Binding of Ala-scanning analogs of omega-conotoxin MVIIC to N- and P/Q-type calcium channels |
| |
Authors: | Sato K Raymond C Martin-Moutot N Sasaki T Ohtake A Minami K Van Renterghem C Kim J I Takahashi M Seagar M J |
| |
Institution: | Mitsubishi Kasei Institute of Life Sciences, 11 Minamiooya, Machida, Tokyo, Japan. kazuki@libra.ls.m-kagaku.co.jp |
| |
Abstract: | We report the isolation and characterization of a novel human peptide with antimicrobial activity, termed LEAP-1 (liver-expressed antimicrobial peptide). Using a mass spectrometric assay detecting cysteine-rich peptides, a 25-residue peptide containing four disulfide bonds was identified in human blood ultrafiltrate. LEAP-1 expression was predominantly detected in the liver, and, to a much lower extent, in the heart. In radial diffusion assays, Gram-positive Bacillus megaterium, Bacillus subtilis, Micrococcus luteus, Staphylococcus carnosus, and Gram-negative Neisseria cinerea as well as the yeast Saccharomyces cerevisiae dose-dependently exhibited sensitivity upon treatment with synthetic LEAP-1. The discovery of LEAP-1 extends the known families of mammalian peptides with antimicrobial activity by its novel disulfide motif and distinct expression pattern. |
| |
Keywords: | Antimicrobial peptide Liver Hemofiltrate Cysteine-rich peptide |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|