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J Rossier

Publications and source records attributed to J Rossier.

At least 145 records · Page 8Linked to original sources
PubMed1985

Characterization of a new 23 kDalton enkephalin-containing protein in the bovine adrenal medulla.

Immunoblots combined with specific radioimmunoassays (RIAs) have been used to visualize simultaneously all the enkephalin-containing peptides (ECPs) present in a crude extract of bovine adrenal medulla. They have allowed the characterization of a new high molecular weight ECP which has a molecular weight of 23.3 kDalton, contains the amino-terminal part of proenkephalin and ends with the sequence of Leu-enkephalin at its carboxy-terminus.

Adrenal Medulla↗
PubMed1985

A comparison of opioid peptide precursors in guinea pig, rat and bovine striata and guinea pig adrenal.

In this study guinea pig, rat and bovine striatal extracts have been shown to contain putative opioid peptide precursors in the molecular weight (Mr) range 2000-greater than 70000. The material eluting greater than 70 kDalton contained bioassayable opioid activity but not Met- or Leu-enkephalin-like immunoreactivities (ME-IR and LE-IR) and may represent a novel endogenous opioid-peptide precursor.

Adrenal Glands↗
PubMed1985

Release of synenkephalin from neuronal terminals in vitro.

Synenkephalin, the amino-terminal 1-70 residues of proenkephalin is released intact from bovine globus pallidus following potassium-induced depolarization in vitro via a Ca++ dependent mechanism. The release of synenkephalin accompanies that of Met-enkephalin in a molar ratio of 1/4. In contrast to Met-enkephalin which is readily destroyed when released, synenkephalin is not destroyed.

Animals↗
PubMed1985

Release of proenkephalin-derived opioid peptides from rat striatum in vitro and their rapid degradation.

In a previous paper we demonstrated that the heptapeptide [Met]enkephalyl-Arg6-Phe7 was released from rat striatal slices by high K+ concentration and rapidly degraded by peptidases, even in the presence of the neutral endopeptidase 24.11 ("enkephalinase")-inhibitor, thiorphan (0.1 microM), the angiotensin-converting enzyme inhibitor, captopril (1 microM), and the aminopeptidase inhibitor, bestatin (20 microM). In this study the pattern of degradation of exogenous [3H]heptapeptide by rat striatal slices has been studied. The angiotensin-converting enzyme and aminopeptidase(s) were partly responsible for this degradation. In addition an enzymatic activity that cleaved the Phe4-Met5 bond was involved in the degradation of the heptapeptide by striatal slices. This activity was inhibited by the dipeptide Leu-Arg (1 mM) and the tripeptide Leu-Arg-Leu (1 mM). The simultaneous presence of thiorphan (0.1 microM), captopril (1 microM), bestatin (20 microM) and Leu-Arg (1 mM) almost completely inhibited the degradation of [3H]heptapeptide by striatal slices. In the presence of these peptidase inhibitors a concomitant release of [Met]enkephalin, the heptapeptide [Met]enkephalyl-Arg6-Phe7 and the octapeptide [Met]enkephalyl-Arg6-Gly7-Leu8 was evoked by KCl or veratridine. The K+-evoked release was by a Ca2+-dependent mechanism and the release evoked by veratridine was blocked by tetrodotoxin. In both cases the ratio of [Met]enkephalin to heptapeptide amounts released was close to that found in their common precursor, proenkephalin. Thus the enkephalinergic neuron appears to be capable of synthesizing, from a unique precursor, four different putative opioid neurotransmitters, namely [Met]enkephalin, [Leu]enkephalin, the heptapeptide [Met]enkephalyl-Arg6-Phe7 and the octapeptide [Met]enkephalyl-Arg6-Gly7-Leu8, to store these peptides and to release them upon depolarization.

Animals↗
PubMed1985

3-Amino-beta-carboline derivatives and the benzodiazepine receptor. Synthesis of a selective antagonist of the sedative action of diazepam.

Seven 3-N-substituted derivatives of 3-amino-beta-carboline were synthesized and their affinities for the benzodiazepine receptor were assessed in vitro. Two compounds, 3-(ethylamino)-beta-carboline and 3-[(methoxycarbonyl)amino]-beta-carboline (beta-CMC), showing IC50 values of 460 and 71 nM, respectively, were selected for in vivo studies. The former compound showed long-lasting proconvulsant activity in Papio papio baboons while beta-CMC was shown in mice to selectively antagonize the sedative effects of diazepam without exhibiting convulsant, proconvulsant, or anxiogenic activity by itself.

