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F Bosch

Publications and source records attributed to F Bosch.

At least 163 records · Page 9Linked to original sources
PubMed1989

Prostaglandins E2 and F2 alpha affect glycogen synthase and phosphorylase in isolated hepatocytes.

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.

Animals↗
PubMed1989

Insulin controls key steps of carbohydrate metabolism in cultured HT29 colon cancer cells.

Effects of insulin on key steps of carbohydrate metabolism were investigated in cultured HT29 colon cancer cells by two different approaches, i.e. incubation of the cells either in the absence or in the presence of glucose in the medium. In glucose-deprived cells, insulin decreased glycogen breakdown, but did not affect polysaccharide levels when glucose was present. Glycogen synthase became activated after insulin treatment in both conditions, even though the activation was more evident when glucose was omitted. No effect on glycogen phosphorylase activity was evident under our experimental conditions. In cells incubated with glucose, the hormone stimulated in a dose-dependent manner the rates of glucose uptake and lactate release. Concomitantly with the increase in glycolytic rate, insulin caused a strong increase in fructose 2,6-bisphosphate. This effect was not observed in the absence of glucose. It is concluded that the carbohydrate metabolism of cultured HT29 cells responds to insulin, making this biological model suitable for investigations in vitro on the mechanism of insulin action.

Adenocarcinoma↗
PubMed1989

Blocking effect of diltiazem in the isolated rat phrenic hemidiaphragm.

The effects of diltiazem on indirectly and directly elicited twitch were studied in the isolated rat phrenic hemidiaphragm preparation. Diltiazem (30-500 microM) blocked the indirectly elicited twitch response and this effect was not affected by reducing the extracellular calcium from 2.5 to 1.25 mM. An effect on the directly elicited twitch was also observed (100-300 microM). Diltiazem (30-300 microM) blocked the peak tetanic tension and tetanic fade was present. The results were consistent with an action of diltiazem on the nicotinic receptor-ion channel complex.

Animals↗
PubMed1989

The neuromuscular blocking effect of dibekacin and its reversal by Ca2+ and drugs in the isolated rat phrenic-hemidiaphragm preparation.

1. Dibekacin (0.3-3 mM) reduced indirectly elicited twitches in rat phrenic-hemidiaphragm. This effect was potentiated in low extracellular calcium media. 2. The blockade induced by dibekacin (3 mM) could be reversed by calcium (2.5 mM), 3,4-diamino-pyridine (3,4-DAP, 10 microM) or guanidine (3 mM), whereas neostigmine (3 microM), eserine (25 microM) or tetraethylammonium (100 microM) were less potent. 3. Dibekacin (3 mM) blocked directly-elicited twitches. Low concentrations were unable to obtain any effect. 4. It is concluded that dibekacin exerts its blocking action by limiting the calcium entry at motor nerve terminals, but a postsynaptic effect is also present. 3,4-DAP, guanidine and calcium were the most potent drugs in reversing the blockade.

Animals↗
PubMed1989

Control of glycogen synthase and phosphorylase in hepatocytes from diabetic rats. Effects of glucagon, vasopressin, and vanadate.

Although glycogen synthase is present in a highly inactivated state in hepatocytes from streptozocin-induced diabetic rats, glucagon, vasopressin, and vanadate are still able to further decrease the basal activity of the enzyme. This inactivation was observed with the low-to-high glucose 6-phosphate activity ratio assay. The inactivation of glycogen synthase occurred concomitantly with the activation of glycogen phosphorylase. When hepatocytes from diabetic rats were incubated with [32P]phosphate and then with the agents and when the 32P-labeled glycogen synthase was immunoprecipitated, we observed that the 32P bound to the 88,000-Mr subunit increased in all cases. All the [32P]phosphate was located in two cyanogen bromide fragments of the enzyme, indicating that the enzyme was phosphorylated at multiple sites. The fragments were precisely those phosphorylated by glycogenolytic hormones in hepatocytes from normal rats. These results demonstrated that hepatic glycogen synthase, although highly inactive, is under potential hormonal control in diabetes and that the enzyme has not reached its maximal level of phosphorylation. Furthermore, they indicated that vanadate behaves as a glycogenolytic agent regarding its effects on glycogen-metabolizing enzymes in hepatocytes from diabetic rats.

Animals↗
PubMed1989

Acceptability of visual analogue scales in the clinical setting: a comparison with verbal rating scales in postoperative pain.

