Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870105 | FEBS Letters | 2015 | 7 Pages |
Abstract
Phospholipase A2 receptor 1 (PLA2R) mediates collagen-dependent migration. The mechanisms by which PLA2R interacts with collagen remain unclear. We produced HEK293 cells expressing full-length wild-type PLA2R or a truncated PLA2R that lacks fibronectin-like type II (FNII) domains or several regions of C-type lectin-like domain (CTLD). We show that the CTLD1-2 as well as the FNII domain of PLA2R are responsible for binding to collagen and for collagen-dependent migration. Thus, multiple regions and domains of the extracellular portion of PLA2R participate in the responses to collagen. These data suggest a potentially new mechanism for PLA2R-mediated biological response beyond that of a receptor for secretory PLA2.
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Authors
Soichiro Takahashi, Kazuhiro Watanabe, Yosuke Watanabe, Daisuke Fujioka, Takamitsu Nakamura, Kazuto Nakamura, Jun-ei Obata, Kiyotaka Kugiyama,