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Biomedical subjects

V Erspamer

Publications and source records attributed to V Erspamer.

At least 55 records · Page 3Linked to original sources
PubMed1985

Bombesin effects on human GI functions.

In this article some of the actions of amphibian skin peptide Bombesin (BBS) on human gastrointestinal and pancreatic functions are reviewed. BBS causes increases of lower esophageal sphincter pressure, delay of gastric emptying, inhibition of mechanical activity of duodenum and jejunum and gallbladder emptying. BBS also releases in man gastrin and stimulates gastric acid secretion. BBS administration induces release of insulin, glucagon and pancreatic polypeptide from human Islet of Langerhans and causes secretion of pancreatic bicarbonates and enzymes in duodenal juice and release of pancreatic enzymes in blood stream.

Bombesin↗
PubMed1985

Peptides of the APUD system in amphibian skins.

Methanol extracted skins from 84 species of amphibia were screened, measuring by RIAs: gastrin-CCK, VIP, calcitonin, GIP, PP and motilin. G-CCK-like immunoreactivity was found in 97.6%; VIP-like immunoreactivity in 41%; CT-like immunoreactivity in 34%; GIP-like immunoreactivity in 10%; PP-like immunoreactivity in 40% and MT-like immunoreactivity in 60% of the samples. The use of a sequence-specific radioimmunoassay and of gel-chromatography confirmed the caerulein-CCK-8-like nature of the immunoreactive material. Detected amounts of the other peptides (VIP, CT, GIP, PP, MT) were too low for bioassay or chromatographic studies, thus leaving the question open if they are due to some kind of unspecific interferences or, most likely, to species-specificity differences of the used antisera.

APUD Cells↗
PubMed1984

Stimulation of crop sac and pituitary lactotrophs after intraventricular administration of dermorphin in pigeons.

The effects of dermorphin, a new potent opioid peptide, on structural and ultrastructural changes in the crop sac and in pituitary lactotrophs were assessed in pigeons (Columba livia). A single administration of dermorphin into the third cerebral ventricle (1 microgram) and the same dose repeated for 3 consecutive days both produced maximal crop sac stimulation, as documented by the presence of milk-like material as well as by scanning and transmission electron microscopy of crop sac mucosa. In addition, marked stimulatory effects were also observed in pituitary lactotrophs, as shown by stimulation of Golgi apparatus, enlargement of rough endoplasmic reticulum, increase in mitochondria size, and the presence of lysosomes and electron-opaque granules. The stimulatory effects of dermorphin on the crop sac and lactotrophs were completely prevented by naloxone, an antagonist at opiate receptors. Since dermorphin is a natural constituent of the avian brain, it has been suggested that this peptide may represent the still-obscure hypothalamic prolactin stimulatory factor.

Animals↗
PubMed1984

Active peptides in the skins of one hundred amphibian species from Australia and Papua New Guinea.

Extracts prepared from the dried skins of approximately one hundred amphibian species from Australia and Papua New Guinea were subjected to biological screening in order to determine the nature and amounts of peptides active on smooth muscle preparations and systemic blood pressure present in these extracts. The most frequently and abundantly occurring peptides were those of the caerulein, bombesin and tachykinin peptide families represented, respectively, by caerulein; litorin, Glu(OMe)2-litorin and Glu(OEt)2-litorin; uperolein and Lys5-Thr6-physalaemin. Bradykinin-like peptides seem to have a rather diffuse distribution, in the species examined, but so far no peptide of this family has been isolated and sequenced. The only angiotensin-like peptide ever found in amphibian skin, crinia angiotensin II, has been isolated from skin extracts of a few species, belonging to the genera Crinia, Geocrinia, Ranidella and Litoria. The array of peptides occurring in amphibians from Australia and Papua New Guinea is destined to increase, because several apparently novel peptides have been identified in skin extracts by bioassay and radioimmunoassay.

Amphibians↗
PubMed1982

Potent in vivo and in vitro prolactin inhibiting activity of sauvagine, a frog skin peptide.

The effect of sauvagine (SAU), a frog skin peptide, on prolactin (PRL) levels was studied in vivo and in vitro. Subcutaneous administration of SAU (20 micrograms/kg) reduced plasma PRL levels in normal adult male rats and suppressed the suckling-induced rise of PRL in lactating rats even at doses of 1 and 5 micrograms/kg. Perfusion of isolated and dispersed rat pituitary cells in vitro with increasing doses of SAU (from 5 x 10(-10) to 1.7 x 10(-8)M) induced a significant dose-related decrease of PRL secretion in the eluate. These results indicate that SAU is a potent PRL inhibiting factor and that its action is exerted at the pituitary level. If SAU or a SAU-related peptide is present in the mammalian brain, it can be tentatively hypothesized that this peptide plays an important role in the control of PRL secretion.

