Proteolysis of band 3 is enhanced by anti-Rho(D) binding to the red cell membrane
Surface radioiodinated human red cells were incubated with IgG fractions and the radioelectrophoretic profile of the ghost membranes determined. The patterns of RhO(D)-negative membranes exposed to anti-RhO(D) IgG and RhO(D)-positive membranes exposed to non-immune IgG fractions remained intact. Mem...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1984-10, Vol.124 (2), p.437-442 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Victoria, E J Kleeman, J E Masouredis, S P |
| description | Surface radioiodinated human red cells were incubated with IgG fractions and the radioelectrophoretic profile of the ghost membranes determined. The patterns of RhO(D)-negative membranes exposed to anti-RhO(D) IgG and RhO(D)-positive membranes exposed to non-immune IgG fractions remained intact. Membranes of RhO(D)-positive membranes following incubation with anti-RhO(D) IgG showed a sharp reduction in the quantity of intact band 3, the main glycoprotein of the red cell membrane. This process was significantly abrogated in the presence of protease inhibitors. The results suggest a possible role for IgG binding in promoting the generation of band 3-derived fragments described by others as normal constituents of isolated ghosts. |
| doi_str_mv | 10.1016/0006-291X(84)91572-9 |
| format | Article |
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The patterns of RhO(D)-negative membranes exposed to anti-RhO(D) IgG and RhO(D)-positive membranes exposed to non-immune IgG fractions remained intact. Membranes of RhO(D)-positive membranes following incubation with anti-RhO(D) IgG showed a sharp reduction in the quantity of intact band 3, the main glycoprotein of the red cell membrane. This process was significantly abrogated in the presence of protease inhibitors. 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The patterns of RhO(D)-negative membranes exposed to anti-RhO(D) IgG and RhO(D)-positive membranes exposed to non-immune IgG fractions remained intact. Membranes of RhO(D)-positive membranes following incubation with anti-RhO(D) IgG showed a sharp reduction in the quantity of intact band 3, the main glycoprotein of the red cell membrane. This process was significantly abrogated in the presence of protease inhibitors. The results suggest a possible role for IgG binding in promoting the generation of band 3-derived fragments described by others as normal constituents of isolated ghosts.</description><subject>ABO Blood-Group System - immunology</subject><subject>Anion Exchange Protein 1, Erythrocyte - metabolism</subject><subject>Antigen-Antibody Complex</subject><subject>Erythrocyte Membrane - immunology</subject><subject>Humans</subject><subject>Immunoglobulin G</subject><subject>Protease Inhibitors - blood</subject><subject>Rh-Hr Blood-Group System - immunology</subject><issn>0006-291X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kElPwzAUhH0AlVL4ByD5hNpDwFts54jKKlViEUjcLMcLDUriYqeH_HsSWvX0NE8zo9EHwAVG1xhhfoMQ4hkp8NdcskWBc0Gy4ghMD-8TcJrSD0IYM15MwIQzKhgiU_D2GkPnQt2nKsHgYalbCykchGvXujXOwrKHuu2q7H0d5ncLWFatrdpv2AXYrR2Mg8O4uoaNa8qoW3cGjr2ukzvf3xn4fLj_WD5lq5fH5-XtKjMUkS7T1nPqKKNWSmHzEmlWeGQo9iV30hCJnOU5wTQXgnkvmSVMUi8cMbkwgtMZuNr1bmL43brUqaZK45JhQ9gmJTGlEmEyGNnOaGJIKTqvNrFqdOwVRmqkp0ZMasSkJFP_9FQxxC73_duycfYQ2qOjf45ca0M</recordid><startdate>19841030</startdate><enddate>19841030</enddate><creator>Victoria, E J</creator><creator>Kleeman, J E</creator><creator>Masouredis, S P</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19841030</creationdate><title>Proteolysis of band 3 is enhanced by anti-Rho(D) binding to the red cell membrane</title><author>Victoria, E J ; Kleeman, J E ; Masouredis, S P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c302t-adf63e343d887d5b0a49f0c31fb6e8c280ed652135774ff84d2483f7e2c57c763</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>ABO Blood-Group System - immunology</topic><topic>Anion Exchange Protein 1, Erythrocyte - metabolism</topic><topic>Antigen-Antibody Complex</topic><topic>Erythrocyte Membrane - immunology</topic><topic>Humans</topic><topic>Immunoglobulin G</topic><topic>Protease Inhibitors - blood</topic><topic>Rh-Hr Blood-Group System - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Victoria, E J</creatorcontrib><creatorcontrib>Kleeman, J E</creatorcontrib><creatorcontrib>Masouredis, S P</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Victoria, E J</au><au>Kleeman, J E</au><au>Masouredis, S P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteolysis of band 3 is enhanced by anti-Rho(D) binding to the red cell membrane</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1984-10-30</date><risdate>1984</risdate><volume>124</volume><issue>2</issue><spage>437</spage><epage>442</epage><pages>437-442</pages><issn>0006-291X</issn><abstract>Surface radioiodinated human red cells were incubated with IgG fractions and the radioelectrophoretic profile of the ghost membranes determined. 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| fulltext | fulltext |
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| ispartof | Biochemical and biophysical research communications, 1984-10, Vol.124 (2), p.437-442 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | ABO Blood-Group System - immunology Anion Exchange Protein 1, Erythrocyte - metabolism Antigen-Antibody Complex Erythrocyte Membrane - immunology Humans Immunoglobulin G Protease Inhibitors - blood Rh-Hr Blood-Group System - immunology |
| title | Proteolysis of band 3 is enhanced by anti-Rho(D) binding to the red cell membrane |
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