PURIFICATION AND IDENTIFICATION OF 91-KDA NEUTROPHIL GELATINASE - RELEASE BY THE ACTIVATING PEPTIDE INTERLEUKIN-8

被引:248
作者
MASURE, S [1 ]
PROOST, P [1 ]
VANDAMME, J [1 ]
OPDENAKKER, G [1 ]
机构
[1] CATHOLIC UNIV LEUVEN,REGA INST MED RES,MINDERBROEDERSSTR 10,B-3000 LOUVAIN,BELGIUM
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1991年 / 198卷 / 02期
关键词
D O I
10.1111/j.1432-1033.1991.tb16027.x
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
Human neutrophils were found to release a 91-kDa gelatinase that is serologically related to tumor-derived gelatinolytic enzymes, as evidenced by immunoprecipitation. In order to identify the neutrophil gelatinase, the activity in conditioned medium from human neutrophil suspensions was purified by affinity chromatography on a gelatin substrate. The 91-kDa active enzyme was further separated from other stainable protein bands by classical SDS/PAGE and blotting to a solid support. Amino-terminal sequence analysis of blotted proteins showed that the 91-kDa enzyme is a truncated form of tumor-derived 92-kDa gelatinase (type IV collagenase), lacking eight residues at the NH2-terminus. Sequence analysis of enzymatically inactive cleavage products of this neutrophil gelatinase demonstrated that the gelatin-binding part of the molecule is restricted to the amino-terminal third. Exocytosis of gelatinase-containing granules from neutrophils occurred spontaneously within 6 h after neutrophil plating. When the cells were triggered with the phorbol ester phorbol 12-myristate 13-acetate, a strong secretagogue, rapid gelatinase release was observed. When granulocytes were stimulated with the neutrophil-activating peptide interleukin-8, maximal exocytosis occurred within 1 h. The almost immediate release of neutrophil gelatinase after stimulation of the cells with a chemotactic factor might play a key role in remodeling of the extracellular matrix during granulocyte movement in response to chemotactic stimuli.
引用
收藏
页码:391 / 398
页数:8
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