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• W2022504433 abstract "Members of the β1 integrin family mediate cellular adherence to a wide range of extracellular and cell surface associated ligands. Conformational changes have been shown to be associated with integrin activation and ligand binding. Some studies suggest that there may be a restricted region of the β1 integrin that serves as the target for regulatory antibodies which can inhibit or stimulate integrin function. Here we identify an inhibitory epitope that is located at a distinct sight from that suggested for other inhibitory antibodies. Three different adhesion blocking antibodies, JB1A, C30B, and DUB bind to a peptide corresponding to residues 82–87 of the mature β1 chain. Mn++ inhibited the binding of JB1A to purified β? integrin. In contrast the binding of several other antibodies to β1 were not influenced by these conditions. JB1A binding to purified peptide was also inhibited by Mn++ suggesting that it related to interference with the antibody function rather than a cation dependent change in the epitope. Our data 1) directly demonstrates the peptide sequence recognised by three adhesion blocking antibodies to the human β1 integrin chain 2) identifies a novel epitope located at residues 82–87, distinct from that of previously described regulatory epitopes 3) characterises a Mn++ sensitive antibody integrin interaction. Collectively, these results indicate the existence of multiple regulatory sites on the β1 integrin molecule." @default.
• W2022504433 created "2016-06-24" @default.
• W2022504433 creator A5050268815 @default.
• W2022504433 creator A5090942754 @default.
• W2022504433 date "1998-01-01" @default.
• W2022504433 modified "2023-09-26" @default.
• W2022504433 title "Localisation of a Novel Adhesion Blocking Epitope on the Human β₁Integrin Chain" @default.
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• W2022504433 doi "https://doi.org/10.3109/15419069809040296" @default.
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