Platelet-endothelial cell tetra-span antigen (PETA-3) was originally i
dentified as a novel human platelet surface glycoprotein, gp27, which
was detected by a monoclonal antibody (MoAb), 14A2.H1. Although this g
lycoprotein is present in low abundance on the platelet surface, MoAb
14A2.H1 stimulates platelet aggregation and mediator release. We now r
eport isolation of a cDNA clone encoding PETA-3 from a library derived
from the megakaryoblastic leukemia cell line MO7e. The clone encodes
an open reading frame of 253 amino acids that displays 25% to 30% amin
o acid sequence identity with several members of the newly defined Tet
raspan, or Transmembrane 4 superfamily. These proteins consist of four
conserved putative transmembrane domains with a large divergent extra
cellular loop between the third and fourth membrane-spanning regions,
PETA-3 has a single consensus sequence for N-linked glycosylation loca
ted in this extracellular loop. A single PETA-3 RNA transcript (1.6 kb
) was detected in RNA isolated from MO7e cells, bane marrow stromal ce
lls, the C11 endothelial cell line, and several myeloid leukemia cell
lines. No transcript was detected in the lymphoblastoid cell lines MOL
T-4 and BALM-1. This pattern correlates well with previous protein exp
ression data. Northern blot analysis of RNA from a range of human tiss
ues indicated that the transcript was present in most tissues, the not
able exception being brain. (C) 1995 by The American Society of Hemato
logy.