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Biomedical subjects

J Christophe

Publications and source records attributed to J Christophe.

At least 55 records · Page 3Linked to original sources
PubMed1977

Lipolysis and cyclic AMP levels in epididymal adipose tissue of obese-hyperglycaemic mice.

Glycerol release from epididymal fat fragments of young adult (3-month old) ob/ob mice was three times lower than normal, on a tissue weight basis. Dose-response curves in response to isoproterenol and ACTH-(1--24) indicated that the capacity of the lipolytic process was reduced. However, the sensitivity to both hormones was normal, i.e. greater for ACTH than for isoproterenol. The burst of cyclic AMP observed at 7 minutes was affected even more than the lipolytic capacity in adipose tissue from obese mice. This was already observed in 1-month old animals, i.e. at a time when total body weight was still normal. It is concluded that the adenylate cyclase system is defective in adipose tissue of ob/ob mice. Besides, glucagon, vasoactive intestinal polypeptide, and secretin failed to stimulate glycerol release and cyclic AMP accumulation in both ob/ob, ob+/ob+, and HA-ICR mice, suggesting that mouse adipose tissue does not possess receptors for this group of hormones.

Adipose Tissue↗
PubMed1977

Lack of adaptation of pancreatic colipase in rats and mice.

A new automated potentiometric method for the determination of colipase was developed, taking advantage of the reactivation of purified lipase, in the presence of bile salt and at pH 6.5. High-fat and high-starch diets induced an opposite regulation of lipase and amylase in the rat pancreas. At the same time, the level of colipase was not influenced by nutrition. During fasting and in alloxan diabetes, the specific activity of lipase almost doubled, that of amylase decreased sharply, and colipase was not affected in the rat pancreas. In obese-hyperglycemic mice, suffering from obesity, hyperinsulinism, and moderate diabetes, there was also no regulation of pancreatic colipase. Thus, at variance with a number of hydrolases, there was no dietary or hormonal adaptation of colipase. However, this was probably without any bearing on intraluminal lipolysis. Indeed, comparison of lipase and colipase activities in pancreas and in small intestine suggests that colipase concentration is not a limiting factor of intraluminal lipolysis. The molecular mechanism of this assumption is discussed on the basis of in vitro studies.

Adaptation, Physiological↗
PubMed1977

Wheat germ agglutinin inhibits basal- and stimulated-adenylate cyclase activity as well as the binding of [3H] caerulein to rat pancreatic plasma membranes.

Wheat germ agglutinin, but not concanavalin A or soybean lectin, inhibited the basal-and stimulated-adenylate cyclase activity which was present in a plasma membrane preparation from the rat pancreas. The inhibition by wheat germ agglutinin was rapid and sustained. It was of the non-competitive type and never exceeded 20% for Gpp (NH) p- and NaF-stimulated adenylate cyclase activity. The inhibition of secretin-stimulated activity was also non-competitive but more pronounced (57% inhibition at a wheat germ agglutinin concentration of 20 microgram/ml). For the C-terminal octapeptide of cholecystokinin-pancreozymin (OC-PZ)-stimulated cyclase, the inhibition amounted to 68% and was of a mixed type (both competitive and non-competitive). This last observation might be explained by the competitive inhibition exerted by wheat germ agglutinin on the binding of peptides of the OC-PZ family to their membrane specific receptors. The various inhibitory effects of wheat germ agglutinin were completely suppressed by incubating the membranes in the presence of ovomucoid, a N-acetyl-D-glucosamine rich glycoprotein. The possible functional implication of these results is discussed.

Adenylyl Cyclases↗
PubMed1977

Discharge of newly synthesized proteins in pure juice collected from the human pancreas. Indication of more than one pool of intracellular digestive enzymes.

The pancreatic secretion of 6 normal human volunteers was collected by endoscopic cannulation of the main pancreatic duct. The appearance of newly synthesized proteins was monitored at 1-min intervals after labeling with [75Se]methionine. The minimum transit time of these proteins from their site of synthesis to the acinar lumen was 36 +/- 8 min. Stimulation of protein secretion by a rapid intravenous injection of caerulein (40 ng per kg), 1 hr after [75Se]methionine administration, greatly decreased (by 73% on an average) the specific radioactivity of the discharged proteins. These data support the concept of a functional heterogeneity of proteins secreted by the human pancreas.

Adult↗
PubMed1976

Subcellular distribution and response to gastroinetstinal hormones of adenylate cyclase in the rat pancreas. Partial purification of a stable plasma membrane preparation.

1. The subcellular distribution of adenylate cyclase activity in rat pancreatic homogenates was examined after differential centrifugation. Divalent cations exerted significant effects on this distribution. In addition, the ratio of adenylate cyclase activities in the presence of the C-terminal octapeptide of cholecystokinin-pancreozymin and secretin was lower in the crude 'mitochondrial' fraction than in 'microsomal' fractions. This difference was due to the lability of cholecystokinin-pancreozymin receptors compared to secretin receptors. The Km,app of activation was affected more than the V by this lability. Such a degradation of cholecystokinin-pancreozymin receptors was markedly delayed by isolation and storage in the presence of a phospholipid mixture. 2. A simple, reasonably rapid (6 h), and easily reproducible method was developed to prepare a stable semi-purified plasma membrane fraction, characterized by a 10-fold increase in the specific activity of adenylate cyclase with respect to the whole homogenate. At variance with data obtained on crude subcellular fractions, the V of adenylate cyclase activity observed in this preparation, under maximal concentration of the C-terminal octapeptide of cholecystokinin-pancreozymin, was higher than that obtained with secretin or the vasoactive intestinal polypeptide.

Adenylyl Cyclases↗
PubMed1976

Influence of litter size on lipid composition in infant mice.

The amount of milk available to each member of the litter was varied by adjusting the number of mice pups to 4, 8 or 12 per dam. The total fatty acid content of the carcass of the young increased for 2 weeks, and there was more in the well-fed groups. The fatty acid contents decreased thereafter transiently in all groups until weaning. The milk diet contributed major quantities of lauric and myristic acids to peripheral tissues but not to the liver. Undernourishment during neonatal life was associated with a relative reduction in palmitoleic, oleic and linoleic acids in lipids of the carcass. In contrast the carcass of the progeny subjected to overall dietary abundance showed relative increase in palmitoleic, oleic and linoleic acids at the expense of stearic acid.

Age Factors↗
PubMed1976

In vitro action of bombesin and bombesin-like peptides on amylase secretion, calcium efflux, and adenylate cyclase activity in the rat pancreas: a comparison with other secretagogues.

Bombesin (a tetradecapeptide), the C-terminal nonapeptide of bombesin (bombesin-NP), and litorin (a parent nonapeptide), each stimulated amylase secretion from rat pancreatic fragments. These responses were not affected by atropine. The concentrations that produced half-maximal stumulation of secretion were 0.25 nM for bombesin, 0.30 nM for bombesin-NP, and 0.07 nM for litorin, as compared to 0.12 nM for caerulein and 0.80 muM for the cholinergic agent carbamylcholine. When used at maximal concentrations, bombesin, bombesin-NP, and litorin showed no action on cyclic AMP levels in the presence of 5 mM theophylline. By contrast, caerulein and secretin increased cyclic AMP levels by 27 and 208%, respectively. Bombesin, bombesin-NP, and litorin did not activate adenylate cyclase in a purified pancreatic plasma membrane preparation, whereas caerulein and secretin increased this activity 20 and 16-times, respectively...

Adenylyl Cyclases↗