期刊
IMMUNOBIOLOGY
卷 203, 期 4, 页码 687-698出版社
URBAN & FISCHER VERLAG
DOI: 10.1016/S0171-2985(01)80017-6
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Monoclonal antibody MEM-148 was Previously shown to recognize CD18 chains in a free form un associated within leukocyte integrin heterodimers, bur: yet it is paradoxically able to induce a high-affinity conformation in the native, cell surface expressed LFA-1 molecules. Our results based on kinetics of binding, immunoprecipitation and cell-aggregation experiments demonstrate that the mAb does bind to and stabilizes a specific confirmation of LFA-1 heterodimers apparently distinguished by an increased affinity to its cellular ligand(s). A similar high-affinity conformation of LFA-1, in which the MEM-148 epitope becomes exposed, is induced also by a Mg2+/EDTA or low pH (5.5-6.5) treatments which may mimic physiologically relevant situations in normal or inflamed tissues. Thus, mAb MEM-148 is a novel valuable tool for detection and induction of specific conformations of human leukocyte integrins.
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