Kinetic determination of focal adhesion protein formation
Kinetic determination of focal adhesion protein formation
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DOI:
10.1006/bbrc.2000.2653
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发表时间:
2000-05-10
影响因子:
3.1
通讯作者:
Goldmann, WH
中科院分区:
文献类型:
--
作者:
Goldmann, WH
I examined the binding kinetics between integrin (alpha(IIb)beta(3)) and purified focal adhesion proteins, including alpha-actinin, filamin, vinculin, talin, and F-actin. Using static light-scatter technique, I observed affinities of the order talin > filamin > F-actin > alpha-actinin > (talin when bound to vinculin) which were lower when integrin was complexed with fibronectin. No binding between integrin and vinculin was detected. The calculated dissociation constants (K-d) ranged between 0.4 mu M and 5 mu M. These results in part confirm previously published data using different methods. The modest affinity with which the focal adhesion proteins interact in vitro might be indicative of how cells, e.g., thrombocytes, gain a high degree of versatility and velocity. (C) 2000 Academic Press.