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J. Biol. Chem., Vol. 266, Issue 24, 15966-15973, Aug, 1991
JP Arm, MF Gurish, DS Reynolds, HC Scott, CS Gartner, KF Austen and HR Katz
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.
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
Department of Medicine, Harvard Medical School, Boston, Massachusetts 02115.
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