Calreticulin, a Potential Cell Surface Receptor Involved in Cell Penetration of Anti-DNA Antibodies
| Autor: | Farida Nato, Jean Claude Mazié, Pierre Lafaye, J.C. Piette, Zahir Amoura, Nabila Seddiki |
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| Rok vydání: | 2001 |
| Předmět: |
Cytoplasm
Cell Membrane Permeability genetic structures Molecular Sequence Data Immunology Receptors Cell Surface CHO Cells Autoantigens law.invention Pathogenesis Jurkat Cells Mice Antibody Specificity Cell surface receptor Confocal microscopy law Cricetinae Tumor Cells Cultured Animals Humans Immunology and Allergy Amino Acid Sequence cardiovascular diseases Receptor Cell Line Transformed Hybridomas Mice Inbred NZB biology Chinese hamster ovary cell Calcium-Binding Proteins Antibodies Monoclonal Membrane Proteins DNA Molecular biology Cell biology Ribonucleoproteins Antibodies Antinuclear Biotinylation biology.protein Binding Sites Antibody Antibody Calreticulin K562 Cells |
| Zdroj: | The Journal of Immunology. 166:6423-6429 |
| ISSN: | 1550-6606 0022-1767 |
| DOI: | 10.4049/jimmunol.166.10.6423 |
| Popis: | A 50-kDa protein was purified as a potential receptor, using an affinity matrix containing biotinylated F14.6 or H9.3 anti-DNA mAbs derived from autoimmune (New Zealand Black × New Zealand White)F1 mouse and membrane extracts from cells. This protein was identified as calreticulin (CRT) by microsequencing. Confocal microscopy and FACS analysis showed that CRT was present on the surface of various cells. CRT protein was recognized by a panel of anti-DNA mAbs in ELISA. The binding of F14.6 to lymphocytes and Chinese hamster ovary cells was inhibited by soluble CRT or SPA-600. Thus, the anti-DNA mAbs used in this study bound to CRT, suggesting that CRT may mediate their penetration into the cells and play an important role in lupus pathogenesis. |
| Databáze: | OpenAIRE |
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