Phosphatidylserine as an anchor for plasminogen and its plasminogen receptor, histone H2B, to the macrophage surface.

ABSTRACT:

Background

Plasminogen (Plg) binding to cell surface Plg receptors (Plg-Rs) on the surface of macrophages facilitates Plg activation and migration of these cells. Histone H2B (H2B) acts as a Plg-R and its cell surface expression is up-regulated when monocytes are differentiated to macrophages via a pathway dependent on L-type Ca(2+) channels and intracellular Ca(2+).

Objectives

We sought to investigate the mechanism by which H2B, a protein without a transmembrane domain, is retained on the macrophage surface.

Methods

THP-1 monocytoid cells were induced to differentiate with interferon gamma + Vitamin D3 or to undergo apoptosis by treatment with camptothecin. Flow cytometry and cell surface biotinylation followed by Western blotting were used to measure the interrelati

SUBMITTER: Das R 

PROVIDER: S-EPMC3881192 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature