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      Disturbances of apoptotic cell clearance in systemic lupus erythematosus

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      Author(s): 1 , 1 ,
      Publication date (Electronic):
      Journal: Arthritis Research & Therapy
      Publisher: BioMed Central

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          Abstract

          Systemic lupus erythematosus is a multifactorial autoimmune disease with an as yet unknown etiopathogenesis. It is widely thought that self-immunization in systemic lupus is driven by defective clearance of dead and dying cells. In lupus patients, large numbers of apoptotic cells accumulate in various tissues including germinal centers. In the present review, we discuss the danger signals released by apoptotic cells, their triggering of inflammatory responses, and the breakdown of B-cell tolerance. We also review the pathogenic role of apoptotic cell clearance in systemic lupus erythematosus.

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          Cell-surface calreticulin initiates clearance of viable or apoptotic cells through trans-activation of LRP on the phagocyte.

          Shyra Gardai, Kathleen McPhillips, S. Frasch … (2005)
          Apoptotic-cell removal is critical for development, tissue homeostasis, and resolution of inflammation. Although many candidate systems exist, only phosphatidylserine has been identified as a general recognition ligand on apoptotic cells. We demonstrate here that calreticulin acts as a second general recognition ligand by binding and activating LDL-receptor-related protein (LRP) on the engulfing cell. Since surface calreticulin is also found on viable cells, a mechanism preventing inadvertent uptake was sought. Disruption of interactions between CD47 (integrin-associated protein) on the target cell and SIRPalpha (SHPS-1), a heavily glycosylated transmembrane protein on the engulfing cell, permitted uptake of viable cells in a calreticulin/LRP-dependent manner. On apoptotic cells, CD47 was altered and/or lost and no longer activated SIRPalpha. These changes on the apoptotic cell create an environment where "don't eat me" signals are rendered inactive and "eat me" signals, including calreticulin and phosphatidylserine, congregate together and signal for removal.
          Article 0 comments Cited 455 times – based on 0 reviews     Review now
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            Homeostatic regulation of the immune system by receptor tyrosine kinases of the Tyro 3 family.

            Q. Lu, G Lemke (2001)
            Receptor tyrosine kinases and their ligands mediate cell-cell communication and interaction in many organ systems, but have not been known to act in this capacity in the mature immune system. We now provide genetic evidence that three closely related receptor tyrosine kinases, Tyro 3, Axl, and Mer, play an essential immunoregulatory role. Mutant mice that lack these receptors develop a severe lymphoproliferative disorder accompanied by broad-spectrum autoimmunity. These phenotypes are cell nonautonomous with respect to lymphocytes and result from the hyperactivation of antigen-presenting cells in which the three receptors are normally expressed.
            Article 0 comments Cited 202 times – based on 0 reviews     Review now
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              TIM-1 and TIM-4 glycoproteins bind phosphatidylserine and mediate uptake of apoptotic cells.

              Norimoto Kobayashi, Piia Karisola, Victor Pena-Cruz … (2007)
              The T cell immunoglobulin mucin (TIM) proteins regulate T cell activation and tolerance. Here we showed that TIM-4 is expressed on human and mouse macrophages and dendritic cells, and both TIM-4 and TIM-1 specifically bound phosphatidylserine (PS) on the surface of apoptotic cells but not any other phospholipid tested. TIM-4(+) peritoneal macrophages, TIM-1(+) kidney cells, and TIM-4- or TIM-1-transfected cells efficiently phagocytosed apoptotic cells, and phagocytosis could be blocked by TIM-4 or TIM-1 monoclonal antibodies. Mutations in the unique cavity of TIM-4 eliminated PS binding and phagocytosis. TIM-4 mAbs that blocked PS binding and phagocytosis mapped to epitopes in this binding cavity. These results show that TIM-4 and TIM-1 are immunologically restricted members of the group of receptors whose recognition of PS is critical for the efficient clearance of apoptotic cells and prevention of autoimmunity.
              Article 0 comments Cited 192 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): Arthritis Res Ther
                Journal ID (iso-abbrev): Arthritis Res. Ther
                Title: Arthritis Research & Therapy
                Publisher: BioMed Central
                ISSN (Print): 1478-6354
                ISSN (Electronic): 1478-6362
                Publication date (Print): 2011
                Publication date (Electronic): 28 February 2011
                Publication date PMC-release: 28 August 2011
                Volume: 13
                Issue: 1
                Page: 202
                Affiliations
                [1 ]Section of Rheumatology, Department of Medicine, Temple University, 3322 North Broad Street, Room 205, Philadelphia, PA 19140, USA
                Article
                Publisher ID: ar3206
                DOI: 10.1186/ar3206
                PMC ID: 3157636
                PubMed ID: 21371352
                SO-VID: 3d54dce8-a721-407e-b6cf-6b8dc82c9044
                Copyright © Copyright ©2011 BioMed Central Ltd
                History
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                Subject: Review

                ScienceOpen disciplines: Orthopedics
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                ScienceOpen disciplines: Orthopedics

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