Structures of genes for two cathelin-associated antimicrobial peptides: prophenin-2 and PR-39.

Abstract

We characterized genes for prophenin (PF)-2 and PR-39, two cathelin-associated antimicrobial peptides found in porcine leukocytes. Both contained 4 exons and 3 introns and were compact, contiguous and highly homologous. Exons I-III encoded most of their cathelin domains. Exon IV specified the final few cathelin residues, including its conserved C-terminal valine, followed by the mature PR-39 peptide or a PF-2 precursor. The highly conserved 5' flanking sequences of this gene family contained NF-kappa B, IL-6, GM-CSF and NF-1 binding motifs and the introns were unusually conserved. These data suggest that the panoply of porcine cathelin-associated antimicrobial peptides arose relatively recently via gene reduplications and exon shuffling, and that in vivo expression of cathelin-associated antimicrobial peptides may respond to mediators generated early during infection.

• Authors: C Zhao, T Ganz, R I Lehrer
• Journal: FEBS letters (FEBS Lett) Vol. 376 Issue 3 Pg. 130-4 (Dec 04 1995) ISSN: 0014-5793 [Print] England
• PMID: 7498526 (Publication Type: Comparative Study, Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Anti-Infective Agents
• Antimicrobial Cationic Peptides
• DNA Primers
• PF-2 protein, Sus scrofa
• Peptides
• Proteins
• cathelin
• PR 39

Topics

• Amino Acid Sequence
• Animals
• Anti-Infective Agents
• Antimicrobial Cationic Peptides
• Base Sequence
• DNA Primers (chemistry)
• Genes
• Introns
• Molecular Sequence Data
• Peptides (genetics)
• Proteins (chemistry, genetics)
• Sequence Alignment
• Sequence Homology, Nucleic Acid
• Swine