to be closely linked with the Kupffer cell activity. On the basis of the data obtained we propose that a paracrine circuit between activated Kupffer cell and hepatocytes is an early key event in the induction of postischaemic oxidative stress in the liver. Furthermore the interference with the mitochondrial electron flow by some biomolecules released from the activated Kupffer cell, such as tumour necrosis factor, interleukins, eicosanoids, etc., would increase the rate of generation of reactive oxygen species by the inhibited mitochondrial respiratory chain.

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Diabetes in chronic liver disease: from old concepts to new evidence

Picardi

D’Avola

Gentilucci

et al. 2006

Diabetes Metab. Res. Rev.

102

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SummaryThe liver is one of the principal organs involved in glucose metabolism together with skeletal muscle and adipose tissue. A link between diabetes and chronic liver disease (CLD) was first observed in the early half of the last century, but to date several questions remain unsolved. Altered glucose tolerance has been well described in alcoholic CLD, non-alcoholic fatty liver disease, chronic hepatitis C and portal hypertension. Moreover, insulin resistance is assuming an ever-growing importance in CLD; chronic hepatitis C has recently been proposed as a metabolic disease and insulin sensitivity as a predictive factor for liver fibrosis.CLD is also complicated by acquired growth hormone (GH) resistance, characterized by low concentrations of insulin-like growth factor-1 (IGF-1) with respect to normal or elevated GH levels. GH resistance in CLD is determined by several factors, including malnutrition, impaired liver function and reduced expression of hepatic GH receptors. We recently described the possible role of tumour necrosis factor-alpha (TNF-α) in blunting the hepatic response to GH in patients with chronic hepatitis C. The role of GH in impaired glucose metabolism is well known, and recent evidence suggests a receptor and/or post-receptor modulation of insulin signalling. Moreover, as in other chronic inflammatory conditions, pro-inflammatory cytokines may directly modulate the signal cascade that follows insulin binding to its receptor in the course of CLD.In this review, the proposed links between impaired glucose tolerance and CLD are analysed, special emphasis being focussed on the most recent findings concerning the interplay of chronic inflammation, GH resistance and insulin resistance.

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Hormonal control of glycogenolysis in parenchymal liver cells by Kupffer and endothelial liver cells.

Cited by 93 publications

References 24 publications

Prostaglandins E2 and F2α affect glycogen synthase and phosphorylase in isolated hepatocytes

Prostaglandins E2 and F2α affect glycogen synthase and phosphorylase in isolated hepatocytes

Primary role of Kupffer cell–hepatocyte communication in the expression of oxidative stress in the post-ischaemic liver

Diabetes in chronic liver disease: from old concepts to new evidence

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