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      Tethering and tickling : a new role for the phosphatidylserine receptor

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      The Journal of Cell Biology
      The Rockefeller University Press

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          Abstract

          Several receptors are implicated in apoptotic cell (AC) uptake by phagocytic cells; however, their relative dominance in mammalian systems remains to be established. New studies shed light on the role of the phosphatidyl serine (PS) receptor (PSR). Ligation of PSR by PS on AC surfaces is considered essential for signaling uptake of ACs that are tethered to phagocytes via other receptors.

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          Dendritic cells acquire antigen from apoptotic cells and induce class I-restricted CTLs.

          CD8+ cytotoxic T lymphocytes (CTLs) mediate resistance to infectious agents and tumours. Classically, CTLs recognize antigens that are localized in the cytoplasm of target cells, processed and presented as peptide complexes with class I molecules of the major histocompatibility complex (MHC). However, there is evidence for an exogenous pathway whereby antigens that are not expected to gain access to the cytoplasm are presented on MHC class I molecules. The most dramatic example is the in vivo phenomenon of cross-priming: antigens from donor cells are acquired by bone-marrow-derived host antigen-presenting cells (APCs) and presented on MHC class I molecules. Two unanswered questions concern the identity of this bone-marrow-derived cell and how such antigens are acquired. Here we show that human dendritic cells, but not macrophages, efficiently present antigen derived from apoptotic cells, stimulating class I-restricted CD8+ CTLs. Our findings suggest a mechanism by which potent APCs acquire antigens from tumours, transplants, infected cells, or even self-tissue, for stimulation or tolerization of CTLs.
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            Bacterially speaking.

            Bacteria use a variety of means to communicate with one another and with their eukaryotic hosts. In some cases, social interactions allow bacteria to synchronize the behavior of all of the members of the group and thereby act like multicellular organisms. By contrast, some bacterial social engagements promote individuality among members within the group and thereby foster diversity. Here we explore the molecular mechanisms underpinning some recently discovered bacterial communication systems. These include long- and short-range chemical signaling channels; one-way, two-way, and multi-way communication; contact-mediated and contact-inhibited signaling; and the use and spread of misinformation or, more dramatically, even deadly information.
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              CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin.

              Complexes of the heat shock protein gp96 and antigenic peptides are taken up by antigen-presenting cells and presented by MHC class I molecules. In order to explain the unusual efficiency of this process, the uptake of gp96 had been postulated to occur through a receptor, identified recently as CD91. We show here that complexes of peptides with heat shock proteins hsp90, calreticulin, and hsp70 are also taken up by macrophages and dendritic cells and re-presented by MHC class I molecules. All heat shock proteins utilize the CD91 receptor, even though some of the proteins have no homology with each other. Postuptake processing of gp96-chaperoned peptides requires proteasomes and the transporters associated with antigen processing, utilizing the classical endogenous antigen presentation pathway.
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                Author and article information

                Journal
                J Cell Biol
                The Journal of Cell Biology
                The Rockefeller University Press
                0021-9525
                1540-8140
                12 November 2001
                : 155
                : 4
                : 501-504
                Affiliations
                The Laboratory of Molecular Neuro-Oncology, The Rockefeller University, New York, NY, 10021
                Author notes

                Address correspondence to Nina Bhardwaj, The Laboratory of Molecular Neuro-Oncology, The Rockefeller University, Room 41, Box #176, 1230 York Ave., New York, NY 10021. Tel.: (212) 327-8332. Fax: (212) 327-7232. E-mail bhardwn@ 123456mail.rockefeller.edu

                Article
                0110066
                10.1083/jcb.200110066
                2198851
                11706046
                ac860ddb-8494-4e1e-bd60-2380ce24eab9
                Copyright © 2001, The Rockefeller University Press
                History
                : 15 October 2001
                : 15 October 2001
                : 18 October 2001
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                Cell biology
                Cell biology

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