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Molecular cloning of cDNA encoding a novel platelet-endothelial cell
tetra-span antigen, PETA-3
S Fitter, TJ Tetaz, MC Berndt and LK Ashman
Division of Haematology, Institute of Medical and Veterinary Science,
Adelaide, Australia.
Platelet-endothelial cell tetra-span antigen (PETA-3) was originally
identified as a novel human platelet surface glycoprotein, gp27, which was
detected by a monoclonal antibody (MoAb), 14A2.H1. Although this
glycoprotein is present in low abundance on the platelet surface, MoAb
14A2.H1 stimulates platelet aggregation and mediator release. We now report
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% amino acid sequence
identity with several members of the newly defined Tetraspan, or
Transmembrane 4 superfamily. These proteins consist of four conserved
putative transmembrane domains with a large divergent extracellular loop
between the third and fourth membrane-spanning regions. PETA-3 has a single
consensus sequence for N-linked glycosylation located in this extracellular
loop. A single PETA-3 RNA transcript (1.6 kb) was detected in RNA isolated
from MO7e cells, bone marrow stromal cells, the C11 endothelial cell line,
and several myeloid leukemia cell lines. No transcript was detected in the
lymphoblastoid cell lines MOLT-4 and BALM-1. This pattern correlates well
with previous protein expression data. Northern blot analysis of RNA from a
range of human tissues indicated that the transcript was present in most
tissues, the notable exception being brain.
Volume 86,
Issue 4,
pp. 1348-1355,
08/15/1995
Copyright © 1995 by The American Society of Hematology
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