Peptide Tyrosine Arginine, a potent immunomodulatory peptide isolated and structurally characterized from the skin secretions of the dusky gopher frog, Rana sevosa

C Graham, A. E. Irvine, Stephen McClean, S. C. Richter, Peter Flatt, C. Shaw

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

An octadecapeptide was isolated from the skin secretions of the dusky gopher frog (Rana sevosa) on the basis of histamine release from rat peritoneal mast cells. This peptide was purified to homogeneity by HPLC and found to have the following primary structure, YLKGCWTKSYPPKPCFSR, using both Edman degradation chemistry and peptide sequencing using high-resolution mass spectrometry (Q-TOF MS). The peptide, named peptide Tyrosine Arginine (pYR) shares 77.8% homology with peptide Leucine Arginine (pLR). The effects of the natural amidated peptide, non-amidated peptide and C-loop region of pYR on granulopoiesis and neutrophil apoptosis were investigated. All three analogues inhibited the early development of granulocyte macrophage colonies from bone marrow stem cells but did not induce apoptosis of the end stage granulocytes, the mature neutrophil. Thus, pYR is a novel member of an important and emerging new class of amphibian peptides with hemopoietic actions.
LanguageEnglish
Pages737-743
JournalPeptides
Volume26
Issue number5
Publication statusPublished - May 2005

Fingerprint

Tyrosine
Arginine
Skin
Peptides
Apoptosis
Macrophages
Stem cells
Histamine
Mass spectrometry
Rats
Bone
Degradation

Keywords

  • Amino Acid Sequence
  • Amphibian Proteins/chemistry/isolation &amp
  • purification/pharmacology
  • Animals
  • Colony-Forming Units Assay
  • Granulocytes/drug effects
  • Histamine Release/drug effects
  • Immunologic Factors/chemistry/isolation &amp
  • Macrophages/drug effects
  • Male
  • Mast Cells/drug effects
  • Molecular Sequence Data
  • Peptides/chemistry/isolation &amp
  • purification
  • Ranidae/metabolism
  • Rats
  • Skin/secretion

Cite this

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title = "Peptide Tyrosine Arginine, a potent immunomodulatory peptide isolated and structurally characterized from the skin secretions of the dusky gopher frog, Rana sevosa",
abstract = "An octadecapeptide was isolated from the skin secretions of the dusky gopher frog (Rana sevosa) on the basis of histamine release from rat peritoneal mast cells. This peptide was purified to homogeneity by HPLC and found to have the following primary structure, YLKGCWTKSYPPKPCFSR, using both Edman degradation chemistry and peptide sequencing using high-resolution mass spectrometry (Q-TOF MS). The peptide, named peptide Tyrosine Arginine (pYR) shares 77.8{\%} homology with peptide Leucine Arginine (pLR). The effects of the natural amidated peptide, non-amidated peptide and C-loop region of pYR on granulopoiesis and neutrophil apoptosis were investigated. All three analogues inhibited the early development of granulocyte macrophage colonies from bone marrow stem cells but did not induce apoptosis of the end stage granulocytes, the mature neutrophil. Thus, pYR is a novel member of an important and emerging new class of amphibian peptides with hemopoietic actions.",
keywords = "Amino Acid Sequence, Amphibian Proteins/chemistry/isolation &amp, purification/pharmacology, Animals, Colony-Forming Units Assay, Granulocytes/drug effects, Histamine Release/drug effects, Immunologic Factors/chemistry/isolation &amp, Macrophages/drug effects, Male, Mast Cells/drug effects, Molecular Sequence Data, Peptides/chemistry/isolation &amp, purification, Ranidae/metabolism, Rats, Skin/secretion",
author = "C Graham and Irvine, {A. E.} and Stephen McClean and Richter, {S. C.} and Peter Flatt and C. Shaw",
note = "LR: 20061115; PUBM: Print-Electronic; DEP: 20050113; JID: 8008690; 0 (Amphibian Proteins); 0 (Immunologic Factors); 0 (Peptides); 0 (peptide tyrosine arginine, Rana sevosa); 2004/10/26 [received]; 2004/12/08 [revised]; 2004/12/08 [accepted]; 2005/01/13 [aheadofprint]; ppublish",
year = "2005",
month = "5",
language = "English",
volume = "26",
pages = "737--743",
number = "5",