Pain is the clinical symptom most difficult to evaluate. Although clinical trials methodology have permitted assessment of pain objectively through rating scales, these strategies have not been used in clinical setting. The present study was undertaken to determine if visual analogue scales could be useful in the measurement of postoperative pain in usual medical practice. The study comprised 212 patients with abdominal, orthopedic or gynecological surgical procedures within the previous 24 h. Patients evaluated their pain using a verbal rating scale (VRS) of five points or a visual analogue scale (VAS) of 10 cm. The investigators also evaluated patient pain through a VAS. The results obtained showed that a high correlation between VRS and VAS could be established in all patients (p less than 0.001). The VAS of patients and researchers were also found to be highly correlated (p less than 0.001). When values of each group were compared by pain intensity a total agreement of VAS scores at low pain level could be established, but differences were found at high pain intensity levels, suggesting that physicians scored lower than patients when pain was severe to unbearable. It is concluded that VAS could be a reliable method to assess pain in clinical setting.

Adult↗
PubMed1989

[Analysis of the treatment of postoperative pain at 3 hospitals].

Postoperative pain management protocols have been examined in a total of 212 patients from three Spanish hospitals. Metamizole was the analgesic drug most frequently prescribed (50%) followed by pethidine (18.4%). To a lesser degree, aspirin, pentazocine, lysine acetylsalicylate, paracetamol and buprenorphine were used. Important differences among the hospitals were found when choosing the analgesic. The dosage prescribed varied and in general, drugs were prescribed at lower doses than the daily defined dose (DDD). Intramuscular route was the most used. Only 27.6% of the patients received the prescribed doses and 43.3% received a lower one. This was basically due to a greater interval of dosing. 14.6% of the patients were painless while 25.5% showed intense and unbearable pain. From this study one may conclude that when metamizole is preferably used as an analgesic drug, it is given at a smaller dose than that recommended and in addition, nurses decrease even more the doses. An important number of patients were found with intense pain even though analgesic drugs were given.

Analgesics↗
PubMed1988

Vanadate raises fructose 2,6-bisphosphate concentrations and activates glycolysis in rat hepatocytes.

In rat hepatocytes, vanadate increases fructose 2,6-bisphosphate (Fru-2,6-P2) in a time- and dose-dependent manner, and counteracts the decrease in this metabolite caused by glucagon, forskolin or exogenous cyclic AMP. Vanadate does not directly modify the activity of 6-phosphofructo-2-kinase, even though it can counteract the inactivation of this enzyme caused by glucagon. Furthermore, vanadate raises the yield of 3H2O from [3-3H]glucose, indicating that it increases the flux through 6-phosphofructo-1-kinase. Moreover, vanadate in hepatocytes incubated in the presence of glucose increases the production of both lactate and CO2. Therefore vanadate has insulin-like effects on the glycolytic pathway in rat hepatocytes. These results clearly contrast with our previous observation that vanadate exerts glycogenolytic non-insulin-like effects on glycogen synthase and phosphorylase.

Animals↗
PubMed1988

Glycogen synthase activation by sugars in isolated hepatocytes.

We have investigated the activation by sugars of glycogen synthase in relation to (i) phosphorylase a activity and (ii) changes in the intracellular concentration of glucose 6-phosphate and adenine nucleotides. All the sugars tested in this work present the common denominator of activating glycogen synthase. On the other hand, phosphorylase a activity is decreased by mannose and glucose, unchanged by galactose and xylitol, and increased by tagatose, glyceraldehyde, and fructose. Dihydroxyacetone exerts a biphasic effect on phosphorylase. These findings provide additional evidence proving that glycogen synthase can be activated regardless of the levels of phosphorylase a, clearly establishing that a nonsequential mechanism for the activation of glycogen synthase occurs in liver cells. The glycogen synthase activation state is related to the concentrations of glucose 6-phosphate and adenine nucleotides. In this respect, tagatose, glyceraldehyde, and fructose deplete ATP and increase AMP contents, whereas glucose, mannose, galactose, xylitol, and dihydroxyacetone do not alter the concentration of these nucleotides. In addition, all these sugars, except glyceraldehyde, increase the intracellular content of glucose 6-phosphate. The activation of glycogen synthase by sugars is reflected in decreases on both kinetic constants of the enzyme, M0.5 (for glucose 6-phosphate) and S0.5 (for UDP-glucose). We propose that hepatocyte glycogen synthase is activated by monosaccharides by a mechanism triggered by changes in glucose 6-phosphate and adenine nucleotide concentrations which have been described to modify glycogen synthase phosphatase activity. This mechanism represents a metabolite control of the sugar-induced activation of hepatocyte glycogen synthase.

Adenine Nucleotides↗
PubMed1987

Capillary column gas chromatographic identification of sugars in honey as trimethylsilyl derivatives.

A method for identifying carbohydrates (mono-, di- and trisaccharides) in honey is presented. It is based on the separate preparation of both trimethylsilyl ethers and oxime trimethylsilyl ethers of the sugars followed by their gas chromatographic separation on a fused-silica capillary column coated with OV-101 using temperature programming. From the two chromatograms, the number of peaks given by each derivatized sugar, their relative retention times and peak-area ratios are used for identification. The identities of two unidentified trisaccharide peaks are considered. Quantitative applications to honey sugar analysis are discussed.

