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Y Shiota, JG Wilson, K Harjes, ED Zanjani and M Tavassoli
Department of Veterans Affairs Medical Center, Jackson, MS 39216.
The adhesion of hematopoietic progenitor cells to bone marrow stromal cells
is critical to hematopoiesis and involves multiple effector molecules.
Stromal cell molecules that participate in this interaction were sought by
analyzing the detergent-soluble membrane proteins of GBI/6 stromal cells
that could be adsorbed by intact FDCP-1 progenitor cells. A single-chain
protein from GBI/6 cells having an apparent molecular weight of 37 Kd was
selectively adsorbed by FDCP-1 cells. This protein, designated p37, could
be surface-radiolabeled and thus appeared to be exposed on the cell
membrane. An apparently identical 37- Kd protein was expressed by three
stromal cell lines, by Swiss 3T3 fibroblastic cells, and by FDCP-1 and
FDCP-2 progenitor cells. p37 was selectively adsorbed from membrane lysates
by a variety of murine hematopoietic cells, including erythrocytes, but not
by human erythrocytes. Binding of p37 to cells was calcium-dependent, and
was not affected by inhibitors of the hematopoietic homing receptor or the
cell-binding or heparin-binding functions of fibronectin. It is proposed
that p37 may be a novel adhesive molecule expressed on the surface of a
variety of hematopoietic cells that could participate in both homotypic and
heterotypic interactions of stromal and progenitor cells.
This article has been cited by other articles:
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| Copyright © 1993 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||