Homotypic fibrillin-1 interactions in microfibril assembly
Homotypic fibrillin-1 interactions in microfibril assembly
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DOI：
10.1074/jbc.m409029200
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发表时间：
2005-02-11
影响因子：
4.8
通讯作者：
Kielty, CM
中科院分区：
文献类型：
--
作者：
Marson, A;Rock, MJ;Kielty, CM
我们已经定义了纤维的同型相互作用。lin-1以获得对微纤维组装的新见解。N-末端片段之间、弗林蛋白酶处理的C-末端片段之间以及这些N和C-末端片段之间证明了剂量依赖性的可饱和高亲和力结合。N末端还与下游片段相互作用。后弗林蛋白酶切割位点C-末端序列也与N-末端相互作用，与其自身和与弗林蛋白酶加工的片段相互作用。未检测到其他同型的β-淀粉样蛋白-1相互作用。一些终端同型相互作用被其他终端序列抑制，并具有强烈的钙依赖性。用N-乙基马来酰亚胺处理N-末端片段减少了同型结合。微原纤维相关糖蛋白-1抑制N-至C-末端相互作用，但不抑制同型N-末端相互作用。这些repeatin-1的相互作用可能会调节细胞周repeatin-1微纤维组装。
We have defined the homotypic interactions of fibril. lin-1 to obtain new insights into microfibril assembly. Dose-dependent saturable high affinity binding was demonstrated between N-terminal fragments, between furin processed C-terminal fragments, and between these Nand C-terminal fragments. The N terminus also interacted with a downstream fragment. A post-furin cleavage site C-terminal sequence also interacted with the N terminus' with itself and with the furin-processed fragment. No other homotypic fibrillin-1 interactions were detected. Some terminal homotypic interactions were inhibited by other terminal sequences, and were strongly calcium-dependent. Treatment of an N-terminal fragment with N-ethylmaleimide reduced homotypic binding. Microfibril-associated glycoprotein-1 inhibited N- to C-terminal interactions but not homotypic N-terminal interactions. These fibrillin-1 interactions are likely to regulate pericellular fibrillin-1 microfibril assembly.