Animals↗
PubMed1985

Identification of a proenkephalin precursor in striatal tissue.

Recent studies have supported the suggestion that proenkephalin is the same in both adrenal medulla and brain. However, although previous investigations have characterized enkephalin-containing adrenal intermediates derived from proenkephalin, as yet no such intermediates have been isolated from the brain. This has led to the belief that the processing of proenkephalin in the brain is extremely rapid and enkephalin-containing intermediates do not accumulate. In this investigation Sephacryl-300 gel filtration chromatography of guinea pig striata, extracted in 8 M urea, demonstrated several peaks of both bioactive and immunoreactive enkephalin-like peptides after enzymatic digest (trypsin followed by carboxypeptidase B). Comparable profiles were obtained using rat and bovine striatal tissue. In guinea pig the major species emerging from gel filtration, eluting with an apparent molecular weight of 29,000, represented approximately 9% of the total (methionine) enkephalin immunoreactivity. It had an apparent pI of 5.0 when subjected to chromatofocusing. This species was further characterized using sodium dodecyl sulphate-polyacrylamide gel electrophoresis and nitrocellulose blotting techniques as well as highly specific radioimmunoassays to (Met5)-enkephalin, (Leu5)-enkephalin, and (Met5)-enkephalin-Arg6-Phe7. This species was found to contain these opioid peptides in an approximately 6:1:1 ratio, respectively, and to have an apparent molecular weight of 31,000. It was also indicated that (Met5)-enkephalin-Arg6-Phe7 constituted the C-terminal seven residues of this molecule.

Animals↗
PubMed1985

Co-existence of cholecystokinin- or gastrin-like peptides with other peptides in the hypophysis and the hypothalamus.

The presence of cholecystokinin and gastrin has been reported in the hypothalamohypophyseal system. These peptides present a peculiar distribution in the hypothalamic nuclei, the median eminence, and the neurohypophysis. CCK and gastrin have close relationships with other peptides like oxytocin, CRF, vasopressin, and the enkephalins; these relationships vary in different projecting areas and in different types of hypothalamic neurons. The functional role of G-CCK in neurosecretion seems to be linked to the role of these closely associated peptides and certainly deserves further investigation.

Animals↗
PubMed1984

Characterization of convulsions induced by methyl beta-carboline-3-carboxylate in mice.

The convulsive properties of methyl beta-carboline-3-carboxylate (beta-CCM) were evaluated in mice. When injected subcutaneously at a dose of 10 mg/kg beta-CCM induced convulsions in 75% of the mice with a median latency of 2.12 +/- 0.25 min. The CD50 was determined to be about 5 mg/kg. Electroencephalographic recordings showed that convulsions were brief (10 s), of cortical origin and propagating rapidly to the hippocampus. EEG alterations induced by low doses of beta-CCM lasted up to 1 h. The convulsive effect of beta-CCM was compared to that of PTZ. PTZ-induced convulsions occurred with a longer latency (9.26 +/- 1.33 min). beta-CCM and PTZ could act synergistically when injected in non-convulsive doses. When beta-CCM was injected 2-30 min before pentylenetetrazol (PTZ) there was a clear potentiation of the convulsive effect of PTZ. The convulsions induced by beta-CCM were blocked by diazepam (DZ) and by Ro 15-1788. In addition, beta-CCM reversed the sedative effect of a high dose of DZ for more than 30 min. Our results confirm that beta-CCM acts through the BZ receptor and indicate that the effects induced by a single dose of beta-CCM last more than 30 min.

Animals↗
PubMed1984

Processing of proenkephalin is tissue-specific.

Most neuropeptides are synthesized as large precursor proteins. These precursors undergo a maturation process involving several proteolytic events that generate the biologically active peptides. The enzymatic mechanisms underlying this processing are still largely unknown. The processing of the precursor protein proenkephalin was studied in two different bovine tissues, the hypothalamus and adrenal medulla. The high molecular weight enkephalin-containing peptides that accumulate in these two tissues were found to be different, indicating the existence of two processing pathways for this neuropeptide precursor.

Adrenal Medulla↗
PubMed1984

Synenkephalin is coreleased with Met-enkephalin from neuronal terminals in vitro.

Synenkephalin, the amino-terminal 1-70 residues of proenkephalin, is released intact from bovine globus pallidus and neurohypophysis following potassium-induced depolarization in vitro via a Ca2+-dependent mechanism. The release of synenkephalin accompanies that of Met-enkephalin in a molar ratio of 1/4. In contrast to Met-enkephalin, which is readily destroyed when released, synenkephalin is not destroyed.

