Dissection of α₄β₇ integrin regulation by Rap1 using novel conformation-specific monoclonal anti-β₇ antibodies.

ABSTRACT: Integrin activation is associated with conformational regulation. In this study, we developed a system to evaluate conformational changes in α₄β₇ integrin. We first inserted the PA tag into the plexin-semaphorin-integrin (PSI) domain of β₇ chain, which reacted with an anti-PA tag antibody (NZ-1) in an Mn²⁺-dependent manner. The small GTPase Rap1 deficiency, as well as chemokine stimulation and the introduction of the active form of Rap1, Rap1V12, enhanced the binding of NZ-1 to the PA-tagged mutant integrin, and increased the binding affinity to mucosal addressing cell adhesion molecule-1 (MAdCAM-1). Furthermore, we generated two kinds of hybridomas producing monoclonal antibodies (mAbs) that recognized Mn²⁺-dependent epitopes of β

SUBMITTER: Sato T 

PROVIDER: S-EPMC7413538 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature