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Biomedical subjects

J Kuiper

Publications and source records attributed to J Kuiper.

At least 91 records · Page 5Linked to original sources
PubMed1988

Characterization of the interaction in vivo of tissue-type plasminogen activator with liver cells.

The interaction in vivo of 125I-labeled tissue-type plasminogen activator (t-PA) with the rat liver and the various liver cell types was characterized. Intravenously injected 125I-t-PA was rapidly cleared from the plasma (t1/2 = 1 min), and 80% of the injected dose associated with the liver. After uptake, t-PA was rapidly degraded in the lysosomes. The interaction of 125I-t-PA with the liver could be inhibited by preinjection of the rats with ovalbumin or unlabeled t-PA. The intrahepatic recognition site(s) for t-PA were determined by subfractionation of the liver in parenchymal, endothelial, and Kupffer cells. It can be calculated that parenchymal cells are responsible for 54.5% of the interaction of t-PA with the liver, endothelial cells for 39.5%, and Kupffer cells for only 6%. The association of t-PA with parenchymal cells was not mediated by a carbohydrate-specific receptor and could only be inhibited by an excess of unlabeled t-PA, indicating involvement of a specific t-PA recognition site. The association of t-PA with endothelial cells could be inhibited 80% by the mannose-terminated glycoprotein ovalbumin, suggesting that the mannose receptor plays a major role in the recognition of t-PA by endothelial liver cells. An excess of unlabeled t-PA inhibited the association of 125I-t-PA to endothelial liver cells 95%, indicating that an additional specific t-PA recognition site may be responsible for 15% of the high affinity interaction of t-PA with this liver cell type. It is concluded that the uptake of t-PA by the liver is mainly mediated by two recognition systems: a specific t-PA site on parenchymal cells and the mannose receptor on endothelial liver cells. It is suggested that for the development of strategies to prolong the half-life of t-PA in the blood, the presence of both types of recognition systems has to be taken into account.

Animals↗
PubMed1988

Conditioned media of Kupffer and endothelial liver cells influence protein phosphorylation in parenchymal liver cells. Involvement of prostaglandins.

The possible role of Kupffer and endothelial liver cells in the regulation of parenchymal-liver-cell function was assessed by studying the influence of conditioned media of isolated Kupffer and endothelial cells on protein phosphorylation in isolated parenchymal cells. The phosphorylation state of three proteins was selectively influenced by the conditioned media. The phosphorylation state of an Mr-63,000 protein was decreased and the phosphorylation state of an Mr-47,000 and an Mr-97,000 protein was enhanced by these media. These effects could be mimicked by adding either prostaglandin E1, E2 or D2. Both conditioned media and prostaglandins stimulated the phosphorylase activity in parenchymal liver cells, suggesting that the Mr-97,000 phosphoprotein might be phosphorylase. Parenchymal liver cells secrete a phosphoprotein of Mr-63,000 and pI 5.0-5.5. The phosphorylation of this protein is inhibited by Kupffer- and endothelial-liver-cell media, and prostaglandins E1, E2 and D2 had a similar effect. The data indicate that Kupffer and endothelial liver cells secrete factors which influence the protein phosphorylation in parenchymal liver cells. This forms further evidence that products from non-parenchymal liver cells, in particular prostaglandin D2, might regulate glucose homoeostasis and/or other specific metabolic processes inside parenchymal cells. This stresses the concept of cellular communication inside the liver as a way by which the liver can rapidly respond to extrahepatic signals.

Animals↗
PubMed1988

Endotoxin stimulates glycogenolysis in the liver by means of intercellular communication.

Escherichia coli endotoxin (lipopolysaccharide) was shown to increase glycogenolysis in the perfused liver 2-3-fold. In isolated parenchymal liver cells, however, endotoxin did not influence glycogenolysis, whereas stimulation by endotoxin of glycogenolysis in the perfused liver could be blocked by aspirin. This suggests that the effect of endotoxin on liver glycogenolysis is mediated by eicosanoids. The amount of prostaglandin D2 (which is the major prostanoid formed by Kupffer cells) in the liver perfusates was increased 5-fold upon endotoxin addition, with a time course which preceded the increase in glucose output. It is concluded that endotoxin stimulates glycogenolysis in the liver by stimulating prostaglandin D2 release from Kupffer cells, with a subsequent activation of glycogenolysis in parenchymal liver cells. This mechanism of intercellular communication may be designed to provide the carbohydrate source of energy necessary for the effective destruction of invaded microorganisms, by phagocytic cells, including the Kupffer cells.