Animals↗
PubMed1984

Characterization of new enkephalin-containing peptides in the adrenal medulla by immunoblotting.

Immunoblotting combined with radioimmunoassays (RIAs) directed specifically towards certain sequences of the proenkephalin molecule has been used to characterize the enkephalin-containing peptides (ECPs) present in the bovine adrenal medulla. Immunoblotting allowed the simultaneous visualization of all ECPs present in a crude extract of this gland. Combining this technique with RIAs we have been able to characterize a new high molecular mass ECP, a 23.3-kDa protein which contains the amino-terminal part of proenkephalin and ends with the sequence of Leu-enkephalin at its carboxy-terminus.

Adrenal Medulla↗
PubMed1984

Hypnotic action of ethyl beta-carboline-3-carboxylate, a benzodiazepine receptor antagonist, in cats.

The present study demonstrates that ethyl beta-carboline-3-carboxylate (beta-CCE), a benzodiazepine receptor antagonist, has hypnotic and sedative actions in cats. Moreover, at a dose that does not by itself affect sleep, beta-CCE reverses the action of diazepam on sleep organization. The hypnotic effect of subcutaneous administration of beta-CCE (5 mg/kg) lasts for 3-4 h. During this period, deep slow wave sleep (deep non-REM sleep) and paradoxical sleep (REM sleep) significantly increase, while wakefulness markedly decreases. These results, which are quite opposite to the effects of benzodiazepines on sleep organization in cats, support the notion that beta-CCE also acts as a benzodiazepine antagonist of sleep organization.

Animals↗
PubMed1984

Quantitation and localization of Met-enkephalin-Arg-Gly-Leu in rat brain using highly sensitive antibodies.

Met-enkephalin-Arg-Gly-Leu is an endogenous opioid peptide recently identified in bovine adrenal medulla. In the present study, we describe the production of highly sensitive and specific antibodies against this octapeptide. The sensibility of the radioimmunoassay procedure allows us to quantify at the femtomole level, the Met-enkephalin-Arg-Gly-Leu in individual parts of the brain without prior purification or concentration. The antibodies are highly specific for the C terminal part of the molecule, and did not cross-react with the other opioid peptides. Immunochemical techniques were used also to determine the histological location of the immunoreactive substances in individual structures of the brain. In the present paper, the comparative regional distribution of Met-enkephalin-Arg-Gly-Leu and of Met-enkephalin in rat brain are described. Our results are in good agreement with the biosynthetic relationship between Met-enkephalin and Met-enkephalin-Arg-Gly-Leu.

Animals↗
PubMed1984

Distribution and characterization of synenkephalin immunoreactivity in the bovine brain and pituitary.

The distribution of synenkephalin, the N-terminal fragment of proenkephalin, was studied in various parts of the bovine brain (globus pallidus, caudate nucleus, hypothalamus) and in the posterior pituitary by the use of a radioimmunoassay. The distribution of synenkephalin-immunoreactivity (IR) was compared to the distribution of Met-enkephalin-IR. Gel exclusion chromatography was used to examine the molecular forms of the immunoreactivities present in the tissues. The distribution of synenkephalin-IR was similar to the distribution of Met-enkephalin-IR, with a molar ratio of Met-enkephalin/synenkephalin ranging between 2.7 and 5.9. In all regions tested except the hypothalamus the synenkephalin-IR was present as a single species. However, in the hypothalamus a small amount of IR material (3% of the total synenkephalin-IR) was detected in fractions where larger Met-enkephalin-containing peptides eluted. Based on the concordance between the molar ratio of Met-enkephalin to synenkephalin found in the tissues and the molar ratio present in the sequence of adrenal proenkephalin, it is concluded that the brain and adrenal glands utilize a similar precursor for enkephalin biosynthesis.

Animals↗
PubMed1984

Purification from brain of synenkephalin, the N-terminal fragment of proenkephalin.

The primary sequence of adrenal proenkephalin was recently deduced from the structure of the cloned cDNA that codes for this protein. Several enkephalin-containing proteins with molecular weights between 8,000 and 20,000 daltons were purified from the bovine adrenal medulla. These proteins appear to represent intermediates in the processing of proenkephalin into physiologically active opioid peptides. While the concentrations of these large processing intermediates in the adrenal medulla are quite high, similar proteins have not yet been shown to be present in brain, and there is some question as to whether the brain synthesizes an enkephalin precursor similar to adrenal proenkephalin. We report here the purification from bovine caudate nucleus of synenkephalin, the N-terminal fragment of adrenal proenkephalin. The amino acid composition of synenkephalin indicates that the protein represents residues 1-70 of adrenal proenkephalin. Thus the brain and adrenal glands appear to utilize a similar precursor for enkephalin biosynthesis.