}

Peptide Tyrosine Arginine, a potent immunomodulatory peptide isolated and structurally characterized from the skin secretions of the dusky gopher frog, Rana sevosa. / Graham, C; Irvine, A. E.; McClean, Stephen; Richter, S. C.; Flatt, Peter; Shaw, C.

Vol. 26, No. 5, 05.2005, p. 737-743.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Peptide Tyrosine Arginine, a potent immunomodulatory peptide isolated and structurally characterized from the skin secretions of the dusky gopher frog, Rana sevosa

AU - Graham, C

AU - Irvine, A. E.

AU - McClean, Stephen

AU - Richter, S. C.

AU - Flatt, Peter

AU - Shaw, C.

N1 - LR: 20061115; PUBM: Print-Electronic; DEP: 20050113; JID: 8008690; 0 (Amphibian Proteins); 0 (Immunologic Factors); 0 (Peptides); 0 (peptide tyrosine arginine, Rana sevosa); 2004/10/26 [received]; 2004/12/08 [revised]; 2004/12/08 [accepted]; 2005/01/13 [aheadofprint]; ppublish

PY - 2005/5

Y1 - 2005/5

N2 - An octadecapeptide was isolated from the skin secretions of the dusky gopher frog (Rana sevosa) on the basis of histamine release from rat peritoneal mast cells. This peptide was purified to homogeneity by HPLC and found to have the following primary structure, YLKGCWTKSYPPKPCFSR, using both Edman degradation chemistry and peptide sequencing using high-resolution mass spectrometry (Q-TOF MS). The peptide, named peptide Tyrosine Arginine (pYR) shares 77.8% homology with peptide Leucine Arginine (pLR). The effects of the natural amidated peptide, non-amidated peptide and C-loop region of pYR on granulopoiesis and neutrophil apoptosis were investigated. All three analogues inhibited the early development of granulocyte macrophage colonies from bone marrow stem cells but did not induce apoptosis of the end stage granulocytes, the mature neutrophil. Thus, pYR is a novel member of an important and emerging new class of amphibian peptides with hemopoietic actions.

AB - An octadecapeptide was isolated from the skin secretions of the dusky gopher frog (Rana sevosa) on the basis of histamine release from rat peritoneal mast cells. This peptide was purified to homogeneity by HPLC and found to have the following primary structure, YLKGCWTKSYPPKPCFSR, using both Edman degradation chemistry and peptide sequencing using high-resolution mass spectrometry (Q-TOF MS). The peptide, named peptide Tyrosine Arginine (pYR) shares 77.8% homology with peptide Leucine Arginine (pLR). The effects of the natural amidated peptide, non-amidated peptide and C-loop region of pYR on granulopoiesis and neutrophil apoptosis were investigated. All three analogues inhibited the early development of granulocyte macrophage colonies from bone marrow stem cells but did not induce apoptosis of the end stage granulocytes, the mature neutrophil. Thus, pYR is a novel member of an important and emerging new class of amphibian peptides with hemopoietic actions.

KW - Amino Acid Sequence

KW - Amphibian Proteins/chemistry/isolation &amp

KW - purification/pharmacology

KW - Animals

KW - Colony-Forming Units Assay

KW - Granulocytes/drug effects

KW - Histamine Release/drug effects

KW - Immunologic Factors/chemistry/isolation &amp

KW - Macrophages/drug effects

KW - Male

KW - Mast Cells/drug effects

KW - Molecular Sequence Data

KW - Peptides/chemistry/isolation &amp

KW - purification

KW - Ranidae/metabolism

KW - Rats

KW - Skin/secretion

M3 - Article

VL - 26

SP - 737

EP - 743

IS - 5

ER -