| Literature DB >> 25724334 |
Soichiro Takahashi1, Kazuhiro Watanabe1, Yosuke Watanabe1, Daisuke Fujioka1, Takamitsu Nakamura1, Kazuto Nakamura1, Jun-ei Obata1, Kiyotaka Kugiyama2.
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.Entities:
Keywords: Binding; Collagen; Fibronectin-like type II domain; Migration; Phospholipase A(2) receptor 1; Secretory phospholipase A(2)
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Year: 2015 PMID: 25724334 DOI: 10.1016/j.febslet.2015.02.016
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124