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At least 1,225 records · Page 68Linked to original sources
PubMed1993

Transfected cGMP-dependent protein kinase suppresses calcium transients by inhibition of inositol 1,4,5-trisphosphate production.

cGMP is a key regulatory molecule in visual transduction, integration of neuronal response to excitatory neurotransmitters, relaxation of smooth muscle, intestinal secretion of water and salt, and reabsorption of sodium and water in the distal tubules of the nephron. Some of these cellular functions are associated with the activation of cGMP kinase and a decrease in cytosolic calcium levels ([Ca2+]i). The mechanism by which cGMP kinase lowers [Ca2+]i is controversial. We have used CHO cells stably transfected with cGMP kinase to test several of the proposed [Ca2+]i-lowering mechanisms. Thrombin induces a calcium transient in wild-type and cGMP kinase-expressing CHO cells by releasing calcium from intracellular stores. Preincubation of wild-type cells with 8-bromo-cGMP had no effect on the calcium transient, whereas 8-bromo-cGMP prevented the thrombin-stimulated calcium transient in cGMP kinase-expressing CHO cells. In both cell types 8-bromo-cGMP had no effect on [Ca2+]i transients induced by replacing extracellular sodium by tetramethylammonium, ruling out an effect of cGMP kinase on Ca(2+)-ATPases. However, cGMP kinase activation effectively suppressed thrombin-induced stimulation of inositol 1,4,5-trisphosphate production. These results show that cGMP kinase lowers [Ca2+]i by interfering with the inositol 1,4,5-trisphosphate synthesis.

Animals↗
PubMed1994

Molecular cloning of a functional human galanin receptor.

The ubiquitous neuropeptide galanin controls numerous functions such as endocrine secretions, intestinal motility, and behavioral activities. These regulatory effects of galanin are mediated through the interaction with specific membrane receptors and involve the pertussis toxin-sensitive guanine nucleotide binding proteins Gi/Go as transducing elements. We report here the isolation of a cDNA coding for a human galanin receptor from a Bowes melanoma cell line cDNA expression library, by using a radioligand binding strategy. The nucleotide sequence of the cloned receptor reveals an open reading frame encoding a 349-amino acid protein with seven putative hydrophobic transmembrane domains and significant homology with members of the guanine nucleotide binding protein-coupled neuropeptide receptor family. The cloned receptor expressed in COS cells specifically binds human, porcine, and rat galanin with high affinity (Kd in the nanomolar range) and mediates the galanin inhibition of adenylate cyclase. A 2.8-kb galanin receptor transcript was identified in several human tissues. Cloning of this galanin receptor should enhance our knowledge of its distribution, structure, and function in human physiology and pathophysiology.

Amino Acid Sequence↗
PubMed1986

Digestion of the zinc in human milk, cow's milk and a commercial babyfood: some implications for human infant nutrition.

1. The digestion of zinc present in human milk, cow's milk and a commercial babyfood was compared, using the piglet as a model for the human infant. 2. In piglets given human milk the pH of stomach contents was approximately 1 and 0.4 units lower than that of animals given respectively cow's milk and babyfood. The pH values of intestinal contents were approximately neutral and did not vary with the type of feed. 3. Hard casein curds were present throughout the stomachs and small intestines of animals fed on cow's milk or babyfood and between 55 and 70% Zn in these digesta samples were recovered in an insoluble form by centrifugation. In contrast, little solid material was observed in the digesta of animals fed on human milk, and 57 and 93% respectively of the Zn in digesta were recovered in a soluble form in the stomach and small intestine. 4. Soluble fractions prepared by centrifugation of digesta were analysed by filtration on Sephadex G-150. After any of the three feeds, soluble Zn in stomach contents was mainly in a low-molecular-weight form. In intestinal samples, however, Zn was present in low- and high-molecular-weight forms. Whilst there were similar amounts of Zn in the low-molecular-weight form in all samples, approximately three times as much of the total intestinal Zn was in a soluble high-molecular-weight form complexed to proteins in the animals fed on human milk compared with those fed on cow's milk or babyfood. 5. Analysis of protein-bound soluble Zn in intestinal samples on SDS-polyacrylamide gels resulted in a similar pattern of proteins for all feeds. Results indicated that at least some of these proteins were derived from intestinal secretions of the piglet. 6. Some implications of these results in respect of the mode of digestion of Zn and its biological availability to the human infant are discussed.

Animals↗
PubMed1995

Growth, viscosity and beta-glucanase activity of intestinal fluid in broiler chickens fed on barley-based diets with or without exogenous beta-glucanase.

1. Three groups of birds were fed for up to 35 days on diets containing 500 g barley (cv. Condor)/kg diet, with or without exogenous beta-glucanase, either a commercial preparation or a recombinant endoglucanase. 2. Birds which received diets containing the exogenous enzymes grew faster for the first 3 weeks but after that there was no apparent difference in rate of growth. 3. beta-Glucanase activities in the crop and small intestine of birds given exogenous enzymes were generally higher than those of birds given only the basal diet. 4. Viscosity of intestinal fluid in birds given only the basal diet decreased with age but there was no corresponding increase in beta-glucanase activity. This discounts bacterial beta-glucanase as a contributory factor in the adaptation to beta-glucanase apparent in older birds.

Animals↗
PubMed1984

Deconjugation of bilirubin conjugates and urobilin formation by conventionalized germ-free rats.

