Brown S S, Malinoff H L, Wicha M S
Proc Natl Acad Sci U S A. 1983 Oct;80(19):5927-30. doi: 10.1073/pnas.80.19.5927.
A purified cell surface receptor protein for laminin (Mr = 70,000) isolated from mouse fibrosarcoma cells binds to actin with specificity and high affinity. This binding was demonstrated both by cosedimentation of the receptor with actin and binding of the receptor to actin immobilized on nitrocellulose filters. Specificity was demonstrated by displacement of 35S-labeled receptor by unlabeled receptor. Scatchard analysis of receptor binding to actin yielded a Kd of 6 X 10(-7) M. The receptor was observed to reduce the viscosity of actin filaments. It also caused the formation of bundles of parallel filaments. This observation and the stoichiometry of binding suggest that the receptor binds along the sides of actin filaments. Based on the ability of this receptor to bind both extracellular laminin and intracellular actin, we have named this protein "connectin." Connectin may be an example of a transmembrane protein that is capable of mediating the interaction of a cell with its extracellular matrix.
从小鼠纤维肉瘤细胞中分离出的一种纯化的层粘连蛋白细胞表面受体蛋白(分子量为70,000)能特异性且高亲和力地与肌动蛋白结合。通过受体与肌动蛋白的共沉降以及受体与固定在硝酸纤维素滤膜上的肌动蛋白的结合,均证实了这种结合。未标记的受体能够取代35S标记的受体,从而证明了其特异性。对受体与肌动蛋白结合的Scatchard分析得出解离常数(Kd)为6×10^(-7) M。观察到该受体可降低肌动蛋白丝的黏度,还能促使平行丝束的形成。这一观察结果以及结合的化学计量关系表明,该受体沿肌动蛋白丝的侧面结合。基于这种受体既能结合细胞外的层粘连蛋白又能结合细胞内的肌动蛋白的能力,我们将这种蛋白命名为“连接蛋白”。连接蛋白可能是一种能够介导细胞与其细胞外基质相互作用的跨膜蛋白的实例。