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Isolation and Characterization of cDNAs Coding for the β Subunit of the High-Affinity Receptor for Immunoglobulin E

Kinet, Jean-Pierre ; Blank, Ulrich ; Ra, Chisei ; White, Kenneth ; Metzger, Henry ; Kochan, Jarema

Proceedings of the National Academy of Sciences - PNAS, 1988-09, Vol.85 (17), p.6483-6487 [Periódico revisado por pares]

Washington, DC: National Academy of Sciences of the United States of America

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Título:
Isolation and Characterization of cDNAs Coding for the β Subunit of the High-Affinity Receptor for Immunoglobulin E
Autor: Kinet, Jean-Pierre ; Blank, Ulrich ; Ra, Chisei ; White, Kenneth ; Metzger, Henry ; Kochan, Jarema
Assuntos: Amino Acid Sequence ; Amino acids ; Animals ; Antibodies ; Antigens, Differentiation - genetics ; Base Sequence ; Basophils - immunology ; Biological and medical sciences ; Cloning, Molecular ; Complementary DNA ; DNA - genetics ; DNA - isolation & purification ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Gels ; Genes ; Immunobiology ; Immunoglobulin E - metabolism ; Leukemia, Experimental - immunology ; Lymphoid cells: ontogeny, maturation, markers, receptors, circulation and recirculation ; Macromolecular Substances ; Messenger RNA ; Molecular Sequence Data ; Molecular weight ; Monoclonal antibodies ; Nucleotides ; Rats ; Receptors ; Receptors, IgE ; RNA
É parte de: Proceedings of the National Academy of Sciences - PNAS, 1988-09, Vol.85 (17), p.6483-6487
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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Descrição: Among receptors that bind the Fc region of immunoglobulins (``Fc receptors''), only the one with high affinity for immunoglobulin E (IgE) is known to consist of more than a single polypeptide. In addition to the IgE-binding α chain, the receptor contains a single β chain and two, disulfide-linked, γ chains. From a cDNA library of a rat mucosal mast cell tumor, from which we recently cloned cDNAs coding for the α chain, we have now isolated cDNAs coding for the β subunit. In vitro transcription-translation of the cDNA directed the synthesis of a polypeptide reactive with two distinctive anti-β monoclonal antibodies and whose molecular weight was identical to that of authentic β chains. Polyclonal antibodies to β peptides expressed in Escherichia coli reacted with intact receptors and isolated β chains. The gene encodes a protein of 243 residues with no leader sequence. A hydropathicity plot suggests that the polypeptide crosses the plasma membrane four times. The epitope recognized by one of the monoclonal antibodies was localized to the NH2 terminus; that by the other was localized to the COOH terminus. Since those antibodies react with membranes and not with intact cells, we suggest that both ends of the β subunit are cytoplasmic. RNA transfer blots at high stringency failed to reveal mRNA for β chains in a variety of cells (in particular, monocytes) that do not contain the high-affinity receptor for IgE.
Editor: Washington, DC: National Academy of Sciences of the United States of America
Idioma: Inglês

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Isolation and Characterization of cDNAs Coding for the β Subunit of the High-Affinity Receptor for Immunoglobulin E

Kinet, Jean-Pierre ; Blank, Ulrich ; Ra, Chisei ; White, Kenneth ; Metzger, Henry ; Kochan, Jarema

Washington, DC: National Academy of Sciences of the United States of America

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