Animals↗
PubMed1988

Identification of prostaglandin D2 as the major eicosanoid from liver endothelial and Kupffer cells.

The capacity of freshly isolated endothelial, Kupffer and parenchymal rat liver cells to produce eicosanoids from [1-14C]arachidonic acid was investigated in order to determine the relative importance of these cells to total liver eicosanoid production. Based upon the total formation of [1-14C]arachidonate metabolites in the liver, it can be calculated that Kupffer and endothelial cells are responsible for 65 and 23%, respectively, of the total amount of eicosanoids produced by the liver. Consequently, parenchymal liver cells, representing 92.5% of the total liver mass, contribute only 12% to the total liver production of eicosanoids. The main product of Kupffer cells was prostaglandin D2 (PGD2), representing 55% of the total amount of eicosanoids produced. Liver endothelial cells produced about 4-times less eicosanoids (per mg cell protein) than Kupffer cells, and PGD2 was also the main product of these cells (44%). The production of eicosanoids by parenchymal cells was lower by a factor of 180 (per mg cell protein) than that in Kupffer cells. Besides the ability to form eicosanoids from added 14C-labeled arachidonic acid, Kupffer and endothelial liver cells were also able to produce significant amounts of PGD2 (the main liver prostaglandin) from endogenous arachidonic acid, as determined by a radioimmunoassay. It is concluded that inside the liver, Kupffer cells together with endothelial cells are of major importance in the production of eicosanoids, while the parenchymal cells may be considered metabolic target cells for these products, as indicated by the finding that the major liver prostaglandin, PGD2, could stimulate the glucose output in isolated parenchymal cells.

Animals↗
PubMed1988

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

Conditioned media of isolated Kupffer and endothelial liver cells were added to incubations of parenchymal liver cells, in order to test whether secretory products of Kupffer and endothelial liver cells could influence parenchymal liver cell metabolism. With Kupffer cell medium an average stimulation of glucose production by parenchymal liver cells of 140% was obtained, while endothelial liver cell medium stimulated with an average of 127%. The separation of the secretory products of Kupffer and endothelial liver cells in a low and a high molecular weight fraction indicated that the active factor(s) had a low molecular weight. Media, obtained from aspirin-pretreated Kupffer and endothelial liver cells, had no effect on the glucose production by parenchymal liver cells. Because aspirin blocks prostaglandin synthesis, it was tested if prostaglandins could be responsible for the effect of media on parenchymal liver cells. It was found that prostaglandin (PG) E1, E2, and D2 all stimulated the glucose production by parenchymal liver cells, PGD2 being the most potent. Kupffer and endothelial liver cell media as well as prostaglandins E1, E2, and D2 stimulated the activity of phosphorylase, the regulatory enzyme in glycogenolysis. The data indicate that prostaglandins, present in media from Kupffer and endothelial liver cells, may stimulate glycogenolysis in parenchymal liver cells. This implies that products of Kupffer and endothelial liver cells may play a role in the regulation of glucose homeostasis by the liver.

Alprostadil↗
PubMed1988

Prostaglandin D2 mediates the stimulation of glycogenolysis in the liver by phorbol ester.

The tumour-promoting phorbol ester, phorbol 12-myristate 13-acetate (PMA), when added to the perfused liver, stimulates glycogenolysis 2-fold. This stimulation is not seen when aspirin is present in the perfusion medium. In isolated parenchymal liver cells. PMA is not able to stimulate glycogenolysis, suggesting that its effect on glycogenolysis might be indirect and depends on the presence of the non-parenchymal liver cell types. To test the possible operation of an indirect mechanism, we measured the amount of prostaglandin (PG) D2 in liver perfusates. After addition of PMA, the amount of PGD2 is doubled, in parallel with the increase in glycogenolysis. Glycogenolysis in both isolated parenchymal liver cells and perfused liver could be stimulated by the addition of PGD2. Our data indicate that stimulation of glycogenolysis in the liver by PMA may be mediated by non-parenchymal liver cells, which produce PGD2 in response to PMA. Subsequently PGD2 activates glycogenolysis in the parenchymal liver cells. The intercellular communication inside the liver in response to PMA adds a new mechanism to the complex regulation of glucose homoeostasis by the liver.

Animals↗
PubMed1988

Regulation of liver metabolism by intercellular communication.

