1. Alarin but not its alternative-splicing form, GALP (Galanin-like peptide) has antimicrobial activity.
- Author
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Wada A, Wong PF, Hojo H, Hasegawa M, Ichinose A, Llanes R, Kubo Y, Senba M, and Ichinose Y
- Subjects
- Amino Acid Sequence, Animals, Antimicrobial Cationic Peptides, Cathelicidins pharmacology, Cell Membrane drug effects, Erythrocytes drug effects, Escherichia coli growth & development, Escherichia coli ultrastructure, Hemolysis, Horses blood, Humans, Microbial Sensitivity Tests, Microscopy, Electron, Scanning, Molecular Sequence Data, Staphylococcus aureus drug effects, Staphylococcus aureus growth & development, Anti-Bacterial Agents pharmacology, Escherichia coli drug effects, Galanin-Like Peptide analogs & derivatives, Galanin-Like Peptide pharmacology
- Abstract
Alarin is an alternative-splicing form of GALP (galanin-like peptide). It shares only 5 conserved amino acids at the N-terminal region with GALP which is involved in a diverse range of normal brain functions. This study seeks to investigate whether alarin has additional functions due to its differences from GALP. Here, we have shown using a radial diffusion assay that alarin but not GALP inhibited the growth of Escherichia coli (strain ML-35). The conserved N-terminal region, however, remained essential for the antimicrobial activity of alarin as truncated peptides showed reduced killing effect. Moreover, alarin inhibited the growth of E. coli in a similar potency as human cathelicidin LL-37, a well-studied antimicrobial peptide. Electron microscopy further showed that alarin induced bacterial membrane blebbing but unlike LL-37, it did not cause hemolysis of erythrocytes. In addition, alarin is only active against the gram-negative bacteria, E. coli but not the gram-positive bacteria, Staphylococcus aureus. Thus, these data suggest that alarin has potentials as an antimicrobial and should be considered for the development in human therapeutics., (Copyright © 2013 Elsevier Inc. All rights reserved.)
- Published
- 2013
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