Monoclonal antibodies to ligand-occupied conformers of integrin alpha IIb beta 3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function.
作者： AL Frelinger 3rd , XP Du , Edward F Plow , Mark H Ginsberg , None
DOI: 10.1016/S0021-9258(19)47346-8
关键词:
摘要: Occupancy of integrin receptors induces conformational changes in the receptor, resulting exposure novel interactive sites termed ligand-induced binding (LIBS). We report here that Fab fragments certain antibodies against LIBS on alpha IIb beta 3 (platelet glycoprotein IIb-IIIa) block platelet aggregation. Thus, or regions surrounding them may participate events required for In addition, anti-alpha stimulated This was due to induction fg 3, apparently by shifting a equilibrium between "resting" and an "activated" state 3. Some activating anti-LIBS also induced high affinity fibronectin whereas others did not. conformation this modulate both specificity ligand recognition.
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