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Signaling and induction of enhanced cytoadhesiveness via the hematopoietic
progenitor cell surface molecule CD34
O Majdic, J Stockl, WF Pickl, J Bohuslav, H Strobl, C Scheinecker, H Stockinger and W Knapp
Institute of Immunology, University of Vienna, Austria.
The transmembrane glycoprotein CD34 shows a highly restricted expression on
a crucial subset of hematopoietic cells. We show here that engagement of
particular determinants of CD34 can lead to signal transduction and to
enhanced adhesiveness of CD34+ hematopoietic cells. Monoclonal antibodies
(MoAbs) directed against O-sialoglycoprotease- sensitive epitopes of CD34
(QBEND10, ICH3, BI.3C5, MY10) but not MoAbs against
O-sialoglycoprotease-resistant epitopes (9F2, 8G12) induce actin
polymerization in KG-1a and KG-1 cells and strongly enhanced
cytoadhesiveness. The capacity to induce adhesion requires cellular energy,
divalent cations, and intact cytoskeleton but not de novo protein
synthesis. The observed cytoadhesion seems at least in part to be caused by
a concomitant activation of the beta 2 integrin cytoadhesion pathway. It
can be significantly inhibited with lymphocyte function-associated
antigen-1 and intercelluar adhesion molecule-1 antibodies. Protein kinase
inhibition analyses suggest that the pathways initiated by engagement of
the CD34 molecule with certain CD34 MoAbs involves protein tyrosine kinases
but that protein kinase C is not critically involved.
Volume 83,
Issue 5,
pp. 1226-1234,
03/01/1994
Copyright © 1994 by The American Society of Hematology
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