Interaction of annexins IV and VI with ATP. An alternative mechanism by which a cellular function of these calcium- and membrane-binding proteins is regulated.
Interaction of annexins IV and VI with ATP. An alternative mechanism by which a cellular function of these calcium- and membrane-binding proteins is regulated.
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膜联蛋白 IV 和 VI 与 ATP 的相互作用。
DOI：
10.1016/s0014-5793(97)00534-6
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发表时间：
1997
期刊：
影响因子：
3.5
通讯作者：
Awasthi,YC
中科院分区：
文献类型：
--
作者：
Bandorowicz-Pikuła,J;Awasthi,YC
猪肝膜联蛋白VI可与8-叠氮基-[γ-32P]三磷酸腺苷以浓度依赖的饱和方式进行光亲和标记。标记的程度随钙浓度的不同而不同。核苷酸的离解常数被发现在报道的范围内的三磷酸腺苷结合蛋白。ATP类似物，2‘-(或3’)-O-(2，4，6-三硝基苯基)腺苷5‘-三磷酸，也与AnxVI结合，在蛋白质存在下其荧光光谱发生变化。AnxIV没有观察到任何显著的8-叠氮基-ATP或TNP-ATP结合。ATP调节AnxVI与红细胞膜的结合，并增加AnxVI与F-肌动蛋白半最大结合所需的钙离子浓度。
Annexin VI from porcine liver can be photoaffinity-labeled with 8-azido-[γ-32P]ATP in a concentration-dependent, saturable manner. The extent of labeling varied with the concentration of calcium. The dissociation constant for the nucleotide was found to be in the range reported for ATP-binding proteins. The ATP analog, 2′-(or 3′)-O-(2,4,6-trinitrophenyl)adenosine 5′-triphosphate, also bound to AnxVI, as indicated by shift in its fluorescence spectra in the presence of protein. Any significant 8-azido-ATP or TNP-ATP binding was not observed with AnxIV. ATP modulated the binding of AnxVI to erythrocyte membrane and increased the Ca2+concentration required for half-maximal binding of AnxVI to F-actin.