The amounts of conjugated bilirubin and urobilins/urobilinogen were determined semiquantitatively in faeces of germ-free (GF) rats during GF condition and after conventionalization by oral administration of faeces suspension from conventional (CONV) rats. The amount of bilirubin conjugates, detected as their ethyl anthranilate azopigments, decreased rapidly 1 day after conventionalization. Thin-layer chromatography analysis of the corresponding faecal azopigment preparations showed that some azopigments started to disappear a few days after the conventionalization, indicating that their corresponding bilirubin conjugates were deconjugated by the bacteria in the intestine. On day 21 after conventionalization, only two azopigments were detected, namely the unconjugated and glucuronic acid conjugated dipyrroles of bilirubin, respectively, thus indicating the presence of only one bilirubin conjugate, the monoglucuronide. After 69 days no azopigments could be detected, indicating the total absence of conjugated bilirubin in these faeces samples. No urobilins were detected in faeces of the rats during their GF state, but these metabolites appeared in faeces one day after conventionalization and increased during a few days to a CONV level.

Animals↗
PubMed1981

[Physiological nutrition studies of swine for the evaluation of modified proteins. 3. Relationship between the true and apparent N digestibility and amino acid absorption of the small intestines and the parameters of N metabolism].

Modified proteins were tested in absorption investigations with eight pigs with ileocaecal re-entrant cannulae. The apparent digestibility up to the end of the small intestines showed considerable differences between the feed proteins (77-93%). The same differences could be observed with regard to the apparent absorption of amino acids. Concerning the true N-digestibility resp. the true absorption of the amino acids in the above mentioned section of the intestinal tract there were hardly any differences between the proteins given. The results show that there is a relation between the amount of endogenous N in the chyme at the end of the small intestines and the protein consumed. The amount of endogenous N in the chyme in the small intestines influence N-excretion in urine and thus the intermediary utilisation of feed protein. From the point of view of nutrition physiology it follows that the spun vicia-faba protein/casein (1 : 1) fibres (C) approximate best the value of casein (A). While the treatment of this mixed protein with dyaldehyde starch had a negligible effect on the ascertained parameters only, the treatment of the same protein with aluminium chloride diminished its value more. The isolated vicia-faba (B) was the poorest of the modified proteins tested.

Amino Acids↗
PubMed1981

[Nutritional and physiological studies of swine for the evaluation of modified proteins. 2. Determination of endogenous N in the contents of the small intestines using the 15N-tracer method].

The endogenous N-quota in the chyme of the small intestines after providing modified proteins was determined with re-entrant cannulae at the end of the ileum in investigations with pigs (35 to 50 kg live weight) with the isotope dilution method. The N-pool of the test animals was labelled with 15N-glycine and 15N-leucine. The TCA-soluble fraction of the blood plasma served as criterion for the labelling level of the N-pool. The results showed a direct connection between N-intake and endogenous N in the chyme of the small intestines. With regard to N-intake, the dependence of endogenous N in the chyme of the small intestines on feed protein could be observed.

Animals↗
PubMed1984

Investigations about influence of the content of plant crude protein in the ration on the utilization of urea in dairy cattle. 6. Digestive enzymes and their interactions in contents of proximal small intestine.

Forty-two samples were taken from the contents of the proximal small intestine of two lactating dairy cows fitted with re-entrant duodenal cannula. Most samples were free of detectable amylase activity. The (chymo)trypsinogen present was only partially activated to (chymo)trypsin. The activation was continued in vitro: slowly at the original pH of the samples (between pH 2.8 and 4.2), and faster after neutralization or a slight alkalinization. The effect of Ca, EDTA and soybean inhibitor on the activation of trypsinogen was also studied. The pancreatic enzymes were inactive in the acid pH range of the samples, but pepsin was markedly active. At pH 3.8 casein was digested rapidly by purified pepsin and slowly by the samples (agar-plate experiments). In model experiments performed with purified enzymes, pepsin digested (chymo)trypsin rapidly at pH 1-2 and slowly at pH 3.8. In the intestinal juice (chymo)trypsin and their zymogens seemed to be unaffected by pepsin under the conditions of the samples. It is concluded that the conditions prevailing in the duodenum/upper jejunum of the experimental cows account for a gastric-type digestion, despite the presence of pancreatic enzymes. In vivo the intestinal contents pass in distal direction. Meanwhile the pH of the chyme gradually increases and gives rise to first an increase of enterokinase activity accounting for a faster activation of the zymogens; second a start of function of activated pancreatic proteases and third a gradual decrease of pepsin activity and finally to its irreversible denaturation. Thus the development of intestinal type digestion is delayed in ruminants.

Animals↗
PubMed1976

Mechanism and site of small intestinal uptake of vitamin D3 in pharmacological concentrations.

The site and mechanism of initial uptake of 1,2-3H vitamin D3 pharmacological concentrations was investigated using everted rat small bowel sacs incubated in a micellar medium. The mean +/- SE uptake rates of the vitamin at 300 muM incubation solution concentration by proximal, medial, and distal small bowel segments were 6.7 +/- 0.26, 7.8 +/- 0.54, and 3.3 +/- 0.20 nmole/min/100 mg tissue, respectively. Incubation with the addition of 10(-3) M 2,4-dinitrophenol, or 10(-3) M KCN, or under nitrogen atmosphere did not change (P greater than 0.05) the above rates of absorption. Incremental increases in the concentration of vitamin D in the incubation medium up to 1200 muM resulted in a linear increase in the uptake rate indicating lack of saturation kinetics. In all the above experiments, greater rate of uptake of the vitamin occurred in the proximal and medial small bowel than the distal small bowel (P less than 0.01). The above experiments indicate that vitamin D3 in this range of concentrations is taken up by enterocytes by a nonsaturable passive diffusion mechanism showing no evidence for carrier mediation. The rate of intestinal uptake is highest in the proximal and medial segments of the small bowel.

Animals↗