Further characterization of a fodrin-containing transmembrane complex from mouse T-lymphoma cells.
Further characterization of a fodrin-containing transmembrane complex from mouse T-lymphoma cells.
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小鼠 T 淋巴瘤细胞中含胞因子的跨膜复合物的进一步表征。
DOI：
10.1016/0005-2736(87)90353-1
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发表时间：
1987
期刊：
影响因子：
--
通讯作者：
Bourguignon,LY
中科院分区：
文献类型：
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作者：
Suchard,SJ;Bourguignon,LY
先前通过非离子洗涤剂提取和蔗糖梯度离心的互补技术从小鼠T淋巴瘤细胞中分离到一个包含Fodrin(一种肌动蛋白结合蛋白)和一个主要表面糖蛋白(GP 180)的跨膜复合体(Bourguignon等人)。(1985)J.细胞生物学。101、477-487)。对这种复合体的分析已经扩展到验证结构关联，并进一步确定Fodrin和GP 180之间的相互作用。以下证据证实了Fodrin与GP 180之间的联系：(1)Fodrin和GP 180在蔗糖梯度上共沉淀，沉淀系数为20 S；(2)Fodrin和GP 180的比例恒定地跨越20 S峰；(3)利用抗Fodrin抗体从20 S峰特异地共沉淀GP 180和Fodrin；以及(4)利用免疫电子显微镜技术，Fodrin和GP 180从20 S峰共定位在肌动蛋白细丝上。此外，在0.6M的氯化钠存在和不存在的情况下，这种Fodrin-GP 180复合体都可以很容易地解离和重组。Fodrin-Gp180复合体具有肌动蛋白结合能力的事实表明，这种跨膜复合体可能在淋巴细胞修补和封顶过程中受体与细胞骨架之间的连接事件中发挥重要作用。
A transmembrane complex containing fodrin (an actin-binding protein) and a major surface glycoprotein (GP 180) was previously isolated from mouse T-lymphoma cells by the complementary techniques of non-ionic detergent extraction and sucrose gradient centrifugation (Bourguignon et al. (1985) J. Cell Biol. 101, 477–487). The analysis of this complex has been extended to verify the structural association and further define the interaction between fodrin and GP 180. The association between fodrin and GP 180 has been confirmed by the following evidence: (1) co-sedimentation of fodrin and GP 180 in a single peak on a sucrose gradient with a sedimentation coefficient of 20 S; (2) a constant ratio of fodrin and GP 180 across the 20 S peak; (3) the specific co-precipitation of GP 180 with fodrin from the 20 S peak using anti-fodrin antibody; and (4) the colocalization of fodrin and GP 180 from the 20 S peak on actin filaments using an immuno-electron microscopic technique. Furthermore, this fodrin-GP 180 complex can be readily dissociated and reassembled in the presence and absence of 0.6 M NaCl, respectively. The fact that this fodrin-GP 180 complex displays actin-binding ability indicates that this transmembrane complex may play an important role in the linking event between receptors and the cytoskeleton during lymphocyte patching and capping.