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

FEBS Letters

Ganz, Tomas¹  Lehrer, Robert I.¹  Zhao, Chengquan¹ 

[1] Department of Medicine, UCLA Center for the Health Sciences, CHS 37-055, 10833 LeConte Avenue, Los Angeles, CA 90095-1678, USA

关键词: Protegrin;    Antimicrobial peptide;    Cathelin;    Prophenin;    PR-39;   

DOI  :  10.1016/0014-5793(95)01237-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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-κB, 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.

【 授权许可】

Unknown