Amphibian Proteins↗
PubMed1981

The brain-gut-skin triangle: new peptides.

New data on tachykinins and bombesins are displayed and the present situation of research on the novel amphibian skin peptides sauvagine and dermorphin is illustrated. The potent stimulant effect of sauvagine on ACTH and beta-endorphin release has been confirmed both in vivo and on columns of isolated and dispersed rat pituitary cells, and similarly the potent inhibitory effect on PRL and GH release, both in the rat and man. Particular emphasis is laid on the occurrence of sauvagine-like immunoreactivity in fish urophysis and in amphibian nervous structures, including the retina. It is suggested that the long-searched corticotropin releasing factor and PRL release-inhibiting factor may be a sauvagine-like peptide. Dermorphin, in its turn, has been found to cause, by intracerebroventricular injection, not only analgesia and catalepsy, but also conspicuous EEG and behavioral changes in the rabbit and chick, as well as a sharp reduction in gastric emptying time and gastric acid output in the rat, together with marked stimulation of PRL release.

Adrenocorticotropic Hormone↗
PubMed1981

Radioimmunoassay of dermorphin-like peptides in mammalian and non-mammalian tissues.

A selective RIA for D-Ala2-Dermorphin (Der), a natural peptide extracted from amphibian skin, has been developed using an antibody raised in rabbits against Der which has been coupled to BSA through its phenolic hydroxyl groups of tyrosine residues with 2,4-Dichloro-6-methoxy-1,3,5-triazine. The cross-reactivity of this antibody with dermorphin analogs, C- and N-terminal fragments of dermorphin molecule, some opioid and gastrointestinal peptides was tested. Der-like immunoreactivity has been identified in tissue extracts of rats, frog and cephalopoda. Der-like peptides were purified by passing methanol extracts of the tissues through a Sephadex G25 column (16 x 100 cm) eluted with 0.1 M acetic acid at 4 degrees C. Der-like immunoreactivity from neural tissue of Dosidicus gigas, Eledone moscata, and rat brain showed a good agreement with an authentic sample of synthetic dermorphin.

Animals↗
PubMed1981

Synthetic peptides related to the dermorphins. I. Synthesis and biological activities of the shorter homologues and of analogues of the heptapeptides.

Dermorphins are potent opiate-like peptides isolated from the skin of some species of frogs. They are characterized by the presence of a D-amino acid residue, which is crucial for bioactivity. A number of analogues were prepared in order to evaluate the structure-activity relationships. The syntheses were accomplished either by conventional or solid-phase procedures. In vitro assays included both guinea pig ileum (GPI) and mouse vas deferens (MVD) preparations. Central analgesic (tail-flick and hot plate tests) and cataleptic activities were determined in the rat by intracerebroventricular route. The potency of dermorphin (H- Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2) in the different tests was: GPI: IC50 = 3.3 nM; MVD: IC50 = 29 nM; hot plate: ED50 = 13.3 pmol/rat; tail-flick: ED50 = 23 pmol/rat; catalepsy: ED50 = 130 pmol/rat.

Analgesics↗
PubMed1981

Amino acid composition and sequence of dermorphin, a novel opiate-like peptide from the skin of Phyllomedusa sauvagei.

Dermorphin, a heptapeptide with very potent opiate-like activity, has been isolated from methanol extracts of the skin of the South American frog Phyllomedusa sauvagei. The amino acid sequence of the peptide is: H-Try-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2. Dermorphin presents striking differences from the known enkephalins; it offers a surprising example of a peptide from Vertebrata containing a D-amino acid residue in its sequence.

Amino Acid Sequence↗
PubMed1981

Identification of dermorphin and Hyp6-dermorphin in skin extracts of the Brazilian frog Phyllomedusa rhodei.

Methanol extracts of the skin of the Brazilian frog Phyllomedusa rhodei contain approximately equal amounts of dermorphin and its analogue Hyp6-dermorphin, two opiate-like heptapeptides. A unique feature of their sequence is the presence of a D-amino acid residue at position 2. Hyp6-dermorphin possesses a spectrum of central and peripheral bioactivity very similar to that of dermorphin.

Amino Acid Sequence↗
PubMed1981

Pharmacological data on dermorphins, a new class of potent opioid peptides from amphibian skin.

