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Biomedical subjects

M Roseghini

Publications and source records attributed to M Roseghini.

At least 19 recordsLinked to original sources

Choline esters and biogenic amines in the hypobranchial gland of 55 molluscan species of the neogastropod Muricoidea superfamily.

As many as 55 neogastropod molluscs, all belonging to the Muricoidea superfamily, have been investigated for occurrence and contents, in their hypobranchial gland (HG), of choline esters and, subordinately, biogenic amines. Very high amounts of esters, strictly localized in the median area of the HG, were found in all dye-secreting molluscs. The choline esters were represented by murexine, dihydromurexine and senecioylcholine. A fourth ester, acryloylcholine, occurred in the HG of a single, non dye-secreting mollusc. All the compounds displayed potent neuromuscular blocking actions in all examined vertebrate and invertebrate species, as well as potent nicotinic actions. Muscarinic effects were either lacking or unimportant. In addition to choline esters the HG occasionally contained known and hitherto unknown biogenic amines: tyramine, octopamine, 5-hydroxytryptamine, histamine, urocanylhistamine and imidazole-propionylhistamine. The interest of extending the search of bioactive compounds to carnivorous, predatory molluscs other than those described in this paper and, more, extensively, to any molluscan species provided with 'venomous' glands or apparatuses, is emphasized.

Animals↗

Biogenic amines and active peptides in extracts of the skin of thirty-two European amphibian species.

1. Extracts prepared from fresh or dried skins of 32 European amphibian species were submitted to chemical (colour reactions) and biological screening to determine the occurrence and contents of biogenic amines and peptides active on smooth muscle preparations and blood pressure. 2. Only indolealkylamines were detectable in the skins. They were represented by tryptamine, 5-hydroxytryptamine, and its N-methylated, cyclized and sulphoconjugated derivatives. 3. The peptide families identified in the extracts were as follows: bombesins (bombesin and alytesin), bradykinins (bradykinin, bradykinin 1-8, bradykinin 1-7), chemotactic peptides (RECP I, II and III), bombinins and TRH. Bombesins, bombinins and TRH (thyrotropin-releasing hormone) were isolated from skin extracts of discoglossid frogs; chemotactic peptides and again TRH from extracts of ranid frogs. 4. Further research will certainly lengthen the list of active peptides in the skin of European amphibians, as is the case with Australian, American and African amphibians.

Amino Acid Sequence↗

Biogenic amines and active peptides in the skin of fifty-two African amphibian species other than bufonids.

1. Extracts prepared from dried or fresh skins of 52 African amphibian species, other than bufonids, were subjected to chemical (colour reactions) and biological screening, to determine occurrence and contents of aromatic biogenic amines and peptides active on smooth muscle preparations and blood pressure. 2. Only indolealkylamines were detectable in the skins. They were represented by 5-hydroxytryptamine, its N-methylated derivatives and tryptamine. The indolealkylamines considered included the alkaloid trypargine, a carboline derivative resulting from the condensation of tryptamine with arginine. 3. The peptide families identified in skin extracts of the African frogs were as follows: caeruleins (caerulein, [Asn2, Leu5] caerulein), tachykinins (kassinin, [Glu2, Pro5] kassinin, hylambatin), bradykinins [( Hyp3] bradykinin), xenopsin, thyrotropin releasing hormone, peptide PYLa and the magainins I and II. The last five peptides have been so far identified only in the skin of Xenopus laevis, together with their precursors. 4. Since numerous other peptide molecules await isolation, elucidation of structure, and definition of possible biological activities, the array of peptides occurring in the skin of African amphibians, as in that of Australian and American amphibians, is destined to increase.

Amphibians↗

Indole-, imidazole- and phenyl-alkylamines in the skin of one hundred and forty American amphibian species other than bufonids.

