| bwgxutwlumk | Date: Sunday, 2013-12-15, 0:30 AM | Message # 1 |
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| Cell adhesion interactions are important in the understanding of various cellular processes where specific recoggition of prote锟斤拷n surfaces is essential. Erythrocytes parasitized (PE)by P. Falciparum segregate/sequester themselves, from your circulation by adhering to microvascular endothelial cells (MEC). This segregation contributes directly on the virulence and severe pathology of malaria derived from P. falciparum; it is known that cell surface protein CD36 is surely an important host receptor for PE adherence, and this adhesion is mediated from the malarial variant antigen, P. falciparum erythrocyte membrane protein 1 <a href=http://www.uggoutletstores2014.com>Uggs outlet online</a> (PfEMP1) plus by its cysteine-rich interdomain region 1 (CIDR-1). A group of peptides in the immunodominant domain of CD36 (residues 139-184) ranging in sizes from 17 to 29 aminos, interfered while using the CD36-PfEMP1 protein-protein interaction. Each one of these peptides diminished binding at low micromolar <a href=http://www.uggoutletstore2014.net>Uggs outlet online</a> range. Two such peptides, CD36 145-171 and CD36 156-184, selectively blocked PE adhesion to CD36 without the <a href=http://www.uggsoutletstores2014.net>UGG Outlet</a> need of effect on its binding on the host receptor intercellular adhesion molecule-1 (ICAM-1).It <a href=http://www.uggoutletstores2014.net>Ugg outlet</a> is actually also described that an adhesion blocking peptide on the ICAM-1 sequence interferes with PfEMP1锟紺 ICAM-1 interaction without any effect on its adhesion to CD36. These experiments validate earlier evidence that PfEMP1 is additionally a receptor for ICAM.In summary it truly is shown that region 139-184 <a href=http://www.uggonsale2014.net>UGGS Clearance Sale</a> ,comprise the binding/adhesion for P. falciparum. These peptides might be be very useful for understanding the PE/PfEMP1 interaction with CD36 and for possible development of anti-adhesion molecular therapies.
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