References of "Leprince, Pierre"
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See detailPlasminogen activators in developing peripheral nervous system, cellular origin and mitogenic effect.
Baron-Van Evercooren, A.; Leprince, Pierre ULg; Rogister, Bernard ULg et al

in Brain Research (1987), 433(1), 101-8

Newborn rat dorsal root ganglia release two different plasminogen activators (PAs): the urokinase (UK) and the tissue (tPA) type. The former is secreted by neurons while the latter is secreted by Schwann ... [more ▼]

Newborn rat dorsal root ganglia release two different plasminogen activators (PAs): the urokinase (UK) and the tissue (tPA) type. The former is secreted by neurons while the latter is secreted by Schwann cells. tPA release by Schwann cells is modulated by choleratoxin, a known mitogen for these cells. UK but not tPA stimulates in a dose-dependent fashion the proliferation of Schwann cells. This effect is observed in the absence of plasminogen, suggesting that the substrate for PAs in the developing nervous system is not plasminogen. Since UK is secreted by neurons, our data suggest a new mechanism for neuronal control of Schwann cell proliferation. [less ▲]

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See detailPlasminogen activators and laminin in developing nervous system
Moonen, Gustave ULg; Leprince, Pierre ULg; Rogister, Bernard ULg

in Metabolism and Development of the Nervous System (1987)

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See detailPlasminogen activators in brain development
Selak, Ivan ULg; Rogister, Bernard ULg; Lefebvre, Philippe ULg et al

in Advances in the Biosciences (1986), 61

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See detailTwo step synthesis of a new Na channel marker by mild oxidation of tetrodotoxin, monitored by HPLC and coupling of (3)ethylenediamine of high specific radioactivity
Bontemps, J; Grandfils, Christian ULg; Cantineau, R et al

in Archives Internationales de Physiologie et de Biochimie (1984), 92

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See detailHigh-Yield Synthesis of a (3H)Ethylenediamine Ditetrodotoxin Derivative
Bontemps, José; Cantineau, Robert; Grandfils, Christian ULg et al

in Analytical Biochemistry (1984), 139

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See detailChemical modification of the nicotinic cholinergic receptor of PC-12 nerve cell.
Leprince, Pierre ULg

in Biochemistry (1983), 22(24), 5551-6

The identity of the protein that mediates the nicotinic acetylcholine sensitivity in neuronal cells has been investigated by chemical modification and affinity labeling. When an ion flux assay is used, it ... [more ▼]

The identity of the protein that mediates the nicotinic acetylcholine sensitivity in neuronal cells has been investigated by chemical modification and affinity labeling. When an ion flux assay is used, it is possible to measure specifically the activity of the ionophore associated with the nicotinic acetylcholine receptor in cultured nerve cells (PC-12 pheochromocytoma). This activity is modulated by modification of the redox state of at least one disulfide bridge located at the vicinity of the agonist binding site. The oxidizing agent 5,5'-dithiobis(nitrobenzoic acid) restores the complete receptor response which had been inhibited by reduction with dithiothreitol. N-Ethylmaleimide and the nicotinic affinity labels [4-(N-maleimido)benzyl]-alpha-trimethylammonium iodide and bromoacetylcholine react also with the reduced receptor and irreversibly block the agonist-dependent response of the ionophore. The two affinity labels show strong affinities for the receptor, and apparent IC50 values of 20 and 560 nM can be respectively evaluated. Bromoacetylcholine, being an acetylcholine analogue, blocks the receptor function by desensitization, a process in which the constant interaction with the activator causes a shift into an inactive form of the receptor. Bromoacetylcholine can also be shown to activate untreated as well as reduced cells. In this case, the bound label induces a lasting response which is terminated by the irreversible desensitization of the modified receptor. These experiments thus show that the PC-12 nicotinic ionophore shares functional and structural similarities with peripheral receptors. They suggest that nicotinic affinity labels developed for the muscle receptor can also be used as specific markers of the nicotinic neural ionophore. [less ▲]

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See detailPhencyclidine inhibition of the acetylcholine receptor: measurement of cation flux in a sympathetic neuronal cell line using 22Na+ and spectroscopic detection of Cs+.
Sachs, A. B.; Leprince, Pierre ULg; Karpen, J. W. et al

in Archives of Biochemistry & Biophysics (1983), 225(2), 500-4

The site of action of phencyclidine, a powerful and increasingly abused drug, in sympathetic nerve cells has not previously been identified. Here it is demonstrated that phencyclidine is a powerful ... [more ▼]