Amino Acids↗
PubMed1984

Co-release of enkephalins and precursors with catecholamines from the perfused cat adrenal gland in situ.

We have compared the nature of the enkephalin-like material derived from proenkephalin present in the intact cat adrenal gland with the material co-released with catecholamines from the perfused adrenal in response to splanchnic nerve stimulation and to perfusions with solutions containing acetylcholine (ACh) or high potassium chloride (KCl). In cat adrenals most of the enkephalin-like material was in the form of large enkephalin-containing peptides. Free (met)enkephalin immunoreactivity represented only 25% of the total (met)enkephalin immunoreactivity as determined by enzymatic digestion of large enkephalin-containing fragments. Electrical stimulation (15 Hz) of the splanchnic nerve or perfusion of the gland with ACh (0.1 mM) or KCl (50 mM), applied for 10 min, induced an immediate release of free (met)enkephalin immunoreactivity, (met)enkephalyl-arg-phe immunoreactivity, and of large (met)enkephalin-containing peptides. The release by all three modes of stimulation followed a pattern that paralleled the output of catecholamines. A rapid fatigue of all secretory processes developed during the stimulation periods, similar to that observed for catecholamines. During splanchnic nerve stimulation, each nanomole of catecholamine output was accompanied by the output of 0.4 pmol free (met)enkephalin immunoreactivity, of 1.1 pmol total (met)enkephalin immunoreactivity and of 0.1 pmol (met)enkephalyl-arg-phe immunoreactivity. Analysis of the perfusate by high-pressure liquid chromatography revealed that (met)enkephalin, (met)enkephalyl-arg-phe and (met)enkephalyl-arg-gly-leu were released in molar ratios of 4 to 1 to 1 which is similar to the ratio found in the precursor, proenkephalin. The ratio of total (met)enkephalin immunoreactivity to free (met)enkephalin immunoreactivity in the perfusate was the same (approximately 2.7) during two successive periods of splanchnic nerve stimulation separated by 10 min. When release was evoked by increasing the K+ concentration to 50 mM-KCl, this ratio was increased more than twofold compared with that obtained by electrical stimulation of the splanchnic nerve. Analysis of the perfusate by gel filtration showed that, during splanchnic nerve stimulation, 47% of the total (met)enkephalin immunoreactivity eluted in fractions containing fragments of low molecular weight. When KCl was used as stimulus only 12% of total (met)enkephalin immunoreactivity eluted in these fractions. The results indicate that the nature of the released peptides depends on the type of stimulus used to evoke release.(ABSTRACT TRUNCATED AT 400 WORDS)

Acetylcholine↗
PubMed1984

[The coexistence of neuropeptides and catecholamines in the adrenal gland. Research on paracrine effects on adrenal cortex cells].

The aim of the present review was to compare in mammals and amphibians the data concerning the presence of neuropeptides in the chromaffin cells and the possible action of these substances on adrenocortical cell function. Major homologies are to be found concerning the coexistence in chromaffin granules of catecholamines, Met-and Leu-enkephalins, and their precursor, proenkephalin A. However, the inhibitory action that might be exerted by enkephalins in vitro on corticosteroid production in mammalian adrenal gland, does not occur in amphibia. Dynorphin has been isolated in bovine adrenal medulla extracts; the presence of this opioid peptide has not been reported yet in amphibian interrenal tissue. All chromaffin cells of the frog interrenal gland contain VIP-like immunoreactivity whereas this neuropeptide is not contained in the adrenal medulla of mammals, exept in certain pheochromocytomas. In the frog, VIP, Metenkephalin and catecholamines are co-sequestered in the same chromaffin granules. In addition, synthetic porcine or chicken VIP stimulate in vitro the secretion of corticosteroids by frog interrenal fragments. In mammals, the steroidogenic action of VIP has been observed exclusively in tumor cell lines. The existence of somatostatin has been demonstrated in the human adrenal medulla and in pheochromocytomas, but not in amphibia. Somatostatin has been found to inhibit the response of adrenocortical cells to angiotensin II in mammals. A similar effect of somatostatin was not observed in amphibia. The coexistence of VIP and catecholamines in frog chromaffin granules and the stimulatory effect exerted by VIP on corticosteroidogenesis suggest that, in these animals, VIP may be co-liberated with noradrenaline during stress conditions, and thus may act locally on adrenocortical cells to stimulate corticosteroid secretion.

Adrenal Cortex↗