Caerulein-and xenopsin-related peptides with insulin-releasing activities from skin secretions of the clawed frogs, Xenopus borealis and Xenopus amieti (Pipidae)

Osama K. Zahid, Milena Mechkarska, Opeolu O. Ojo, Yasser Abdel-Wahab, Peter Flatt, Mohammed A. Meetani, J. Michael Conlon

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Caerulein-related peptides were identified in norepinephrine-stimulated skin secretions of the tetraploid frog Xenopus borealis and the octoploid frog Xenopus amieti using negative ion electrospray mass spectrometry and their primary structures determined by positive ion tandem (MS/MS) mass spectrometry. X. borealis caerulein-B1 (pGlu-Gln-Asp-Tyr(SO(3))-Gly-Thr-Gly-Trp-Met-Asp-Phe.NH2) contains an additional Gly(5) residue compared with X. laevis caerulein and caerulein-B2 (pGlu-Asp-Tyr(SO(3))-Thr-Gly-Trp-Met-Asp-Phe.NH2) contains a Gln(2) deletion. X. amieti caerulein was identical to the X. laevis peptide. In addition, xenopsin, identical to the peptide from X. laevis, together with xenopsin-AM2 (pGlu-Gly-Arg-Arg-Pro-Trp-Ile- Leu) that contains the substitution Lys(3) -> Arg were isolated from X. amieti secretions. X. borealis caerulein-B1, and X. amieti xenopsin and xenopsin-AM2 produced significant (P < 0.05) and concentration-dependent stimulations of insulin release from the rat BRIN-BD11 clonal beta cell line at concentrations >= 30 nM. The peptides did not stimulate the release of lactate dehydrogenase at concentrations up to 3 mu M demonstrating that the integrity of the plasma membrane had been preserved. While their precise biological role is unclear, the caerulein- and xenopsin-related peptides may constitute a component of the animal's chemical defenses against predators. (C) 2011 Elsevier Inc. All rights reserved.
LanguageEnglish
Pages314-320
JournalGeneral and Comparative Endocrinology
Volume172
Issue number2
DOIs
Publication statusPublished - Jun 2011

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xenopsin
Ceruletide
Skin
Insulin
Peptides
Mass spectrometry
Cell membranes
L-Lactate Dehydrogenase
Norepinephrine

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@article{8e513e2d700c4f73a8be88825daaa7ea,
title = "Caerulein-and xenopsin-related peptides with insulin-releasing activities from skin secretions of the clawed frogs, Xenopus borealis and Xenopus amieti (Pipidae)",
abstract = "Caerulein-related peptides were identified in norepinephrine-stimulated skin secretions of the tetraploid frog Xenopus borealis and the octoploid frog Xenopus amieti using negative ion electrospray mass spectrometry and their primary structures determined by positive ion tandem (MS/MS) mass spectrometry. X. borealis caerulein-B1 (pGlu-Gln-Asp-Tyr(SO(3))-Gly-Thr-Gly-Trp-Met-Asp-Phe.NH2) contains an additional Gly(5) residue compared with X. laevis caerulein and caerulein-B2 (pGlu-Asp-Tyr(SO(3))-Thr-Gly-Trp-Met-Asp-Phe.NH2) contains a Gln(2) deletion. X. amieti caerulein was identical to the X. laevis peptide. In addition, xenopsin, identical to the peptide from X. laevis, together with xenopsin-AM2 (pGlu-Gly-Arg-Arg-Pro-Trp-Ile- Leu) that contains the substitution Lys(3) -> Arg were isolated from X. amieti secretions. X. borealis caerulein-B1, and X. amieti xenopsin and xenopsin-AM2 produced significant (P < 0.05) and concentration-dependent stimulations of insulin release from the rat BRIN-BD11 clonal beta cell line at concentrations >= 30 nM. The peptides did not stimulate the release of lactate dehydrogenase at concentrations up to 3 mu M demonstrating that the integrity of the plasma membrane had been preserved. While their precise biological role is unclear, the caerulein- and xenopsin-related peptides may constitute a component of the animal's chemical defenses against predators. (C) 2011 Elsevier Inc. All rights reserved.",
author = "Zahid, {Osama K.} and Milena Mechkarska and Ojo, {Opeolu O.} and Yasser Abdel-Wahab and Peter Flatt and Meetani, {Mohammed A.} and Conlon, {J. Michael}",
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Caerulein-and xenopsin-related peptides with insulin-releasing activities from skin secretions of the clawed frogs, Xenopus borealis and Xenopus amieti (Pipidae). / Zahid, Osama K.; Mechkarska, Milena; Ojo, Opeolu O.; Abdel-Wahab, Yasser; Flatt, Peter; Meetani, Mohammed A.; Conlon, J. Michael.

