Characterization of the interaction between beta 2-glycoprotein I and mitochondria, platelets, liposomes and bile acids.
Several different binding mechanisms appear to be involved in the binding of beta 2-glycoprotein I to biological membranes. One of these mechanisms is a hydrophilic interaction between negatively-charged phospholipids in the membrane and histidine residues in beta 2-glycoprotein I. This mechanism seems to be involved in binding of the protein to mitochondria but not to platelets. Another mechanism may involve a site on beta 2-glycoprotein I, which binds to the steroid ring system particularly to such steroids not having a 7-hydroxy group. This type of binding may be involved in the interaction between beta 2-glycoprotein I and platelets as well as mitochondria.
D001647:Bile Acids and Salts / Q000378:metabolism*; D001792:Blood Platelets / Q000378:metabolism*; D005260:Female; D006023:Glycoproteins / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007123:Immunoelectrophoresis, Two-Dimensional; D066298:In Vitro Techniques; D008081:Liposomes / Q000378:metabolism*; D008297:Male; D008566:Membranes / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism*; D011485:Protein Binding; D012441:Saccharomyces cerevisiae; D053482:beta 2-Glycoprotein I
D001647:Bile Acids and Salts; D006023:Glycoproteins; D008081:Liposomes; D053482:beta 2-Glycoprotein I