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LFA-1 integrin antibodies inhibit leukocyte α4β1-mediated adhesion by intracellular signalingстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 12 августа 2020 г.
- Авторы: Grönholm M., Jahan F., Bryushkova EA, Madhavan S., Aglialoro F., Soto Hinojosa L., Uotila LM, Gahmberg CG
- Журнал: Blood
- Том: 128
- Номер: 9
- Год издания: 2016
- Издательство: American Society of Hematology
- Местоположение издательства: United States
- Первая страница: 1270
- Последняя страница: 1281
- DOI: 10.1182/blood-2016-03-705160
- Аннотация: Binding of intercellular adhesion molecule-1 to the β2-integrin leukocyte function associated antigen-1 (LFA-1) is known to induce cross-talk to the α4β1 integrin. Using different LFA-1 monoclonal antibodies, we have been able to study the requirement and mechanism of action for the cross-talk in considerable detail. LFA-1-activating antibodies and those inhibitory antibodies that signal to α4β1 induce phosphorylation of Thr-758 on the β2-chain, which is followed by binding of 14-3-3 proteins and signaling through the G protein exchange factor Tiam1. This results in dephosphorylation of Thr-788/789 on the β1-chain of α4β1 and loss of binding to its ligand vascular cell adhesion molecule-1. The results show that with LFA-1 antibodies, we can activate LFA-1 and inhibit α4β1, inhibit both LFA-1 and α4β1, inhibit LFA-1 but not α4β1, or not affect LFA-1 or α4β1 These findings are important for the understanding of integrin regulation and for the interpretation of the effect of integrin antibodies and their use in clinical applications.
- Добавил в систему: Брюшкова Екатерина Александровна