Domain-specific interactions between entactin and neutrophil integrins - G2 domain ligation of integrin alpha(3)beta(1) and E domain ligation of the leukocyte response integrin signal for different responses

被引:34
作者
Gresham, HD
Graham, IL
Griffin, GL
Hsieh, JC
Dong, LJ
Chung, AE
Senior, RM
机构
[1] UNIV MISSOURI,RES SERV,TRAUMA VET ADM MED CTR,COLUMBIA,MO 65201
[2] UNIV MISSOURI,DEPT PHARMACOL,COLUMBIA,MO 65201
[3] UNIV MISSOURI,DEPT MOL MICROBIOL & IMMUNOL,COLUMBIA,MO 65201
[4] WASHINGTON UNIV,SCH MED,BARNES JEWISH HOSP,DEPT MED,RESP & CRIT CARE DIV,ST LOUIS,MO 63110
[5] UNIV PITTSBURGH,DEPT BIOL SCI,PITTSBURGH,PA 15260
关键词
D O I
10.1074/jbc.271.48.30587
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
Extracellular matrix proteins activate neutrophils to up-regulate many physiologic functions that are necessary at sites of tissue injury. To elucidate the ligand-receptor interactions that mediate these functions, we examined neutrophil activation by the basement membrane protein, entactin. Entactin is structurally and functionally organized into distinct domains; therefore, we utilized glutathione S-transferase -fusion proteins encompassing its four major domains, G1, G2, E, and G3, to assess interactions between entactin and neutrophil integrin receptors. We show that the E domain, which contains the single RGD sequence of entactin, is sufficient for ligation of the beta(3)-like integrin, leukocyte response integrin, and signaling for chemotaxis. Moreover, the G2 domain signals for stimulation of Fc receptor-mediated phagocytosis via ligation of alpha(3) beta(1). This receptor-ligand interaction was revealed only after stimulation of neutrophil by immune complexes or phorbol esters. Interestingly, the E domain does not enhance phagocytosis, and the G2 domain is not chemotactic. Furthermore, cleavage of entactin with the matrix metalloproteinase, matrilysin, liberates peptides that retain E domain-mediated chemotaxis and G2 domain-mediated enhancement of phagocytosis. These studies indicate that multiple domains of entactin have the ability to ligate individual integrins expressed by neutrophils and to activate distinct functions.
引用
收藏
页码:30587 / 30594
页数:8
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