Membrane interactions of S100A12 (Calgranulin C).
Membrane interactions of S100A12 (Calgranulin C).
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DOI：
10.1371/journal.pone.0082555
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发表时间：
2013
期刊：
影响因子：
3.7
通讯作者：
Araujo AP
中科院分区：
文献类型：
--
作者：
Garcia AF;Lopes JL;Costa-Filho AJ;Wallace BA;Araujo AP
S100 A12（Calgranulin C）是一种小的酸性钙结合外周膜蛋白，具有两个EF-手形结构基序。它在巨噬细胞和淋巴细胞中表达，并在几种人类炎症性疾病中高度上调。在猪中，S100 A12在粒细胞的胞质溶胶中是丰富的，在那里它被认为参与炎症过程的信号调节。在这项研究中，我们研究了猪S100 A12与磷脂双层的相互作用，以及离子（Ca 2+，Zn 2+或两者一起）在修饰蛋白质-脂质相互作用中的作用。更具体地说，我们打算解决的问题，如：（1）是蛋白质膜相互作用的离子的存在调制？(2)蛋白质的整体结构是否同时受到离子和膜模型的影响？(3)当离子和膜同时存在时，会发生哪些具体的构象变化？(4)这种蛋白质对某种特定的脂质成分有什么分子偏好吗为了深入了解膜的相互作用，并回答这些问题，同步辐射圆二色光谱，荧光光谱，表面等离子体共振。这些组合技术的使用表明，这种蛋白质能够与脂质和溶液中的离子相互作用，并能够检查在不同水平的结构组织发生的变化。Ca 2+和Zn 2+离子的存在改变了蛋白质在脂质存在下的结合、构象和热稳定性。因此，研究猪S100 A12在溶液中的分子相互作用的这些研究补充了以前确定的晶体结构信息，这个家族的蛋白质，增强了我们的理解，其与膜相互作用的动力学。
S100A12 (Calgranulin C) is a small acidic calcium-binding peripheral membrane protein with two EF-hand structural motifs. It is expressed in macrophages and lymphocytes and highly up-regulated in several human inflammatory diseases. In pigs, S100A12 is abundant in the cytosol of granulocytes, where it is believed to be involved in signal modulation of inflammatory process. In this study, we investigated the interaction of the porcine S100A12 with phospholipid bilayers and the effect that ions (Ca2+, Zn2+ or both together) have in modifying protein-lipid interactions. More specifically, we intended to address issues such as: (1) is the protein-membrane interaction modulated by the presence of ions? (2) is the protein overall structure affected by the presence of the ions and membrane models simultaneously? (3) what are the specific conformational changes taking place when ions and membranes are both present? (4) does the protein have any kind of molecular preferences for a specific lipid component? To provide insight into membrane interactions and answer those questions, synchrotron radiation circular dichroism spectroscopy, fluorescence spectroscopy, and surface plasmon resonance were used. The use of these combined techniques demonstrated that this protein was capable of interacting both with lipids and with ions in solution, and enabled examination of changes that occur at different levels of structure organization. The presence of both Ca2+ and Zn2+ ions modify the binding, conformation and thermal stability of the protein in the presence of lipids. Hence, these studies examining molecular interactions of porcine S100A12 in solution complement the previously determined crystal structure information on this family of proteins, enhancing our understanding of its dynamics of interaction with membranes.
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影响因子：
2.9
作者：
Malmendal, A;Kooi, CWV;Chazin, WJ
通讯作者：
Chazin, WJ
影响因子：
2.7
作者：
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KONDO, Y
影响因子：
2.9
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KILHOFFER, MC;DEMAILLE, JG;GERARD, D
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GERARD, D
影响因子：
3.4
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Lopes, Jose Luiz S.;Nobre, Thatyane M.;Beltramini, Leila M.
通讯作者：
Beltramini, Leila M.
影响因子：
2.9
作者：
CALISSANO, P;ALEMA, S;FASELLA, P
通讯作者：
FASELLA, P