Calreticulin is released from activated neutrophils and binds to C1q and mannan-binding protein. 1994

P Eggleton, and T S Lieu, and E G Zappi, and K Sastry, and J Coburn, and K S Zaner, and R D Sontheimer, and J D Capra, and B Ghebrehiwet, and A I Tauber
Department of Pathology, Boston University School of Medicine, Massachusetts 02118.

The Ca2+ storage protein calreticulin is associated with the endoplasmic reticulum and shares a high degree of amino acid homology with the surface receptor C1q-R. In this study, flow cytometric analysis detected calreticulin on the neutrophil surface, which decreased during stimulation probably as a consequence of shedding, as calreticulin was found by ELISA in the cell supernatants of stimulated cells. Antibodies raised against C1q-R and calreticulin demonstrated a high degree of immunological cross-reactivity for purified calreticulin as determined by dot blot analysis. Western blots of neutrophil subcellular fractions located calreticulin in both the cytosol and cell membrane fractions; C1q-R was largely confined to the cell membrane. Calreticulin and C1q-R both bind to C1q and mannan-binding protein. Therefore, calreticulin may be shed on cell activation and may be associated with the cell membrane, where it can potentially interact with C1q and serum lectins. The implications of this are discussed.

UI MeSH Term Description Entries
D009504 Neutrophils Granular leukocytes having a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes. LE Cells,Leukocytes, Polymorphonuclear,Polymorphonuclear Leukocytes,Polymorphonuclear Neutrophils,Neutrophil Band Cells,Band Cell, Neutrophil,Cell, LE,LE Cell,Leukocyte, Polymorphonuclear,Neutrophil,Neutrophil Band Cell,Neutrophil, Polymorphonuclear,Polymorphonuclear Leukocyte,Polymorphonuclear Neutrophil
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D002135 Calcium-Binding Proteins Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS. Calcium Binding Protein,Calcium-Binding Protein,Calcium Binding Proteins,Binding Protein, Calcium,Binding Proteins, Calcium,Protein, Calcium Binding,Protein, Calcium-Binding
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D003429 Cross Reactions Serological reactions in which an antiserum against one antigen reacts with a non-identical but closely related antigen. Cross Reaction,Reaction, Cross,Reactions, Cross
D004797 Enzyme-Linked Immunosorbent Assay An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed. ELISA,Assay, Enzyme-Linked Immunosorbent,Assays, Enzyme-Linked Immunosorbent,Enzyme Linked Immunosorbent Assay,Enzyme-Linked Immunosorbent Assays,Immunosorbent Assay, Enzyme-Linked,Immunosorbent Assays, Enzyme-Linked
D005434 Flow Cytometry Technique using an instrument system for making, processing, and displaying one or more measurements on individual cells obtained from a cell suspension. Cells are usually stained with one or more fluorescent dyes specific to cell components of interest, e.g., DNA, and fluorescence of each cell is measured as it rapidly transverses the excitation beam (laser or mercury arc lamp). Fluorescence provides a quantitative measure of various biochemical and biophysical properties of the cell, as well as a basis for cell sorting. Other measurable optical parameters include light absorption and light scattering, the latter being applicable to the measurement of cell size, shape, density, granularity, and stain uptake. Cytofluorometry, Flow,Cytometry, Flow,Flow Microfluorimetry,Fluorescence-Activated Cell Sorting,Microfluorometry, Flow,Cell Sorting, Fluorescence-Activated,Cell Sortings, Fluorescence-Activated,Cytofluorometries, Flow,Cytometries, Flow,Flow Cytofluorometries,Flow Cytofluorometry,Flow Cytometries,Flow Microfluorometries,Flow Microfluorometry,Fluorescence Activated Cell Sorting,Fluorescence-Activated Cell Sortings,Microfluorimetry, Flow,Microfluorometries, Flow,Sorting, Fluorescence-Activated Cell,Sortings, Fluorescence-Activated Cell
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D012261 Ribonucleoproteins Complexes of RNA-binding proteins with ribonucleic acids (RNA). Ribonucleoprotein

Related Publications

P Eggleton, and T S Lieu, and E G Zappi, and K Sastry, and J Coburn, and K S Zaner, and R D Sontheimer, and J D Capra, and B Ghebrehiwet, and A I Tauber
January 1999, Lupus,
P Eggleton, and T S Lieu, and E G Zappi, and K Sastry, and J Coburn, and K S Zaner, and R D Sontheimer, and J D Capra, and B Ghebrehiwet, and A I Tauber
March 1997, The Biochemical journal,
P Eggleton, and T S Lieu, and E G Zappi, and K Sastry, and J Coburn, and K S Zaner, and R D Sontheimer, and J D Capra, and B Ghebrehiwet, and A I Tauber
January 2020, Frontiers in immunology,
P Eggleton, and T S Lieu, and E G Zappi, and K Sastry, and J Coburn, and K S Zaner, and R D Sontheimer, and J D Capra, and B Ghebrehiwet, and A I Tauber
November 1996, FEBS letters,
P Eggleton, and T S Lieu, and E G Zappi, and K Sastry, and J Coburn, and K S Zaner, and R D Sontheimer, and J D Capra, and B Ghebrehiwet, and A I Tauber
December 1997, Immunopharmacology,
P Eggleton, and T S Lieu, and E G Zappi, and K Sastry, and J Coburn, and K S Zaner, and R D Sontheimer, and J D Capra, and B Ghebrehiwet, and A I Tauber
September 2002, Immunobiology,
P Eggleton, and T S Lieu, and E G Zappi, and K Sastry, and J Coburn, and K S Zaner, and R D Sontheimer, and J D Capra, and B Ghebrehiwet, and A I Tauber
May 2005, Biochemical and biophysical research communications,
P Eggleton, and T S Lieu, and E G Zappi, and K Sastry, and J Coburn, and K S Zaner, and R D Sontheimer, and J D Capra, and B Ghebrehiwet, and A I Tauber
January 2017, Frontiers in immunology,
P Eggleton, and T S Lieu, and E G Zappi, and K Sastry, and J Coburn, and K S Zaner, and R D Sontheimer, and J D Capra, and B Ghebrehiwet, and A I Tauber
April 2020, The Journal of biological chemistry,
P Eggleton, and T S Lieu, and E G Zappi, and K Sastry, and J Coburn, and K S Zaner, and R D Sontheimer, and J D Capra, and B Ghebrehiwet, and A I Tauber
April 2001, Human molecular genetics,
Copied contents to your clipboard!