Carbohydrates↗
PubMed1987

Glycogenolytic, noninsulin-like effects of vanadate on rat hepatocyte glycogen synthase and phosphorylase.

Vanadate inactivated rat hepatocyte glycogen synthase and activated glycogen phosphorylase in a dose- and time-dependent manner. These effects were observed in hepatocytes from both fasted as well as fed rats. When rat hepatocytes were preincubated with [32P]phosphate and then with vanadate, and the 32P-labeled glycogen synthase was specifically immunoprecipitated, it was observed that vanadate stimulated the phosphorylation of the 88,000-dalton subunit of glycogen synthase. All of the phosphate was located in the same two CNBr fragments of the enzyme which are phosphorylated by glucagon and other glycogenolytic hormones. In cells incubated in a calcium-depleted medium, vanadate was still able to inactivate glycogen synthase but its effects on phosphorylase were essentially lost. These results demonstrate that, in the hepatocyte, vanadate exerts opposite effects than in the adipocyte and skeletal muscle, where vanadate has an insulin-like action.

Animals↗
PubMed1986

Effects of lithium ions on glycogen synthase and phosphorylase in rat hepatocytes.

Incubation of hepatocytes from fasted rats with LiCl provoked a concentration- and time-dependent activation of glycogen synthase. This effect was observed in the absence of glucose in the incubation medium. No changes in the intracellular concentrations of ATP or glucose-6-phosphate were detected. Lithium was also able to activate glycogen synthase in the absence of extracellular calcium. If hepatocytes were incubated with lithium and insulin, an additive effect of both agents on glycogen synthase activity was observed. LiCl was also effective in activating the enzyme in hepatocytes obtained from fed rats. When hepatocytes were incubated with [33P]phosphate and then treated with LiCl, a decrease in the amount of [32P]phosphate incorporated in the enzyme was observed. This dephosphorylation affected two CNBr fragments of the enzyme (CB-2 and CB-1), suggesting that several phosphorylation sites were involved. Lithium was also able to activate glycogen phosphorylase from both fasted and fed rats. Phosphorylase activation was concentration- and time-dependent, either in the presence or absence of calcium in the incubation medium. These findings demonstrate that although lithium appears to mimic the effects of insulin on glycogen synthase activity, its mechanism of action must be different from that of the hormone.

Adenosine Triphosphate↗
PubMed1986

Epidermal growth factor mimics insulin effects in rat hepatocytes.

Epidermal growth factor (EGF) mimicked the effect of insulin to activate glycogen synthase and stimulate glycogen synthesis in isolated rat hepatocytes. Both agents required glucose (greater than 5 mM) and had similar time courses of action. The maximum effect of EGF was approx. 70% of that of insulin, and the half-maximally effective concentrations were 9 nM and 4 nM respectively. Combinations of the two agents produced additive responses. EGF also resembled insulin in its ability to inhibit the effects of 0.1-1.0 nM-glucagon on cyclic AMP and glycogen phosphorylase in hepatocytes. The maximum effect of EGF was approx. 70% of that of insulin, and the half-maximally effective concentrations were approx. 5 nM and 0.5 nM respectively. EGF and insulin inhibited phosphorylase activation by exogenous cyclic AMP, and inhibited cyclic AMP accumulation induced by forskolin. They also inhibited phosphorylase activation provoked by phenylephrine, but not by vasopressin. EGF added alone rapidly activated phosphorylase and increased cytosolic [Ca2+], but the effects were no longer apparent at 5 min and were smaller than those of vasopressin. Insulin did not induce these changes. In hepatocytes previously incubated with myo-[3H]inositol, EGF did not significantly increase myo-inositol 1,4,5-trisphosphate. However, its ability to increase cytosolic [Ca2+] was blocked by neomycin, an inhibitor of phosphatidylinositol bisphosphate hydrolysis. It is concluded that some, but not all, of the effects of EGF in liver are strikingly similar to those exerted by insulin, suggesting that these agents may have some similar mechanisms of action in this tissue.

Animals↗
PubMed1986

Inactivation of basal glycogen synthase by glucagon and epinephrine in hepatocytes from fed rats.

Glucagon and epinephrine promote the inactivation of basal glycogen synthase in hepatocytes isolated from fed rats. However, this effect is only observable when the activation state of glycogen synthase is measured using the low glucose-6-P/high glucose-6-P activity ratio assay. This inactivation is the consequence of an increase in the kinetic parameters (S0.5 for UDP-glucose and M0.5 for glucose-6-P) of the enzyme. Therefore, this work demonstrates these hormones are also able to control glycogen synthase from fed animals.

Animals↗