C-type lectin-like domain and fibronectin-like type II domain of phospholipase A(2) receptor 1 modulate binding and migratory responses to collagen

FEBS Lett. 2015 Mar 24;589(7):829-35. doi: 10.1016/j.febslet.2015.02.016. Epub 2015 Feb 25.

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.

Keywords: Binding; Collagen; Fibronectin-like type II domain; Migration; Phospholipase A(2) receptor 1; Secretory phospholipase A(2).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Collagen / metabolism*
  • Fibronectins / metabolism
  • HEK293 Cells
  • Humans
  • Lectins, C-Type / metabolism
  • Mice
  • Mutation
  • Protein Structure, Tertiary
  • Receptors, Phospholipase A2 / chemistry
  • Receptors, Phospholipase A2 / genetics*
  • Receptors, Phospholipase A2 / metabolism*

Substances

  • Fibronectins
  • Lectins, C-Type
  • PLA2R1 protein, human
  • Pla2r1 protein, mouse
  • Receptors, Phospholipase A2
  • Collagen