1 Dermorphin and Hyp6-dermorphin are the first representatives of a new class of potent opioid peptides occurring in amphibian skin. They present the unique feature of having a D-Ala residue incorporated in the peptide molecule. 2 Dermorphin displayed a potent depressive action on electrically stimulated contractions of the guinea-pig ileum and mouse vas deferens preparations. Dermorphin was respectively 57,294, 18 and 39 times more potent than Met-enkephalin, Leu-enkephalin, beta-endorphin, and morphine on the guinea-pig ileum opiate receptors. On the vas deferens receptors, dermorphin was about as potent as the enkephalins and 40 times more potent than morphine. Naloxone was a powerful antagonist to dermorphin in both preparations. 3 Dermorphin produced potent and long-lasting analgesia in mice by intravenous injection, and in rats by intracerebroventricular injection, the ED50 being here of the order of 13-23 pmol/rat. Morphine was 752 and 2170 times less potent, depending on the analgesia test used. At high intracerebroventricular doses analgesia was accompanied by catalepsy. 4 Intracerebroventricular infusion of dermorphin induced development of tolerance and precipitation of withdrawal symptoms upon administration of naloxone. Both tolerance and physical dependence was consistently less marked with dermorphin than with morphine. 5 The minimum sequence requirement for full dermorphin activity was represented by the N-terminal tetrapeptide. The presence of the D-Ala2-residue was of crucial importance.

Amphibians↗
PubMed1981

Comparative histochemistry as a springboard for the discovery of biogenic amines and active peptides in molluscan tissues and amphibian skin.

Histochemistry has been the springboard for the identification in molluscan tissues (hypobranchial body and salivary glands) and amphibian skin of a number of biogenic amines, choline esters and active peptides. Among the biogenic amines 5-HT and related indolealkylamines, octopamine, tyramine and several histamines are to be listed; among the choline esters murexine, dihydromurexine, senecioylcholine and acryloylcholine; among the peptides an array of compounds belonging to at least ten different peptide families. 5-HT, octopamine, tyramine and histamine are present, together with representatives of some peptide families in the posterior salivary glands of octopods, the hypobranchial body of prosobranchiate molluscs and the amphibian skin. This points to the possible occurrence in the above structures of cells belonging to the Pearse's APUD series, intended in its broadest sense. Immunocytochemical studies and even ultrastructural studies on amine and peptide storing cells in molluscan tissues and amphibian skin are virtually lacking. This is certainly a gap that deserves to be filled, considering that these studies may help in elucidating problems of general relevance in invertebrates and vertebrates.

Amphibian Proteins↗
PubMed1981

Effects of active peptides on the isolated muscle of the human urinary bladder.

We studied the effect of 29 active peptides, six biogenic amines, and two prostaglandins on isolated preparations of the longitudinal muscle of the human urinary bladder. The peptide that had the most potent stimulant action was angiotensin II, followed by eledoisin and kassinin (substance P-like peptides), and by bombesin and litorin. The threshold dose of angiotensin was frequently as low as 0.3 to 0.5 ng per ml. Eledoisin showed approximately 10 per cent of the activity of angiotensin II. All peptides had a direct stimulant effect on vesical smooth muscle. Further studies are required to determine if angiotensin and/or substance P-like peptides are involved in the control of motility of the human urinary bladder, as constituents of the secretion of peptidergic nerves.

Angiotensins↗
PubMed1980

Sauvagine, a new polypeptide from Phyllomedusa sauvagei skin. Occurrence in various Phyllomedusa species and pharmacological actions on rat blood pressure and diuresis.

1. The occurrence of sauvagine, a new polypeptide from amphibian skin, and its actions on rat blood pressure and diuresis were studied. 2. Sauvagine was found to be present in the skin of all the 10 Phyllomedusa species so far studied, amounts ranging from a few micrograms to 240 micrograms per g fresh skin. 3. The polypeptide displayed in the rat an intense, long-lasting hypotensive action accompanied by tachycardia. Hypotension was not modified by either atropine or propranolol, excluding the participation of the autonomic nervous system in its production. Tachycardia, on the contrary, was partially inhibited by propranolol. 4. Hypotension is probably the main cause of the intense antidiuresis seen in hydrated rats following sauvagine administration. Reduction in urina volume was accompanied by a decrease in GFR and an increase in tubular NA+ reabsorption.

Amphibian Proteins↗
PubMed1980

Parallel bioassay of physalaemin and kassinin, a tachykinin dodecapeptide from the skin of the African frog Kassina senegalensis.

1. Kassinin, a tachykinin dodecapeptide isolated from the skin of the African frog Kassina senegalensis was submitted to parallel bioassay with physalaemin, eledoisin and substance P, three major representatives of the tachykinin peptide family. Bioassay was carried out on blood pressure, salivary secretion and isolated or in situ smooth muscle preparations. 2. As expected, kassinin possessed the entire spectrum of biological activity peculiar to the tachykinins. However, among the examined tachykinins kassinin was the poorest stimulant of salivary secretion and the weakest hypotensive agent, while displaying very powerful stimulant effects on different smooth muscle preparations, especially on isolated preparations of urinary bladder. 3. Kassinin differed from the other tachykinins also for its more gradual and sustained action on several in situ and isolated preparations. The peptide most similar to kassinin in its spectrum of activity was eledoisin. 4. Emphasis is laid on the possibility to dissociate the effects of the tachykinins on different target systems through changes in the N-moiety of the tachykinin molecule.

Animals↗