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In Vivo Expression of Murine Platelet Glycoprotein Ib
Hiroyuki Fujita,
Yoshimi Hashimoto,
Susan Russell,
Barbara Zieger, and
Jerry Ware
From the Roon Research Center for Arteriosclerosis and Thrombosis,
Division of Experimental Hemostasis and Thrombosis, Departments of
Molecular and Experimental Medicine and Vascular Biology, The Scripps
Research Institute, La Jolla, CA.
We have performed a systematic in vivo evaluation of gene expression
for the glycoprotein (GP) Ib subunit of the murine platelet adhesion
receptor, GP Ib-IX-V. This study is warranted by in vitro observations
of human GP Ib expression in cells of nonhematopoietic lineage and
reports of regulation of the GP Ib gene by cytokines. However, an in
vivo role for a GP Ib-IX-V receptor has not been established beyond
that described for normal megakaryocyte/platelet physiology and
hemostasis. Our Northern analysis of mouse organs showed high levels of
GP Ib mRNA in bone marrow with a similar expression pattern
recapitulated in mice containing a luciferase transgene under the
control of the murine GP Ib promoter. Consistently high levels of
luciferase activity were observed in the two hematopoietic organs of
mice, bone marrow (1,400 relative light units/µg of protein [RLUs])
and spleen (500 RLUs). Reproducible, but low-levels of luciferase
activity were observed in heart, aorta, and lung (30 to 60 RLUs). Among
circulating blood cells, the luciferase activity was exclusively
localized in platelets. No increase in GP Ib mRNA or luciferase
activity was observed after treatment of mice with lipopolysaccharides
(LPS) or tumor necrosis factor- (TNF-). We conclude the murine GP
Ib promoter supports a high level of gene expression in
megakaryocytes and can express heterologous proteins allowing an in
vivo manipulation of platelet-specific proteins in the unique
environment of a blood platelet.
Blood, Vol. 92 No. 2 (July 15), 1998:
pp. 488-495
© 1998 by the American Society of Hematology.
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