Secreted phospholipase A2 type IIA (sPLA2-IIA) activates integrins in an allosteric manner

Yoshikazu Takada, Masaaki Fujita

Research output: Chapter in Book/Report/Conference proceedingChapter

14 Citations (Scopus)

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’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.

Original languageEnglish
Title of host publicationAdvances in Experimental Medicine and Biology
PublisherSpringer New York LLC
Pages103-115
Number of pages13
DOIs
Publication statusPublished - 2017

Publication series

NameAdvances in Experimental Medicine and Biology
Volume925
ISSN (Print)0065-2598
ISSN (Electronic)2214-8019

Keywords

  • Allosteric site
  • Docking simulation
  • Integrin activation
  • Secreted phospholipase A2 type IIA (sPLA2-IIA)

ASJC Scopus subject areas

  • General Biochemistry,Genetics and Molecular Biology

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