Institute of Biochemistry and Molecular Cell Biology, RWTH Aachen University Aachen, Germany.
Front Immunol. 2013 May 16;4:115. doi: 10.3389/fimmu.2013.00115. eCollection 2013.
Macrophage migration inhibitory factor (MIF) has been defined as an important chemokine-like function (CLF) chemokine with an essential role in monocyte recruitment and arrest. Adhesion of monocytes to the vessel wall and their transendothelial migration are critical in atherogenesis and many other inflammatory diseases. Chemokines carefully control all steps of the monocyte recruitment process. Those chemokines specialized in controlling arrest are typically immobilized on the endothelial surface, mediating the arrest of rolling monocytes by chemokine receptor-triggered pathways. The chemokine receptor CXCR2 functions as an important arrest receptor on monocytes. An arrest function has been revealed for the bona fide CXCR2 ligands CXCL1 and CXCL8, but genetic studies also suggested that additional arrest chemokines are likely to be involved in atherogenic leukocyte recruitment. While CXCR2 is known to interact with numerous CXC chemokine ligands, the CLF chemokine MIF, which structurally does not belong to the CXC chemokine sub-family, was surprisingly identified as a non-cognate ligand of CXCR2, responsible for critical arrest functions during the atherogenic process. MIF was originally identified as macrophage migration inhibitory factor (this function being eponymous), but is now known as a potent inflammatory cytokine with CLFs including chemotaxis and leukocyte arrest. This review will cover the mechanisms underlying these functions, including MIF's effects on LFA1 integrin activity and signal transduction, and will discuss the structural similarities between MIF and the bona fide CXCR2 ligand CXCL8 while emphasizing the structural differences. As MIF also interacts with CXCR4, a chemokine receptor implicated in CXCL12-elicited lymphocyte arrest, the arrest potential of the MIF/CXCR4 axis will also be scrutinized as well as the recently identified role of pericyte MIF in attracting leukocytes exiting through venules as part of the pericyte "motility instruction program."
巨噬细胞移动抑制因子 (MIF) 已被定义为一种重要的趋化因子样功能 (CLF) 趋化因子,在单核细胞募集和捕获中起关键作用。单核细胞与血管壁的黏附和跨内皮迁移在动脉粥样硬化形成和许多其他炎症性疾病中至关重要。趋化因子精细地控制单核细胞募集过程的所有步骤。那些专门控制捕获的趋化因子通常固定在血管内皮表面,通过趋化因子受体触发途径介导滚动单核细胞的捕获。趋化因子受体 CXCR2 作为单核细胞上的重要捕获受体发挥作用。已经揭示了真正的 CXCR2 配体 CXCL1 和 CXCL8 的捕获功能,但遗传研究也表明,其他可能参与动脉粥样硬化白细胞募集的捕获趋化因子。虽然已知 CXCR2 与许多 CXC 趋化因子配体相互作用,但结构上不属于 CXC 趋化因子亚家族的 CLF 趋化因子 MIF 出人意料地被鉴定为 CXCR2 的非同源配体,负责动脉粥样形成过程中的关键捕获功能。MIF 最初被鉴定为巨噬细胞移动抑制因子(这个功能是同名的),但现在已知是一种有效的炎症细胞因子,具有包括趋化性和白细胞捕获在内的 CLFs。这篇综述将涵盖这些功能的机制,包括 MIF 对 LFA1 整合素活性和信号转导的影响,并将讨论 MIF 与真正的 CXCR2 配体 CXCL8 之间的结构相似性,同时强调结构差异。由于 MIF 还与 CXCR4 相互作用,后者是与 CXCL12 诱导的淋巴细胞捕获有关的趋化因子受体,因此也将仔细研究 MIF/CXCR4 轴的捕获潜力以及最近发现的周细胞 MIF 在吸引通过小静脉离开的白细胞中的作用,作为周细胞“运动指令程序”的一部分。