@article{citeulike:565725,
	title = {Platelet activation by the apoB/E receptor-binding domain of LDL.},
	address = {Department of Haematology, University Medical Center Utrecht, The Netherlands. i.relou@lab.azu.nl},
	author = {A. M. Relou and G. Gorter and H. J. van Rijn and J. W. Akkerman},
	journal = {Thromb Haemost},
	month = {May},
	number = {5},
	pages = {880--887},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=12038793},
	volume = {87},
	year = {2002},
	biburl = {http://www.bibsonomy.org/bibtex/2605a2253a2ed647dd953a483a8978b99/biblio24},
	abstract = {Low density lipoprotein (LDL) increases the sensitivity of human platelets for agonists by activating p38MAPK. Antibody 4G3 disturbs apoB100 binding to the classical apoB/E receptor and inhibits LDL-induced p38MAPK activation, whereas an antibody against a distal domain on apoB 100 has no effect. Peptide RLTRKRGLKLA mimics the binding domain of apoB 100 called the B-site and activates platelet p38MAPK. Activation by B-site peptide is dose-dependent, transient and followed by desensitization, in accordance with receptor-mediated signalling. A scrambled peptide and a partially homologous peptide RKLRKRLLRDA mimicking the apoB/E receptor binding site of apoE in high density lipoprotein (HDL) also activate p38MAPK albeit 40% weaker, but an uncharged peptide lacks p38MAPK activating capacity. LDL and B-site peptide bind to the same binding sites and initiate similar signalling to p38MAPK and cytosolic phospholipase A2. Thus, LDL and to a lesser extent HDL activate platelets via specific domains in the protein moiety that recognize receptors of the LDL receptor family.},
	issn = {0340-6245}, citeulike-article-id = {565725}, priority = {2},
	keywords = {antibody apob }
}