Molecular cloning of gp49, a cell-surface antigen that is preferentially expressed by mouse mast cell progenitors and is a new member of the immunoglobulin superfamily

gp49 is a Mr 49,000 glycoprotein expressed on the surface of mouse bone marrow-derived mast cells, which are progenitors for the major in vivo mast cell subclasses, typified by intestinal mucosal mast cells and serosal mast cells. The amino-terminal amino acid sequence of gp49 was determined after i...

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Bibliographic Details
Published in:The Journal of biological chemistry 1991-08, Vol.266 (24), p.15966-15973
Main Authors: ARM, J. P, GURISH, M. F, REYNOLDS, D. S, SCOTT, H. C, GARTNER, C. S, AUSTEN, K. F, KATZ, H. R
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino Acids - analysis
Analytical, structural and metabolic biochemistry
Animals
Antigens, Surface - genetics
Base Sequence
Biological and medical sciences
Blotting, Northern
Blotting, Southern
cDNA
cell surface
Cloning, Molecular
DNA - genetics
Electrophoresis, Polyacrylamide Gel
Fundamental and applied biological sciences. Psychology
genes
glycoprotein gp49
Glycoproteins
Immunoglobulins - genetics
mast cells
Mast Cells - metabolism
Membrane Glycoproteins - genetics
Mice
Molecular Sequence Data
Multigene Family
nucleotide sequence
predictions
Proteins
Receptors, Immunologic
RNA - genetics
Sequence Alignment
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Summary:gp49 is a Mr 49,000 glycoprotein expressed on the surface of mouse bone marrow-derived mast cells, which are progenitors for the major in vivo mast cell subclasses, typified by intestinal mucosal mast cells and serosal mast cells. The amino-terminal amino acid sequence of gp49 was determined after isolation of the solubilized membrane protein by affinity chromatography with the B23.1 anti-gp49 monoclonal antibody. Redundant oligonucleotides were used to isolate a full-length 1.3-kilobase cDNA from a mouse mast cell library. The predicted amino acid sequence contains a signal peptide of 23 residues, an extracellular domain of 215 residues with three potential sites of N-linked glycosylation, a transmembrane domain of 23 residues, and a cytoplasmic tail of 42 residues. Hybridization of the gp49 cDNA was limited to mRNA extracted from those cell types that also bound the B23.1 monoclonal antibody as assessed by cytofluorographic analyses. The predicted extracellular domain of gp49 contains two regions of 48 and 51 amino acids, each flanked by cysteine residues. Both regions meet criteria for being C2-type domains of the immunoglobulin superfamily based upon the alignment of consensus amino acids and their predicted secondary structure organization. Thus, gp49, a membrane glycoprotein preferentially expressed by the progenitor mast cell population, is a new member of the immunoglobulin superfamily.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)98502-9