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 H.A. Abdel-Wahab; Peter R. Flatt; Mohammed A. Meetani; J. Michael Conlon

doi:10.1016/j.ygcen.2011.03.022

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 H.A. Abdel-Wahab, Peter R. Flatt, Mohammed A. Meetani, J. Michael Conlon

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

24 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(SO₃)-Gly-Thr-Gly-Trp-Met-Asp-Phe.NH2) contains an additional Gly⁵ residue compared with X. laevis caerulein and caerulein-B2 (pGlu-Asp-Tyr(SO₃)-Thr-Gly-Trp-Met-Asp-Phe.NH2) contains a Gln² 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 Lys³→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 β cell line at concentrations ≥30nM. The peptides did not stimulate the release of lactate dehydrogenase at concentrations up to 3μM 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.

Original language	English
Pages (from-to)	314-320
Number of pages	7
Journal	General and Comparative Endocrinology
Volume	172
Issue number	2
DOIs	https://doi.org/10.1016/j.ygcen.2011.03.022
Publication status	Published - Jun 1 2011

Keywords

Caerulein
Frog skin secretions
Insulin release
Mass spectrometry
Xenopsin
Xenopus

ASJC Scopus subject areas

Animal Science and Zoology
Endocrinology

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10.1016/j.ygcen.2011.03.022

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Zahid, O. K., Mechkarska, M., Ojo, O. O., Abdel-Wahab, Y. H. A., Flatt, P. R., Meetani, M. A., & Conlon, J. M. (2011). Caerulein-and xenopsin-related peptides with insulin-releasing activities from skin secretions of the clawed frogs, Xenopus borealis and Xenopus amieti (Pipidae). General and Comparative Endocrinology, 172(2), 314-320. https://doi.org/10.1016/j.ygcen.2011.03.022

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. et al.
In: General and Comparative Endocrinology, Vol. 172, No. 2, 01.06.2011, p. 314-320.

Research output: Contribution to journal › Article › peer-review

Zahid, OK, Mechkarska, M, Ojo, OO, Abdel-Wahab, YHA, Flatt, PR, Meetani, MA & Conlon, JM 2011, 'Caerulein-and xenopsin-related peptides with insulin-releasing activities from skin secretions of the clawed frogs, Xenopus borealis and Xenopus amieti (Pipidae)', General and Comparative Endocrinology, vol. 172, no. 2, pp. 314-320. https://doi.org/10.1016/j.ygcen.2011.03.022

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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(SO3)-Gly-Thr-Gly-Trp-Met-Asp-Phe.NH2) contains an additional Gly5 residue compared with X. laevis caerulein and caerulein-B2 (pGlu-Asp-Tyr(SO3)-Thr-Gly-Trp-Met-Asp-Phe.NH2) contains a Gln2 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 Lys3→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 β cell line at concentrations ≥30nM. The peptides did not stimulate the release of lactate dehydrogenase at concentrations up to 3μM 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.",

keywords = "Caerulein, Frog skin secretions, Insulin release, Mass spectrometry, Xenopsin, Xenopus",

author = "Zahid, {Osama K.} and Milena Mechkarska and Ojo, {Opeolu O.} and Abdel-Wahab, {Yasser H.A.} and Flatt, {Peter R.} and Meetani, {Mohammed A.} and Conlon, {J. Michael}",

note = "Funding Information: This work was supported by an Interdisciplinary Grant ( 01-03-2-12/08 ) and a Faculty Support Grant ( NP-10-11/103 ) from United Arab Emirates University . The authors thank Laurey Steinke and Michele Fontaine (University of Nebraska Medical Center, Omaha, NE, USA) for amino acid composition analysis.",

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AU - Zahid, Osama K.

AU - Mechkarska, Milena

AU - Ojo, Opeolu O.

AU - Abdel-Wahab, Yasser H.A.

AU - Flatt, Peter R.

AU - Meetani, Mohammed A.

AU - Conlon, J. Michael

N1 - Funding Information: This work was supported by an Interdisciplinary Grant ( 01-03-2-12/08 ) and a Faculty Support Grant ( NP-10-11/103 ) from United Arab Emirates University . The authors thank Laurey Steinke and Michele Fontaine (University of Nebraska Medical Center, Omaha, NE, USA) for amino acid composition analysis.

PY - 2011/6/1

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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(SO3)-Gly-Thr-Gly-Trp-Met-Asp-Phe.NH2) contains an additional Gly5 residue compared with X. laevis caerulein and caerulein-B2 (pGlu-Asp-Tyr(SO3)-Thr-Gly-Trp-Met-Asp-Phe.NH2) contains a Gln2 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 Lys3→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 β cell line at concentrations ≥30nM. The peptides did not stimulate the release of lactate dehydrogenase at concentrations up to 3μM 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.

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(SO3)-Gly-Thr-Gly-Trp-Met-Asp-Phe.NH2) contains an additional Gly5 residue compared with X. laevis caerulein and caerulein-B2 (pGlu-Asp-Tyr(SO3)-Thr-Gly-Trp-Met-Asp-Phe.NH2) contains a Gln2 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 Lys3→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 β cell line at concentrations ≥30nM. The peptides did not stimulate the release of lactate dehydrogenase at concentrations up to 3μM 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.

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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)

Abstract

Keywords

ASJC Scopus subject areas

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