INHIBITION OF CELL-ADHESION BY HIGH-MOLECULAR-WEIGHT KININOGEN

被引:93
作者
ASAKURA, S
HURLEY, RW
SKORSTENGAARD, K
OHKUBO, I
MOSHER, DF
机构
[1] UNIV WISCONSIN,DEPT PHYSIOL CHEM,MADISON,WI 53706
[2] AARHUS UNIV,DEPT MOLEC BIOL,GENE EXPRESS LAB,DK-8000 AARHUS,DENMARK
[3] SHIGA UNIV MED SCI,DEPT BIOCHEM,OTSU,SHIGA 52021,JAPAN
关键词
D O I
10.1083/jcb.116.2.465
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
An anti-cell adhesion globulin was purified from human plasma by heparin-affinity chromatography. The purified globulin inhibited spreading of osteosarcoma and melanoma cells on vitronectin, and of endothelial cells, platelets, and mononuclear blood cells on vitronectin or fibrinogen. It did not inhibit cell spreading on fibronectin. The protein had the strongest anti-adhesive effect when preadsorbed onto the otherwise adhesive surfaces. Amino acid sequence analysis revealed that the globulin is cleaved (kinin-free) high molecular weight kininogen (HKa). Globulin fractions from normal plasma immunodepleted of high molecular weight kininogen (HK) or from an individual deficient of HK lacked adhesive activity. Uncleaved single-chain HK preadsorbed at neutral pH, HKa preadsorbed at pH > 8.0, and HKa degraded further to release its histidine-rich domain had little anti-adhesive activity. These results indicate that the cationic histidine-rich domain is critical for anti-adhesive activity and is somehow mobilized upon cleavage. Vitronectin was not displaced from the surface by HKa. Thus, cleavage of HK by kallikrein results in both release of bradykinin, a potent vasoactive and growth-promoting peptide, and formation of a potent anti-adhesive protein.
引用
收藏
页码:465 / 476
页数:12
相关论文
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