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Active peptides in the skins of two hundred and thirty American amphibian species

Identifieur interne : 006970 ( Istex/Curation ); précédent : 006969; suivant : 006971

Active peptides in the skins of two hundred and thirty American amphibian species

Auteurs : V. Erspamer ; G. Falconieri Erspamer ; J. M. Cei [Argentine]

Source :

RBID : ISTEX:D48B434AA053010E26649DF8B1775116AAF2A822

Descripteurs français

English descriptors

Abstract

Abstract: 1. 1. Extracts prepared from dried or fresh skins of more than 200 American amphibian species were subjected to biological screening in order to determine occurrence and contents of peptides active on smooth muscle preparations, systemic blood pressure and, subordinately, external secretions, anterior pituitary and the central nervous system. 2. 2. The peptide families identified in skin extracts were as follows: caruleins (caerulein, phyllocaerulein), tachykinins (physalaemin, phyllomedusin), bombesins (phyllolitorin, [Leu8]phyllolitorin, rohdeilitorin), bradykinins (phyllokinin and others), sauvagine, dermorphins (dermorphin, [Hyp6]dermorphin), tryptophyllins (numerous peptides) and, finally, miscellaneous peptides. None of the above peptide families showed a widespread distribution, but all were restricted to particular amphibian genera or stocks. 3. 3. The hylid frogs of the Phyllomedusinae family occupy a unique position, as their skin displayed the greatest variety and abundance of active peptides ever found in any amphibian stock in the world. 4. 4. The array of peptide molecules occurring in the skin of the American amphibians is destined to increase because numerous other peptide molecules await isolation, elucidation of structure and definition of possible biological activities.

Url:
DOI: 10.1016/0742-8413(86)90063-0

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V. Erspamer
<affiliation>
<mods:affiliation>Institutes of Medical Pharmacology and of Pharmacology and Pharmacognosy, 1st University of Rome, I 00 100 Rome, Italy. Telephone: (06)4940094</mods:affiliation>
<wicri:noCountry code="subField">(06)4940094</wicri:noCountry>
</affiliation>
G. Falconieri Erspamer
<affiliation>
<mods:affiliation>Institutes of Medical Pharmacology and of Pharmacology and Pharmacognosy, 1st University of Rome, I 00 100 Rome, Italy. Telephone: (06)4940094</mods:affiliation>
<wicri:noCountry code="subField">(06)4940094</wicri:noCountry>
</affiliation>

Le document en format XML

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<term>Active peptides</term>
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<term>Amphibian skin</term>
<term>Amphibian skin peptides</term>
<term>Amphibian species</term>
<term>Anastasi</term>
<term>April</term>
<term>Argentina</term>
<term>August</term>
<term>Average weight</term>
<term>Bioassay</term>
<term>Biogenic amines</term>
<term>Blood pressure</term>
<term>Bombesins</term>
<term>Brad</term>
<term>Bradykinin</term>
<term>Bradykinins</term>
<term>Bufo</term>
<term>Caer</term>
<term>Caerulein</term>
<term>Chile</term>
<term>Costa</term>
<term>Dermorphin</term>
<term>Dermorphins</term>
<term>Ecuador</term>
<term>Erspamer</term>
<term>Falconieri</term>
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<term>Fresh skin</term>
<term>Frog</term>
<term>Hyla</term>
<term>Hylid frogs</term>
<term>Janeiro</term>
<term>July</term>
<term>June</term>
<term>Leptodactylus</term>
<term>Melchiorri</term>
<term>Methanol</term>
<term>Methanol extracts</term>
<term>Montecucchi</term>
<term>Napo</term>
<term>Parallel bioassay</term>
<term>Peptide</term>
<term>Peptide families</term>
<term>Peptide molecules</term>
<term>Peptide protein</term>
<term>Peptides skin</term>
<term>Personal communication</term>
<term>Peru</term>
<term>Pharmac</term>
<term>Pharmacological actions</term>
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<term>Phyllomedusin</term>
<term>Phys</term>
<term>Physalaemin</term>
<term>Physalaemus</term>
<term>Pleurodema</term>
<term>Rana</term>
<term>Rica</term>
<term>Rohdei</term>
<term>Rohdeilitorin</term>
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<term>Skin</term>
<term>Skin extracts</term>
<term>Smilisca</term>
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<term>Subfamily</term>
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<term>Argentina</term>
<term>August</term>
<term>Average weight</term>
<term>Bioassay</term>
<term>Biogenic amines</term>
<term>Blood pressure</term>
<term>Bombesins</term>
<term>Brad</term>
<term>Bradykinin</term>
<term>Bradykinins</term>
<term>Bufo</term>
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<term>Caerulein</term>
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<term>Leptodactylus</term>
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<term>Parallel bioassay</term>
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<term>Peptide families</term>
<term>Peptide molecules</term>
<term>Peptide protein</term>
<term>Peptides skin</term>
<term>Personal communication</term>
<term>Peru</term>
<term>Pharmac</term>
<term>Pharmacological actions</term>
<term>Phyllokinin</term>
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<term>Phys</term>
<term>Physalaemin</term>
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<term>Rohdei</term>
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<term>Sauvagine</term>
<term>Sept</term>
<term>Skin</term>
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<term>Smilisca</term>
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<front>
<div type="abstract" xml:lang="en">Abstract: 1. 1. Extracts prepared from dried or fresh skins of more than 200 American amphibian species were subjected to biological screening in order to determine occurrence and contents of peptides active on smooth muscle preparations, systemic blood pressure and, subordinately, external secretions, anterior pituitary and the central nervous system. 2. 2. The peptide families identified in skin extracts were as follows: caruleins (caerulein, phyllocaerulein), tachykinins (physalaemin, phyllomedusin), bombesins (phyllolitorin, [Leu8]phyllolitorin, rohdeilitorin), bradykinins (phyllokinin and others), sauvagine, dermorphins (dermorphin, [Hyp6]dermorphin), tryptophyllins (numerous peptides) and, finally, miscellaneous peptides. None of the above peptide families showed a widespread distribution, but all were restricted to particular amphibian genera or stocks. 3. 3. The hylid frogs of the Phyllomedusinae family occupy a unique position, as their skin displayed the greatest variety and abundance of active peptides ever found in any amphibian stock in the world. 4. 4. The array of peptide molecules occurring in the skin of the American amphibians is destined to increase because numerous other peptide molecules await isolation, elucidation of structure and definition of possible biological activities.</div>
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