@inbook{61b2014fb4b24f5da952c9907f5ab931,
title = "Secreted phospholipase A2 type IIA (sPLA2-IIA) activates integrins in an allosteric manner",
abstract = "Secreted phospholipase A2 type IIA (sPLA2-IIA) is a well-established pro-inflammatory protein and has been a major target for drug discovery. However, the mechanism of its signaling action has not been fully understood. We previously found that sPLA2-IIA binds to integrins αvβ3 and α4β1 in human and that this interaction plays a role in sPLA2-IIA{\textquoteright}s signaling action. Our recent studies found that sPLA2-IIA activates integrins in an allosteric manner through direct binding to a newly identified binding site of integrins (site 2), which is distinct from the classical RGD-binding site (site 1). The sPLA2-IIA-induced integrin activation may be related to the signaling action of sPLA2-IIA. Since sPLA2-IIA is present in normal human tears in addition to rheumatoid synovial fluid at high concentrations the sPLA2-IIA-mediated integrin activation on leukocytes may be involved in immune responses in normal and pathological conditions.",
keywords = "Allosteric site, Docking simulation, Integrin activation, Secreted phospholipase A2 type IIA (sPLA2-IIA)",
author = "Yoshikazu Takada and Masaaki Fujita",
note = "Publisher Copyright: {\textcopyright} 2016, Springer International Publishing Switzerland.",
year = "2017",
doi = "10.1007/5584_2016_95",
language = "English",
series = "Advances in Experimental Medicine and Biology",
publisher = "Springer New York LLC",
pages = "103--115",
booktitle = "Advances in Experimental Medicine and Biology",
}