In: General and Comparative Endocrinology, Vol. 172, No. 2, 06.2011, p. 314-320.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Caerulein-and xenopsin-related peptides with insulin-releasing activities from skin secretions of the clawed frogs, Xenopus borealis and Xenopus amieti (Pipidae)

AU - Zahid, Osama K.

AU - Mechkarska, Milena

AU - Ojo, Opeolu O.

AU - Abdel-Wahab, Yasser

AU - Flatt, Peter

AU - Meetani, Mohammed A.

AU - Conlon, J. Michael

PY - 2011/6

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N2 - Caerulein-related peptides were identified in norepinephrine-stimulated skin secretions of the tetraploid frog Xenopus borealis and the octoploid frog Xenopus amieti using negative ion electrospray mass spectrometry and their primary structures determined by positive ion tandem (MS/MS) mass spectrometry. X. borealis caerulein-B1 (pGlu-Gln-Asp-Tyr(SO(3))-Gly-Thr-Gly-Trp-Met-Asp-Phe.NH2) contains an additional Gly(5) residue compared with X. laevis caerulein and caerulein-B2 (pGlu-Asp-Tyr(SO(3))-Thr-Gly-Trp-Met-Asp-Phe.NH2) contains a Gln(2) deletion. X. amieti caerulein was identical to the X. laevis peptide. In addition, xenopsin, identical to the peptide from X. laevis, together with xenopsin-AM2 (pGlu-Gly-Arg-Arg-Pro-Trp-Ile- Leu) that contains the substitution Lys(3) -> Arg were isolated from X. amieti secretions. X. borealis caerulein-B1, and X. amieti xenopsin and xenopsin-AM2 produced significant (P < 0.05) and concentration-dependent stimulations of insulin release from the rat BRIN-BD11 clonal beta cell line at concentrations >= 30 nM. The peptides did not stimulate the release of lactate dehydrogenase at concentrations up to 3 mu M demonstrating that the integrity of the plasma membrane had been preserved. While their precise biological role is unclear, the caerulein- and xenopsin-related peptides may constitute a component of the animal's chemical defenses against predators. (C) 2011 Elsevier Inc. All rights reserved.

AB - Caerulein-related peptides were identified in norepinephrine-stimulated skin secretions of the tetraploid frog Xenopus borealis and the octoploid frog Xenopus amieti using negative ion electrospray mass spectrometry and their primary structures determined by positive ion tandem (MS/MS) mass spectrometry. X. borealis caerulein-B1 (pGlu-Gln-Asp-Tyr(SO(3))-Gly-Thr-Gly-Trp-Met-Asp-Phe.NH2) contains an additional Gly(5) residue compared with X. laevis caerulein and caerulein-B2 (pGlu-Asp-Tyr(SO(3))-Thr-Gly-Trp-Met-Asp-Phe.NH2) contains a Gln(2) deletion. X. amieti caerulein was identical to the X. laevis peptide. In addition, xenopsin, identical to the peptide from X. laevis, together with xenopsin-AM2 (pGlu-Gly-Arg-Arg-Pro-Trp-Ile- Leu) that contains the substitution Lys(3) -> Arg were isolated from X. amieti secretions. X. borealis caerulein-B1, and X. amieti xenopsin and xenopsin-AM2 produced significant (P < 0.05) and concentration-dependent stimulations of insulin release from the rat BRIN-BD11 clonal beta cell line at concentrations >= 30 nM. The peptides did not stimulate the release of lactate dehydrogenase at concentrations up to 3 mu M demonstrating that the integrity of the plasma membrane had been preserved. While their precise biological role is unclear, the caerulein- and xenopsin-related peptides may constitute a component of the animal's chemical defenses against predators. (C) 2011 Elsevier Inc. All rights reserved.

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DO - 10.1016/j.ygcen.2011.03.022

M3 - Article

VL - 172

SP - 314

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JO - General and Comparative Endocrinology

T2 - General and Comparative Endocrinology

JF - General and Comparative Endocrinology

SN - 0016-6480

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