The site of action of phencyclidine, a powerful and increasingly abused drug, in sympathetic nerve cells has not previously been identified. Here it is demonstrated that phencyclidine is a powerful, noncompetitive inhibitor of the nicotinic acetylcholine receptor in a sympathetic nerve cell line, PC-12. In the presence of 1 mM carbamoylcholine the rate of the receptor-controlled influx of 22Na+ is reduced by a factor of 2 by 0.7 microM phencyclidine. Increasing concentrations of carbamoylcholine cannot reverse the inhibitory effect of the drug. Both the transmission of electrical signals between nerve cells and the secretion of catecholamines in the PC-12 cell line depend on the receptor-controlled ion flux. Thus phencyclidine interferes with at least two specific, physiologically important functions of these nerve cells. A new spectroscopic method has been developed to measure cation flux in cells. It is shown that this method can replace measurements of tracer ion flux. [less ▲]

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See detailComparison of the interactions of a specific neurotoxin (alpha-bungarotoxin) with the acetylcholine receptor in Torpedo californica and Electrophorus electricus membrane preparations.
Leprince, Pierre ULg; Noble, R. L.; Hess, G. P.

in Biochemistry (1981), 20(19), 5565-70

alpha-Bungarotoxin, a snake neurotoxin, binds irreversibly and specifically to the acetylcholine receptor isolated from the electroplax of Electrophorus electricus and Torpedo species and has been an ... [more ▼]

alpha-Bungarotoxin, a snake neurotoxin, binds irreversibly and specifically to the acetylcholine receptor isolated from the electroplax of Electrophorus electricus and Torpedo species and has been an important tool in the study of the receptor-ligand binding mechanism. Two distinct kinetic processes have been observed in studies with membranes from E. electricus. A minimum mechanism for the toxin reaction involves (i) the reversible binding of two toxin molecules to the receptor prior to the irreversible formation of toxin receptor complexes and (ii) a toxin-induced conformational change of the receptor which leads to an increase in the affinity of the receptor binding sites for toxin [Hess, G. P., Bulger, J. E., Fu, J.-j. L., Hindy, E. F., & Silberstein, R. J. (1975) Biochem. Biophys. Res. Commun. 64, 1018-1027]. Only one process has been detected in Torpedo membranes. Here, we determine whether the receptors in Torpedo californica and E. electricus membranes have different properties or whether the measurements and their interpretation were responsible for the different results. Two methods which are frequently used in binding studies to separate free and bound toxin, a CM-52 cellulose minicolumn assay and DE-81 filter disk assay, have been compared. The results obtained indicate that the interaction of toxin with receptor from T. californica is similar to that observed with receptor from E. electricus. The apparent differences which have been reported in the literature are shown to have arisen from the design of the experiments in which T. californica membranes were used. [less ▲]

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See detailHow are feathers digested by raptors?
Leprince, Pierre ULg; Dandrifosse, Guy ULg; Goffinet, Gerhard ULg et al

in Biochemical Systematics & Ecology (1980), 8(2), 211-219

In order to determine the cause of the evident degradation of feathers from ingested prey in pellets regurgitated by raptors, in vitro digestions of whole feather barbs by pellet extracts, pepsin or ... [more ▼]

In order to determine the cause of the evident degradation of feathers from ingested prey in pellets regurgitated by raptors, in vitro digestions of whole feather barbs by pellet extracts, pepsin or trypsin were carried out. The material was analysed by using biochemical and electron microscopic methods. The results show that the changes in the feathers which occur in the stomach of the Falconidae do not arise from digestion of keratin but from hydrolysis of protein acting as a cement matter in the feather. [less ▲]

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See detailThe digestive enzymes and acidity of the pellets regurgitated by raptors
Leprince, Pierre ULg; Dandrifosse, Guy ULg; Schoffrniels, Ernest

in Biochemical Systematics & Ecology (1979), 7(3), 223-227

The activity of six digestive enzymes (amylase, chitinase, trypsin, chymotrypsin, carboxypeptidase A, pepsin) was examined in the water-soluble contents of the pellets egested by ten species of raptors ... [more ▼]

The activity of six digestive enzymes (amylase, chitinase, trypsin, chymotrypsin, carboxypeptidase A, pepsin) was examined in the water-soluble contents of the pellets egested by ten species of raptors (kestrel, saker, lanner, goshawk, barn owl, tawny owl, little owl, long-eared owl, African great-owl and steppe eagle). All the enzymes studied were present in the pellets from these birds, except for chitinase which was not detected in the pellets of the goshawk and the steppe eagle, and amylase and carboxypeptidase absent in the material egested by the lanner. The origin of the enzymes studied was examined. Pancreatic enzymes, which are present in the pellets, arise from a reflux of intestinal fluid into the stomach. The importance of this phenomenon is discussed. The acidity of the pellets was measured. Relations existing between the type of food, characteristics of the pellet and the digestive process in raptors are analysed. The evolutionary advantage of pellet egestion is discussed. [less ▲]

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