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0342896657
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note
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-/- mice (33) on a mixed 129/C56BL/6 background were a gift from H. Molina (Washington University, St. Louis, MO). Animals were kept in accordance with NIH and local guidelines and maintained in a specific pathogen-free barrier facility.
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17
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0343767681
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note
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-/- recipients (detection by staining for CD47 and flow cytometry) gave similar results.
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20
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0342896656
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note
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Dichloromethylene diphosphonate (clodronate; a gift from Roche Diagnostics/Boehringer Mannheim GmbH) liposomes was prepared as described (T8). Clodronate (200 μl) or NaCl liposomes were given to recipient mice by tail-vein injection at 48 and 24 hours before RBC transfer. Immunohistochemical analyses revealed a complete macrophage depletion in recipient spleens 48 hours after a single injection of clodronate liposomes.
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21
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0343767679
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note
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+ cells were visualized with Tyramide Signal Amplification (NEN Life Science Products, Boston, MA).
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23
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24
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0343331790
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note
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-/- RBCs were added to each well for another 60 min. Nonadherent cells were washed off with warm phosphate-buffered saline (PBS)-0.1% HSA, and noningested RBCs were lysed with ACK lysis buffer. Phagocytosis index (the number of RBCs phagocytosed per 100 adherent macrophages) was determined by fluorescence microscopy (Zeiss Axioscope).
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26
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0039726964
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27
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0343767676
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note
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-/- RBCs were added, then allowed to settle for 3 min at 4 °C, after which sodium pervanadate (Sigma) was added to 2 mM and cells were transferred to a water bath at 37 °C At the times indicated, the medium was quickly aspirated, and cells were lysed in cold lysis buffer [50 mM tris-HCl (pH 7.5), 150 mM NaCl, 1% NP-40 (Pierce, Rockford, IL), 1 mM diisopropyl, aprotinin (10 μg/ml), 2 mM sodium pervanadate]. Lysates were cleared by centrifugation and incubated for 2 hours at 4 °C with anti-SIRP monoclonal antibody (mAb) P84 bound to 20 μl of goat anti-rat Sepharose (ICN, Costa Mesa, CA) for 2 hours at 4 °C. After two washes in lysis buffer, immunoprecipitated proteins were eluted with reducing SDS-polyacrylamide gel electrophoresis (PACE) sample buffer, separated on 8% SDS-PACE, and transferred to a polyvinylidene difluoride membrane (Millipore, Bedford, MA). Tyrosine phosphorylation was detected by Western blot with anti-phosptiotyrosine mAb 4G10, followed by HRP-conjugated secondary antibody and enhanced chemoluminescence as described (36).
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29
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0342462584
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unpublished data
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F. P. Lindberg et al., unpublished data.
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Lindberg, F.P.1
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31
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Mombaerts, P.1
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0343767674
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note
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We thank T. Steinberg, W. Yokoyama, J. Atkinson, and E. Brown for critically reading the manuscript; D. Chaplin, H. Molina, and P. Leenen for reagents; and E. Ford for technical assistance. Supported by grants from the NIH (GM57S73-01), the American Diabetes Association, the Washington University-Monsanto Research Agreement, a pilot grant from the Howard Hughes Medical Institute, and the Medical Research Service of the Depatment of Veterans Affairs. P.-A.O is supported by a postdoctoral fellowship from the Umeå University-Washington University exchange program and by the Swedish Medical Research Council.
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