INTERACTION OF SECRETORY LEUKOCYTE PROTEASE INHIBITOR WITH PROTEINASE-3

被引:62
作者
RAO, NV
MARSHALL, BC
GRAY, BH
HOIDAL, JR
机构
[1] UNIV UTAH, MED CTR, ROOM 4R240, 50 N MED DR, SALT LAKE CITY, UT 84132 USA
[2] UNIV MINNESOTA, DEPT MICROBIOL, MINNEAPOLIS, MN 55455 USA
关键词
D O I
10.1165/ajrcmb/8.6.612
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
Secretory leukocyte protease inhibitor (SLPI) is a 12 kD nonglycosylated serine antiproteinase secreted by cells of mucosal surfaces. In human lung, SLPI is present in the respiratory epithelium. It is the major barrier to tissue destruction mediated by the polymorphonuclear leukocyte (PMN) serine proteinases, elastase and cathepsin G, within the upper respiratory tract. We have recently described a third PMN serine proteinase, proteinase-3, that like elastase causes lung matrix destruction and experimental emphysema. The current studies examine interactions between SLPI and proteinase-3. The results show that: (1) SLPI and its reactive-site variants have no or minimal inhibitory activity against proteinase-3; (2) native SLPI does not complex with proteinase-3; (3) proteinase-3 selectively degrades both native and oxidized SLPI; (4) the cleavage of SLPI by proteinase-3 occurs at the peptide bond COOH-terminal to Ala-16 in the NH2-terminal domain of SLPI.
引用
收藏
页码:612 / 616
页数:5
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