TAILIEUCHUNG - Báo cáo khoa học: Direct interaction between CD91 and C1q

C1q-mediated removal of immune complexes and apoptotic cells plays an important role in tissue homeostasis and the prevention of autoimmune conditions. It has been suggested that C1q mediates phagocytosis of apop-totic cells through a receptor complex assembled from CD91 (a-2- macro-globulin receptor, or low-density lipoprotein receptor-related protein) and calreticulin, with CD91 being the transmembrane part and calreticulin act-ing as the C1q-binding molecule. | ễFEBS Journal Direct interaction between CD91 and C1q Karon Di 11IC1 F rĩ If I lancon2 Pacnalo Tannot3 Philimmro Fronhrrt3 Gororfl I ArlaiiH3 Ixaici I ưuuo CII vv. I lai loci I r aocaie I acucL riiilippe riaMiCL cieiai c u. AAiiauVI Nicole M. Thielens3 and Gunnar Houen1 1 Department of ClinicalBiochemistry and Immunology Statens Serum Institut Copenhagen Denmark 2 Department of Pharmacology and Pharmacotherapy Faculty of PharmaceuticalSciences University of Copenhagen Denmark 3 Laboratoire d Enzymologie Moleculaire Institut de Biologie Structurale Jean-Pierre Ebel Grenoble France Keywords C1q calreticulin CD91 collectin scavenger receptor Correspondence G. Houen Department of Clinical Biochemistry and Immunology Statens Serum Institut Artillerivej 5 DK-2300 Copenhagen Denmark Fax 45 32683149 Tel 45 32683276 E-mail gh@ Received 18 November 2009 revised 27 May 2010 accepted 2 July 2010 doi C1q-mediated removal of immune complexes and apoptotic cells plays an important role in tissue homeostasis and the prevention of autoimmune conditions. It has been suggested that C1q mediates phagocytosis of apop-totic cells through a receptor complex assembled from CD91 a-2- macroglobulin receptor or low-density lipoprotein receptor-related protein and calreticulin with CD91 being the transmembrane part and calreticulin acting as the C1q-binding molecule. In the present study we observe that C1q binds cells from a CD91 expressing monocytic cell line as well as monocytes from human blood. C1q binding to monocytes was shown to be correlated with CD91 expression and could be inhibited by the CD91 chaperone receptor-associated protein. We also report data showing a direct interaction between CD91 and C1q. The interaction was investigated using various protein interaction assays. A direct interaction between purified C1q and CD91 was observed both by ELISA and a surface plasmon resonance assay with either C1q or CD91 immobilized. The interaction .

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