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钙离子结合蛋白MRP8和MRP14的异二聚体与花生四烯酸结合。

The heterodimer of the Ca2+-binding proteins MRP8 and MRP14 binds to arachidonic acid.

作者信息

Klempt M, Melkonyan H, Nacken W, Wiesmann D, Holtkemper U, Sorg C

机构信息

Institute of Experimental Dermatology, University of Münster,

出版信息

FEBS Lett. 1997 May 12;408(1):81-4. doi: 10.1016/s0014-5793(97)00394-3.

Abstract

The S100 proteins MRP8 and MRP14 have been shown to be expressed by myeloid cells during inflammatory reactions. Since the majority of S100 proteins exhibit their biological activity when associated as complex it was investigated whether murine MRP8 and MRP14 form heterodimers and whether this complex may bind lipids of the cell membrane. This is of particular importance since their anchoring into the plasma membrane is unclear although upon calcium binding the proteins translocate from the cytoplasma to the cytoskeleton and the plasma membrane. Using recombinant proteins we could show that not the monomers but only the heterodimers specifically bind arachidonic acid. This finding opens new perspectives for the role of MRP8 and MRP14 in acute and chronic inflammatory processes.

摘要

S100蛋白MRP8和MRP14已被证明在炎症反应期间由髓样细胞表达。由于大多数S100蛋白在形成复合物时表现出其生物学活性,因此研究了小鼠MRP8和MRP14是否形成异二聚体,以及这种复合物是否可能结合细胞膜的脂质。这一点尤为重要,因为尽管在钙结合后蛋白质从细胞质转移到细胞骨架和质膜,但它们在质膜中的锚定尚不清楚。使用重组蛋白,我们可以证明不是单体而是只有异二聚体特异性结合花生四烯酸。这一发现为MRP8和MRP14在急性和慢性炎症过程中的作用开辟了新的视角。

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