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Synthesis of transforming growth factor-beta 1 by megakaryocytes and its
localization to megakaryocyte and platelet alpha-granules
RA Fava, TT Casey, J Wilcox, RW Pelton, HL Moses and LB Nanney
Department of Cell Biology, Vanderbilt University School of Medicine,
Nashville, TN.
We have directly demonstrated that megakaryocytes are a major site of
synthesis and storage of transforming growth factor-beta 1 (TGF/beta 1) by
combined immunohistochemical, immunocytochemical, and in situ hybridization
methods. The presence of TGF/beta 1 messenger RNA (mRNA) in mature
megakaryocytes in adult rat spleen and bone marrow (BM) was established by
in situ hybridization. Localization of TGF/beta 1 protein to intact
alpha-granules of megakaryocytes, its putative storage site, was
accomplished in glycol-methacrylate embedded porcine BM with an
immunoperoxidase technique and light microscopy. The TGF/beta 1 was
sequestered in intracytoplasmic granules in a pattern virtually identical
to that of another alpha-granule marker protein, fibrinogen. This
observation strongly suggests packaging of TGF/beta 1 into this organelle
within megakaryocytes. That TGF/beta 1 mRNA was localized to megakaryocytes
suggests that the TGF/beta 1 found in the alpha-granules in platelets
originates with megakaryocyte synthesis. The alpha-granule localization of
TGF/beta 1, as well as fibrinogen, was also demonstrated in isolated
platelets at the ultrastructural level by electronmicroscopy (EM) and
postembedding colloidal-gold immunocytochemistry, thus directly
demonstrating that alpha-granules are the final storage site for TGF/beta 1
in mature platelets.
Volume 76,
Issue 10,
pp. 1946-1955,
11/15/1990
Copyright © 1990 by The American Society of Hematology
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