期刊
MOLECULAR BIOLOGY OF THE CELL
卷 29, 期 4, 页码 408-418出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E16-12-0827
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资金
- National Natural Science Foundation of China [31230027, 31110103918, 31300776]
- Strategic Priority Research Program and Frontier Science Key Project of Chinese Academy of Sciences [XDA01030102, XDB22040101, QYZDJ-SSW-JSC018]
- National Key Research and Development Program of China [2016YFA0501601]
- Visiting Scholar Foundation of the Key Laboratory of Biorheological Science and Technology (Chongqing University), Ministry of Education [CQKLBST-2015-002]
Lymphocyte function-associated antigen-1 (LFA-1) and macrophage-1 antigen (Mac-1) and their counterreceptors such as intercellular cell adhesion molecules (ICAM-1 and ICAM-2), junctional adhesion molecules (JAM-A, JAM-C), and receptors for advanced glycation end products (RAGE) are crucial for promoting polymorphonuclear leukocyte (neutrophil, PMN) recruitment. The underlying mechanisms of ligand-specific bindings in this cascade remain incompletely known. We compared the dynamic force spectra for various LFA-1/Mac1-ligand bonds using single-molecule atomic force microscopy (AFM) and tested their functions in mediating PMN recruitment under in vitro shear flow. Distinct features of bond rupture forces and lifetimes were uncovered for these ligands, implying their diverse roles in regulating PMN adhesion on endothelium. LFA-1 dominates PMN adhesion on ICAM-1 and ICAM-2, while Mac-1 mediates PMN adhesion on RAGE, JAM-A, and JAM-C, which is consistent with their bond strength. All ligands can trigger PMN spreading and polarization, in which Mac-1 seems to induce outside-in signaling more effectively. LFA-1-ICAM-1 and LFA-1/Mac-1-JAM-C bonds can accelerate PMN crawling under high shear stress, presumably due to their high mechanical strength. This work provides new insight into basic molecular mechanisms of physiological ligands of beta 2 integrins in PMN recruitment.
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