This protein is synthesized by the liver and secreted in plasma, associates with heparin and dextran sulfate and may prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells.
Hypoxia increases irreversible binding to phospholipids, augments the release of inorganic fluoride and is followed by centrilobular hepatic necrosis.
Note that the majority of proteins with an amphipathic helix capable of binding to phospholipids often have lysine residues predominantly interspersed with hydrophobic residues, for example, the epsin ENTH domain (Protein Data Bank (PDB) code 1H0A), and the AP180/CALM ANTH domain (PDB code 1HFA) [55] [57].
The inhibitory effect of ANXA1, initially suggested to respond to an enzyme inhibition-like process, was attributed to direct binding to phospholipids, which would prevent access of cPLA2α to its substrate [26].
Proteomic phage display has been used for the identification of allergens [ 18], antibody epitopes, tumor polypeptides producing immune response [ 19], and PPIs as well as for the identification of proteins binding to phospholipids and small chemical compounds [ 20, 21].
Notably, LV pseudotyped with the VSV-G envelope, which only requires binding to phospholipid constituents of most mammalian cells [ 43], achieved much more efficient infection of T cells than is possible with identical vectors pseudotyped with amphotropic retrovirus envelope [ 44].
Current work suggests that after binding to phospholipid components of the target cell membrane, perforin undergoes polymerisation, triggering a membrane-repair response within the target cell that results in the co-endocytosis of membrane-bound perforin and granzymes (Thiery et al., 2010, 2011).
It shares with the annexin family of proteins the property of binding to phospholipid membranes in a Ca2+-dependent manner.
Aminoglycosides have well-known nephrotoxic effects; they are partially reabsorbed into proximal tubular cells and their cationic charge facilitates their binding to membrane phospholipids of tubular epithelial cells.
BID-α6 and BCLX-α6 altered the surface properties of the monolayer by binding to the interface of phospholipids.
