Abstract
The dorsal skin of the crawfish frog, Rana areolata, is associated with numerous prominent granular glands. Proteomic analysis of electrically stimulated skin secretions from these glands enabled the identification and characterization of eight peptides with antimicrobial and hemolytic activity belonging to the previously identified brevinin-1, temporin-1, palustrin-2, palustrin-3, esculentin-1 (two peptides), and ranatuerin-2 (two peptides) families. The primary structures of the peptides were consistent with a close phylogenetic relationship between R. areolata and the pickerel frog, Rana palustris. Three structurally related cationic, cysteine-containing peptides were identified that show sequence similarity to peptide Leucine-Arginine, a peptide with immunomodulatory and histamine-releasing properties from the skin of the northern leopard frog, Rana pipiens. The skin secretions contained a 61-amino-acid-residue peptide that inhibited porcine trypsin and possessed a 10-cysteine-residue motif that is characteristic of a protease inhibitor previously isolated from the parasitic nematode, Ascaris suum. A 48-amino-acid-residue protein containing eight cysteine residues in the whey acidic protein (WAP) motif, characteristic of elafin (skin-derived antileukoproteinase) and secretory leukocyte protease inhibitor, was also isolated. The data suggest that protease inhibitors in skin secretions may play a role complementary to cationic, amphipathic α-helical peptides in protecting anurans from invasions by microorganisms.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 55-63 |
| Number of pages | 9 |
| Journal | Biochimica et Biophysica Acta - Proteins and Proteomics |
| Volume | 1601 |
| Issue number | 1 |
| DOIs | |
| State | Published - Nov 19 2002 |
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All Science Journal Classification (ASJC) codes
- Analytical Chemistry
- Biophysics
- Biochemistry
- Molecular Biology
Cite this
Antimicrobial peptides and protease inhibitors in the skin secretions of the crawfish frog, Rana areolata. / Ali, Mohamed F.; Lips, Karen R.; Knoop, Floyd C.; Fritzsch, Bernd; Miller, Caroline; Conlon, J. Michael.
In: Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1601, No. 1, 19.11.2002, p. 55-63.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Antimicrobial peptides and protease inhibitors in the skin secretions of the crawfish frog, Rana areolata
AU - Ali, Mohamed F.
AU - Lips, Karen R.
AU - Knoop, Floyd C.
AU - Fritzsch, Bernd
AU - Miller, Caroline
AU - Conlon, J. Michael
PY - 2002/11/19
Y1 - 2002/11/19
N2 - The dorsal skin of the crawfish frog, Rana areolata, is associated with numerous prominent granular glands. Proteomic analysis of electrically stimulated skin secretions from these glands enabled the identification and characterization of eight peptides with antimicrobial and hemolytic activity belonging to the previously identified brevinin-1, temporin-1, palustrin-2, palustrin-3, esculentin-1 (two peptides), and ranatuerin-2 (two peptides) families. The primary structures of the peptides were consistent with a close phylogenetic relationship between R. areolata and the pickerel frog, Rana palustris. Three structurally related cationic, cysteine-containing peptides were identified that show sequence similarity to peptide Leucine-Arginine, a peptide with immunomodulatory and histamine-releasing properties from the skin of the northern leopard frog, Rana pipiens. The skin secretions contained a 61-amino-acid-residue peptide that inhibited porcine trypsin and possessed a 10-cysteine-residue motif that is characteristic of a protease inhibitor previously isolated from the parasitic nematode, Ascaris suum. A 48-amino-acid-residue protein containing eight cysteine residues in the whey acidic protein (WAP) motif, characteristic of elafin (skin-derived antileukoproteinase) and secretory leukocyte protease inhibitor, was also isolated. The data suggest that protease inhibitors in skin secretions may play a role complementary to cationic, amphipathic α-helical peptides in protecting anurans from invasions by microorganisms.
AB - The dorsal skin of the crawfish frog, Rana areolata, is associated with numerous prominent granular glands. Proteomic analysis of electrically stimulated skin secretions from these glands enabled the identification and characterization of eight peptides with antimicrobial and hemolytic activity belonging to the previously identified brevinin-1, temporin-1, palustrin-2, palustrin-3, esculentin-1 (two peptides), and ranatuerin-2 (two peptides) families. The primary structures of the peptides were consistent with a close phylogenetic relationship between R. areolata and the pickerel frog, Rana palustris. Three structurally related cationic, cysteine-containing peptides were identified that show sequence similarity to peptide Leucine-Arginine, a peptide with immunomodulatory and histamine-releasing properties from the skin of the northern leopard frog, Rana pipiens. The skin secretions contained a 61-amino-acid-residue peptide that inhibited porcine trypsin and possessed a 10-cysteine-residue motif that is characteristic of a protease inhibitor previously isolated from the parasitic nematode, Ascaris suum. A 48-amino-acid-residue protein containing eight cysteine residues in the whey acidic protein (WAP) motif, characteristic of elafin (skin-derived antileukoproteinase) and secretory leukocyte protease inhibitor, was also isolated. The data suggest that protease inhibitors in skin secretions may play a role complementary to cationic, amphipathic α-helical peptides in protecting anurans from invasions by microorganisms.
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U2 - 10.1016/S1570-9639(02)00432-6
DO - 10.1016/S1570-9639(02)00432-6
M3 - Article
VL - 1601
SP - 55
EP - 63
JO - Biochimica et Biophysica Acta - Proteins and Proteomics
JF - Biochimica et Biophysica Acta - Proteins and Proteomics
SN - 1570-9639
IS - 1
ER -