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LEAP2 is a cysteine-rich cationic antimicrobial peptide (Krause et al., 2003 [PubMed 12493837]).[supplied by OMIM, Mar 2008]..
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We identified the amphibian leap2 gene which is highly related to its mammalian orthologues at both structural and sequence levels. The gene is expressed in the embryo mostly in the endoderm-derived tissues. Accordingly it is induced in pluripotent animal cap cells by FGF, activin or a combination of vegT/beta-catenin (show CTNNB1 Proteins).
LEAP-2 displays antimicrobial activity against bacteria and yeasts.
These results show that the secondary structure of human LEAP-2 has a profound impact on its antibacterial activity.
Data suggest that LEAP-2 is not involved in the physiological response of GI epithelia to iron, nor is it mitogenic for epithelial cells or chemotactic for THP-1 monocytes.
report the full-length cDNA sequences of porcine hepcidin (show HAMP Proteins) and liver-expressed antimicrobial peptide-2 (LEAP-2)
LEAP2 is a cysteine-rich cationic antimicrobial peptide (Krause et al., 2003
liver expressed antimicrobial peptide 2
, liver-expressed antimicrobial peptide 2
, liver-expressed antimicrobial protein 2