Differential modulation of annexin I binding sites on monocytes and neutrophils

被引:29
作者
Euzger, HS
Flower, RJ
Goulding, NJ
Perretti, M
机构
[1] William Harvey Res Inst, London EC1M 6BQ, England
[2] Dept Biochem Pharmacol, Arthrit Res Unit, London EC1M 6BQ, England
基金
英国惠康基金;
关键词
lipocortin; 1; superoxide; phagocyte; glucocorticoid; elastase; adhesion;
D O I
10.1080/09629359990720
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
SPECIFIC binding sites for the anti-inflammatory protein annexin I have been detected on the surface of human monocytes and polymorphonuclear leukocytes (PMN), These binding sites are proteinaceous in nature and are sensitive to cleavage by the proteolytic enzymes trypsin, collagenase, elastase and cathepsin G, When monocytes and PMN were isolated independently from peripheral blood, only the monocytes exhibited constitutive annexin I binding, However PMN acquired the capacity to bind annexin I following co-culture with monocytes, PMN incubation with sodium azide, but not protease inhibitors, partially blocked this process. A similar increase in annexin I binding capacity was also detected in PMN following adhesion to endothelial monolayers. We propose that a juxtacrine activation rather than a cleavage-mediated transfer is involved in this process, Removal of annexin I binding sites from monocytes with elastase rendered monocytes functionally insensitive to full length annexin I or to the annexin I-derived pharmacophore, peptide Ac2-26, assessed as suppression of the respiratory burst. These data indicate that the annexin I binding site on phagocytic cells may have an important function in the feedback control of the inflammatory response and their loss through cleavage could potentiate such responses.
引用
收藏
页码:53 / 62
页数:10
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