STRUCTURES OF GENES FOR 2 CATHELIN-ASSOCIATED ANTIMICROBIAL PEPTIDES - PROPHENIN-2 AND PR-39

被引:67
作者
ZHAO, CQ [1 ]
GANZ, T [1 ]
LEHRER, RI [1 ]
机构
[1] UNIV CALIF LOS ANGELES, CTR HLTH SCI, DEPT MED, LOS ANGELES, CA 90095 USA
关键词
PROTEGRIN; ANTIMICROBIAL PEPTIDE; CATHELIN; PROPHENIN; PR-39;
D O I
10.1016/0014-5793(95)01237-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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-kappa B, IL-6, GM-CSP 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.
引用
收藏
页码:130 / 134
页数:5
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