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Blood, Vol. 94 No. 8 (October 15), 1999:
pp. 2696-2703
Targeting of a Heterologous Protein to a Regulated Secretion
Pathway in Cultured Endothelial Cells
Yvonne H. Datta,
Hagop Youssoufian,
Peter W. Marks, and
Bruce M. Ewenstein
From the Division of Hematology, Brigham and Women's Hospital,
Boston, MA.
The stimulation of regulated exocytosis in vascular endothelial
cells (EC) by a variety of naturally occurring agonists contributes to
the interrelated processes of inflammation, thrombosis, and fibrinolysis. The Weibel-Palade body (WPB) is a well-described secretory granule in EC that contains both von Willebrand factor (vWF)
and P-selectin, but the mechanisms responsible for the targeting of
these proteins into this organelle remain poorly understood. Through
adenoviral transduction, we have expressed human growth hormone (GH) as
a model of regulated secretory protein sorting in EC.
Immunofluorescence microscopy of EC infected with GH-containing recombinant adenovirus (GHrAd) demonstrated a granular distribution of
GH that colocalized with vWF. In contrast, EC infected with an rAd
expressing the IgG1 heavy chain (IG), a constitutively secreted protein, did not demonstrate colocalization of IG and vWF. In
response to phorbol ester, GH as well as endogenously synthesized vWF
were rapidly released from GHrAd-infected EC. By
immunofluorescence microscopy, granular
colocalization of GH with endogenous tissue-type plasminogen activator
(tPA) was also demonstrated, and most of the tPA colocalized with vWF.
These data indicate that EC are capable of selectively targeting
heterologous proteins, such as GH, to the regulated secretory pathway,
which suggests that EC and neuroendocrine cells share common protein targeting recognition signals or receptors.
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