Presence and primary sequence of a high-affinity IgG receptor on canine mastocytoma (CM-MC) cells
Autor: | Reiko Teshima, Ryosuke Nakamura, Jun-ichi Sawada, Nobuo Sasaki, Kayoko Takagi, Seiichi Kitani, Yoshitaka Sato |
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Rok vydání: | 2003 |
Předmět: |
DNA
Complementary Molecular Sequence Data Immunology Canine Mastocytoma Biology Mice Dogs Species Specificity Complementary DNA Tumor Cells Cultured Genetics Animals Humans Amino Acid Sequence Mast Cells RNA Messenger RNA Neoplasm Receptor Peptide sequence chemistry.chemical_classification Messenger RNA Base Sequence Sequence Homology Amino Acid Receptors IgG DNA Neoplasm Mastocytoma Molecular biology Reverse transcriptase Amino acid chemistry Signal transduction Signal Transduction |
Zdroj: | Immunogenetics. 55:271-274 |
ISSN: | 1432-1211 0093-7711 |
DOI: | 10.1007/s00251-003-0578-5 |
Popis: | Mast cells play a central role in IgE-dependent allergic responses. Although they have been reported to express only low-affinity IgG receptors and no high-affinity receptors (FcgammaRI), our recent study showed that canine mastocytoma CM-MC cells are activated by monomeric canine IgG, suggesting the presence of FcgammaRI on CM-MC cells. In the present study, we measured the affinity of canine IgG with CM-MC cells, determined the presence of the FcgammaRI protein and mRNA, and identified the cDNA sequence of it. The results showed that (7.5+/-3.1)x10(4) receptor molecules are expressed on a CM-MC cell with a Ka of (9.1+/-1.6)x10(7)M(-1) for binding to monomeric canine IgG. Canine IgG-conjugated beads precipitated an approximately 72-kDa surface protein, whose size is consistent with that of the FcgammaRI alpha subunit of humans and mouse. The expression of FcgammaRI mRNA was detected by reverse transcriptase polymerase chain reaction (RT-PCR), and the cDNA encoding the FcgammaRI alpha subunit was found to be 84% and 78% similar to that of humans and the mouse, respectively. The predicted amino acid sequence was 72% and 63% identical, respectively. Canine mastocytoma CM-MC cells are therefore very useful for studying FcgammaRI-mediated signal transduction in mast cells. |
Databáze: | OpenAIRE |
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