IDENTIFICATION OF A NEW-PROTEIN LOCALIZED AT SITES OF CELL-SUBSTRATE ADHESION
IDENTIFICATION OF A NEW-PROTEIN LOCALIZED AT SITES OF CELL-SUBSTRATE ADHESION
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DOI：
10.1083/jcb.103.5.1679
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发表时间：
1986-11-01
影响因子：
7.8
通讯作者：
BECKERLE, MC
中科院分区：
文献类型：
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作者：
BECKERLE, MC
通过对非免疫兔血清的分析，鉴定出了在细胞-基质粘附位点发现的一种新蛋白质。通过间接免疫荧光，该血清对培养鸡细胞中的焦点接触（粘附斑）和肌动蛋白丝束的相关末端进行染色。鸡胚成纤维细胞总蛋白的蛋白质免疫印迹分析表明，普通血清识别的主要蛋白具有 82-kD 的多肽。该82-KD蛋白在免疫学上不同于其他已知的粘附斑蛋白，例如纽蛋白、踝蛋白、α-肌动蛋白和纤毛蛋白。针对电泳分离的硝化纤维结合的 82-kD 蛋白进行亲和纯化的抗体保留了对粘附斑块区域进行染色的能力，这证实了 82-kD 蛋白确实是焦点接触的组成部分。 82-kD 的多肽相对于肌动蛋白和纤连蛋白具有基本等电点，并且其丰度似乎非常低。 82-kD 蛋白质在鸡胚胎组织中普遍存在。然而，它似乎在成纤维细胞和平滑肌中比在大脑或肝脏中更丰富。在骨骼肌和心肌中检测到中等水平的蛋白质。 82-kD 蛋白质的亚细胞分布提出了这种多肽参与将肌动蛋白丝连接至质膜的底物附着位点或调节这些动态相互作用的可能性。
A new protein found at sites of cell-substrate adhesion has been identified by analysis of a nonimmune rabbit serum. By indirect immunofluorescence this serum stains focal contacts (adhesion plaques) and the associated termini of actin filament bundles in cultured chicken cells. Western immunoblot analysis of total chick embryo fibroblast protein demonstrated an 82-kD polypeptide to the major protein recognized by the unfractionated serum. This 82- KD protein is immunologically distinct from other known adhesion plaque proteins such as vinculin, talin, .alpha.-actinin, and fimbrin. Antibody affinity-purified against the electrophoretically isolated, nitrocellulose-bound 82-kD protein retained the ability to stain the area of the adhesion plaque, which confirms that the 82-kD protein is indeed a constituent of the focal contact. The 82-kD polypeptide has a basic isoelectric point relative to actin and fibronectin, and it appears to be very low in abundance. The 82-kD protein is ubiquitous in chicken embryo tissues. However, it appears to be more abundant in fibroblasts and smooth muscle than in brain or liver. Intermediate levels of the protein were detected in skeletal and cardiac muscle. The subcellular distribution of the 82-kD protein raises the possibility that this polypeptide is involved in linking actin filaments to the plasma membrane at sites of substrate attachment or regulating these dynamic interactions.