Novel insulin-releasing peptides in the skin of Phyllomedusa trinitatis frog include 28 amino acid peptide from dermaseptin BIV precursor

L Marenah, Stephen McClean, Peter Flatt, DF Orr, C Shaw, Yasser Abdel-Wahab

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18 Citations (Scopus)

Abstract

Objective: The granular glands of amphibians have long been known to produce many biologically active compounds. The aim of this study was to isolate and characterize insulinotropic peptides from the skin of Phyllomedusa trinitatis frog. Methods and Results: Crude secretions obtained by mild electrical stimulation of the dorsal skin surface were purified by reverse phase HPLC yielding 80 fractions. In acute incubations with glucose-responsive BRIN-BD11 cells, fractions 39-40 ( band 1) and fractions 43-46 ( band 2) significantly stimulated insulin release by 1.5 to 2.5-fold. Pooled fractions in bands 1 and 2 were rechromatographed to 4 homogeneous peaks, each with insulin-releasing activity. Mass spectrometry analysis was successfully completed for 3 peptides, indicating 2996.4, 3379.9, and 8326.4 Da. The sequence of the 2996.4 Da peptide was determined as ALWKDILKNVGKAAGKAVLNTVT-DMVNQ. This 28-amino-acid peptide has 100% homology with the C-terminal of the 75-amino-acid dermaseptin BIV precursor of a family of structurally related antimicrobial peptides in the skin of the Phyllomedusinae subfamily. Conclusion: These data demonstrate that the defensive skin secretions of P. trinitatis contain biologically active peptides, which may have mammalian counterparts and merit further investigation as insulin secretagogues.
LanguageEnglish
Pages110-115
JournalPancreas
Volume29
Issue number2
Publication statusPublished - Aug 2004

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Bovine Immunodeficiency Virus
Anura
Insulin
Amino Acids
Skin
Peptides
Amphibians
Electric Stimulation
dermaseptin
Mass Spectrometry
High Pressure Liquid Chromatography
Glucose

Cite this

@article{e3136d2d98594f58a28b9a0da7022a31,
title = "Novel insulin-releasing peptides in the skin of Phyllomedusa trinitatis frog include 28 amino acid peptide from dermaseptin BIV precursor",
abstract = "Objective: The granular glands of amphibians have long been known to produce many biologically active compounds. The aim of this study was to isolate and characterize insulinotropic peptides from the skin of Phyllomedusa trinitatis frog. Methods and Results: Crude secretions obtained by mild electrical stimulation of the dorsal skin surface were purified by reverse phase HPLC yielding 80 fractions. In acute incubations with glucose-responsive BRIN-BD11 cells, fractions 39-40 ( band 1) and fractions 43-46 ( band 2) significantly stimulated insulin release by 1.5 to 2.5-fold. Pooled fractions in bands 1 and 2 were rechromatographed to 4 homogeneous peaks, each with insulin-releasing activity. Mass spectrometry analysis was successfully completed for 3 peptides, indicating 2996.4, 3379.9, and 8326.4 Da. The sequence of the 2996.4 Da peptide was determined as ALWKDILKNVGKAAGKAVLNTVT-DMVNQ. This 28-amino-acid peptide has 100{\%} homology with the C-terminal of the 75-amino-acid dermaseptin BIV precursor of a family of structurally related antimicrobial peptides in the skin of the Phyllomedusinae subfamily. Conclusion: These data demonstrate that the defensive skin secretions of P. trinitatis contain biologically active peptides, which may have mammalian counterparts and merit further investigation as insulin secretagogues.",
author = "L Marenah and Stephen McClean and Peter Flatt and DF Orr and C Shaw and Yasser Abdel-Wahab",
year = "2004",
month = "8",
language = "English",
volume = "29",
pages = "110--115",
journal = "Pancreas",
issn = "0885-3177",
number = "2",

}

TY - JOUR

T1 - Novel insulin-releasing peptides in the skin of Phyllomedusa trinitatis frog include 28 amino acid peptide from dermaseptin BIV precursor

AU - Marenah, L

AU - McClean, Stephen

AU - Flatt, Peter

AU - Orr, DF

AU - Shaw, C

AU - Abdel-Wahab, Yasser

PY - 2004/8

Y1 - 2004/8

N2 - Objective: The granular glands of amphibians have long been known to produce many biologically active compounds. The aim of this study was to isolate and characterize insulinotropic peptides from the skin of Phyllomedusa trinitatis frog. Methods and Results: Crude secretions obtained by mild electrical stimulation of the dorsal skin surface were purified by reverse phase HPLC yielding 80 fractions. In acute incubations with glucose-responsive BRIN-BD11 cells, fractions 39-40 ( band 1) and fractions 43-46 ( band 2) significantly stimulated insulin release by 1.5 to 2.5-fold. Pooled fractions in bands 1 and 2 were rechromatographed to 4 homogeneous peaks, each with insulin-releasing activity. Mass spectrometry analysis was successfully completed for 3 peptides, indicating 2996.4, 3379.9, and 8326.4 Da. The sequence of the 2996.4 Da peptide was determined as ALWKDILKNVGKAAGKAVLNTVT-DMVNQ. This 28-amino-acid peptide has 100% homology with the C-terminal of the 75-amino-acid dermaseptin BIV precursor of a family of structurally related antimicrobial peptides in the skin of the Phyllomedusinae subfamily. Conclusion: These data demonstrate that the defensive skin secretions of P. trinitatis contain biologically active peptides, which may have mammalian counterparts and merit further investigation as insulin secretagogues.

AB - Objective: The granular glands of amphibians have long been known to produce many biologically active compounds. The aim of this study was to isolate and characterize insulinotropic peptides from the skin of Phyllomedusa trinitatis frog. Methods and Results: Crude secretions obtained by mild electrical stimulation of the dorsal skin surface were purified by reverse phase HPLC yielding 80 fractions. In acute incubations with glucose-responsive BRIN-BD11 cells, fractions 39-40 ( band 1) and fractions 43-46 ( band 2) significantly stimulated insulin release by 1.5 to 2.5-fold. Pooled fractions in bands 1 and 2 were rechromatographed to 4 homogeneous peaks, each with insulin-releasing activity. Mass spectrometry analysis was successfully completed for 3 peptides, indicating 2996.4, 3379.9, and 8326.4 Da. The sequence of the 2996.4 Da peptide was determined as ALWKDILKNVGKAAGKAVLNTVT-DMVNQ. This 28-amino-acid peptide has 100% homology with the C-terminal of the 75-amino-acid dermaseptin BIV precursor of a family of structurally related antimicrobial peptides in the skin of the Phyllomedusinae subfamily. Conclusion: These data demonstrate that the defensive skin secretions of P. trinitatis contain biologically active peptides, which may have mammalian counterparts and merit further investigation as insulin secretagogues.

M3 - Article

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SP - 110

EP - 115

JO - Pancreas

T2 - Pancreas

JF - Pancreas

SN - 0885-3177

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ER -