Extracts prepared from dried or fresh skins of 140 American amphibian species, other than bufonids, were subjected to chemical and biological screening in order to determine the presence and concentrations of aromatic biogenic amines. The most frequent and abundantly occurring amine category was that of indolealkylamines, represented by their prototype 5-hydroxytryptamine and its N-methylated derivatives. Conjugated and cyclized indolealkylamines, typical for the toad skin, were apparently lacking. Phenylalkylamines were represented by two quaternary ammonium bases: leptodactyline and, very rarely, candicine. Leptodactyline was particularly abundant in leptodactylid frogs of the genus Leptodactylus. Histamine occurred in trace amounts in different species, in large amounts only in some Leptodactylus species of the "pachypus" section. On the other hand, N-methylated histamines and cyclized histamines (spinaceamines) were confined to the skin of Leptodactylus pentadactylus labyrinthicus. The possible taxonomical and evolutionary significance of amphibian skin amines is pointed out.

Amphibians↗

Effects of bombesin on erythropoietin production in the anaesthetized dog.

Bombesin, a tetradecapeptide isolated from the skin of some European discoglossid frogs, has been reported previously to reduce renal blood flow and glomerular filtration rate and to increase plasma renin activity in anaesthetized dogs. In the present study bombesin was infused intravenously in anaesthetized dogs at dose levels of 3, 6 and 12 ng/kg/min for 6 h and renal blood flow, glomerular filtration rate, oxygen consumption, oxygen extraction by the kidney tissue, as well as plasma erythropoietin levels (ESF) and plasma renin activity were measured. Plasma levels of ESF increased during bombesin infusion only when renal blood flow was reduced to a level of 1 ml/g/min or less. In this situation glomerular filtration was blocked, renal oxygen consumption was decreased to 10% of normal and oxygen extraction by the kidney was increased by 2 times. No correlation was found between plasma renin activity and ESF concentrations during bombesin infusion. It is concluded that the stimulant action of bombesin on ESF production is a consequence of the renal hypoxia induced by the reduction in renal blood flow.

Animals↗

Natural histamines.

Twelve histamines have been so far identified in living animal tissues. The two reactive sites of the histamine molecule involved in the production of these derivatives are represented by the imino nitrogen of the nucleus and the amino group of the lateral chain. The ring imino nitrogen may be methylated, to form 3-methylhistamine, or conjugated with ribose to give origin to histamine riboside, ribotide and dinucleotide. The amino group of thelateral chain, in its turn, may be methylated (N'-methyl-histamine, N',N'-dimethylhistamine), conjugated with aliphatic acids (N'-imidazoleproprionylhistamine, N'-urocanylhistamine) or amino acids (beta-alanylhistamine or carcinine), and finally linked, through a methyl group, to the imidazole nucleus to give origin to imidazo-c-pyridine derivatives or cyclized histamines. The biosynthesis of the above natural histamines and their physiological significance are discussed.

Amphibians↗

Presence of caerulein in extracts of the skin of Leptodactylus pentadactylus labyrinthicus and of Xenopus laevis.

1. The South American amphibian Leptodactylus pentadactylus labyrinthicus and the South African amphibian Xenopus laevis contain in their skin a polypeptide indistinguishable from caerulein prepared from the Australian amphibian Hyla caerulea.2. The caerulein content of different batches of Leptodactylus pentadactylus labyrinthicus skins varies from 10 to 500-600 mug/g tissue. Drying of the skin causes either a moderate decrease or a slight increase in the caerulein content. Methanol extraction gives considerably higher yields of caerulein than acetone extraction.3. Caerulein or caerulein-like polypeptides also occur in the skin of several other species of Leptodactylus together with 5-hydroxyindole alkylamines and imidazole alkylamines. Yet other species of Leptodactylus lack caerulein-like polypeptides and 5-hydroxyindole alkylamines.4. It is suggested that caerulein and caerulein-like polypeptides may have some function either in the regulation of secretory processes of the skin or in the exchange of water and electrolytes through the skin, or in both.

Amines↗