The regulation of liver metabolism by intercellular communication was assessed by studying the effect of conditioned media of Kupffer and liver endothelial cells on protein synthesis, protein phosphorylation and glycogenolysis in parenchymal cells. Kupffer and endothelial cell-conditioned media enhanced the rate of protein synthesis of parenchymal cells by a factor of 1.7-1.9. The phosphorylation state of only three specific parenchymal cell proteins was influenced by the conditioned media. One, the MW 97,000 band appeared to be phosphorylase and it was found that in parallel with an enhancement of the activity of phosphorylase the glucose output by parenchymal cells could be stimulated. The effects of the conditioned media could be mimicked by prostaglandin E1, E2 and D2, whereas the pretreatment of non-parenchymal cells with aspirin abolished the stimulatory effect of these cells on the glucose output by parenchymal cells. The data indicate that prostaglandins from Kupffer and endothelial cells, mainly PGD2, can influence glucose release from parenchymal cells. The physiological importance of cellular communication was further assessed in a liver perfusion system. The tumor promoting phorbol ester PMA stimulated glycogenolysis in the perfused liver two-fold. This stimulation was blocked by the presence of aspirin. PMA is inactive on isolated parenchymal cells. Addition of PMA to the perfused liver appears to enhance the output of PGD2 in parallel with the stimulation of the glucose output. Addition of prostaglandin D2 itself could also stimulate the glucose output in the perfused liver. Our data indicate that the stimulation of glycogenolysis in the liver by PMA is mediated by non-parenchymal cells which produce PGD2 in response to PMA, leading subsequently to activation of the phosphorylase system in the parenchymal cells. It seems possible also that the tumor-promoting activity of PMA on liver will be mediated by a primary interaction with non-parenchymal cells. It is concluded that the occurrence of intercellular communication inside the liver in response to activation of non-parenchymal cells adds a new mechanism to the complex regulation of liver metabolism which may be relevant under normal and pathological conditions.

Animals↗
PubMed1984

Fate and effects of 4-chlorophenol and 2,4-dichlorophenol in marine plankton communities in experimental enclosures.

The fate and effects of 4-chlorophenol (4CP) and 2,4-dichlorophenol (DCP) added to North Sea coastal plankton communities enclosed by large plastic bags were studied in three experiments of 4 to 6 weeks duration. The biodegradation of the compounds was studied in laboratory experiments using water from the enclosed ecosystems. 4CP and DCP, added at initial concentrations of 0.1-1.0 mg X liter-1, disappeared from the water in the enclosures in 5 to 23 days, 4CP generally being the less persistent. Degradation rates were generally comparable to those found in laboratory tests with the same water. 4CP was removed by biodegradation, and DCP was probably removed by a combination of biodegradation, photodegradation, and/or chemical degradation. Results indicated that biodegradation rates could be limited by lack of inorganic nutrients, leading to much lower degradation rates than would be expected from routine laboratory tests. Faster degradation after repeated addition of 4CP showed adaption of the bacterial community. Addition of 0.3 mg liter-1 4CP or DCP inhibited the phytoplankton growth rate slightly. The 1 mg liter-1 4CP or DCP inhibited the phytoplankton, changed the species composition, and also influenced the zooplankton. In two of the three experiments 1 mg liter-1 DCP resulted in a temporary lowering of bacterial numbers following the addition. In one experiment inhibitory effects were found after 4CP and DCP had disappeared from the water, pointing to the formation of a more toxic intermediate during the degradation of these compounds. The laboratory tests also indicated the formation of relatively stable intermediates. The concentrations causing the effects in the different bag experiments were quite similar. This indicates that, although the development of the plankton communities during the different experiments was different, the concentrations resulting in ecological effects are quite reproducible.

Animals↗
PubMed1984

Fate and effects of 3,4-dichloroaniline (DCA) in marine plankton communities in experimental enclosures.

The fate and effects of single doses of 3,4-dichloroaniline (DCA) on North Sea coastal plankton communities enclosed by large plastic bags (contents 1.5 m3) were studied in two experiments lasting 5 and 6 weeks, respectively. The biodegradation of DCA was also studied in laboratory experiments, which were carried out simultaneously, using water from the enclosed model ecosystems. DCA was not degraded in the laboratory tests and probably also not degraded in the enclosed plankton communities, although concentrations in the water decreased during the experiments. This decrease appeared to be partly caused by diffusion of DCA through the walls of the enclosures. After the addition of single doses of 2, 10, and 25 microgram liter-1 DCA no effects on the enclosed plankton community could be detected. The addition of 0.1 mg liter-1 DCA had a clear influence on the species composition and the biomass development of the phytoplankton, changed the relative species composition of the zooplankton, and resulted in lower numbers of bacteria. In addition to these effects 1 mg liter-1 DCA limited the phytoplankton growth and resulted in mortality and inhibition of growth of the copepods.

Aniline Compounds↗