Force spectroscopy of LFA-1 and its ligands, ICAM-1 and ICAM-2

被引：76

作者：

Wojcikiewicz, Ewa P. ^{[1
]}

Abdulreda, Midhat H. ^{[1
]}

Zhang, Xiaohui ^{[1
]}

Moy, Vincent T. ^{[1
]}

机构：

[1] Univ Miami, Miller Sch Med, Dept Physiol & Biophys, Miami, FL 33136 USA

来源：

BIOMACROMOLECULES | 2006年 / 7卷 / 11期

关键词：

D O I：

10.1021/bm060559c

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：

Single-molecule measurements of the interaction of leukocyte function-associated antigen-1 (LFA-1), expressed on Jurkat T cells, with intercellular adhesion molecules-1 and -2 (ICAM-1 and ICAM-2) were conducted using atomic force microscopy (AFM). The force spectra (i.e., unbinding force versus loading rate) of both the LFA-1/ICAM-1 and LFA-1/ICAM-2 interactions were acquired at a loading rate range covering 3 orders of magnitude (50-60000 pN/s) and revealed a fast loading regime and a slow loading regime. This indicates that the dissociation of both complexes involves overcoming a steep inner and a wide outer activation barrier. LFA-1 binding to ICAM-1 and ICAM-2 was strengthened in the slow loading regime by the addition of Mg2+. Differences in the dynamic strength of the LFA-1/ICAM-1 and LFA-1/ICAM-2 interactions can be attributed to the presence of wider barriers in the ICAM-2 complex, making it more responsive to a pulling force than the ICAM-1 complex.

引用

页码：3188 / 3195

页数：8

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