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Thrombospondin functions as a cytoadhesion molecule for human hematopoietic
progenitor cells
MW Long and VM Dixit
Department of Pediatrics, University of Michigan, Ann Arbor 48109.
We explored the role that thrombospondin (TSP), a multifunctional
extracellular matrix protein, plays in hematopoietic cell-cell and cell-
matrix interactions. Thrombospondin synthesis is differentially regulated
in human long-term bone marrow cultures. Consistent with this, human
hematopoietic progenitor cells of all three lineages (erythrocyte,
megakaryocyte, and granulocyte) use TSP as an attachment protein. However,
terminally differentiated cells (erythrocytes and neutrophils) show absent
or reduced attachment to TSP. The region within the TSP molecule that
mediates cell attachment (cell binding domain) was delineated by examining
both attachment to proteolytic fragments of TSP and by inhibition of
cytoadhesion using monoclonal antibodies directed against TSP domains. The
cell binding domain resides toward the C-terminus of a 140 Kd chymotryptic
fragment of TSP. We conclude that thrombospondin functions as a
hematopoietic cytoadhesion molecule, capable of binding primary
hematopoietic progenitor cells, and may, therefore, be important in blood
cell development.
Volume 75,
Issue 12,
pp. 2311-2318,
06/15/1990
Copyright © 1990 by The American Society of Hematology
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