Binding preferences for GPIHBP1, a glycosylphosphatidylinositol-anchored protein of capillary endothelial cells.

ABSTRACT:

Objective

To define the ability of GPIHBP1 to bind other lipase family members and other apolipoproteins (apos) and lipoproteins.

Methods and results

GPIHBP1, a GPI-anchored lymphocyte antigen (Ly)6 protein of capillary endothelial cells, binds lipoprotein lipase (LPL) avidly, but its ability to bind related lipase family members has never been evaluated. As judged by cell-based and cell-free binding assays, LPL binds to GPIHBP1, but other members of the lipase family do not. We also examined the binding of apoAV-phospholipid disks to GPIHBP1. ApoAV binds avidly to GPIHBP1-transfected cells; this binding requires GPIHBP1's amino-terminal acidic domain and is independent of its cysteine-rich Ly6 domain (the latter domain is essential for LPL binding). GPIHBP1-transfected cell

SUBMITTER: Gin P 

PROVIDER: S-EPMC3004026 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature