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Expression of syndecan regulates human myeloma plasma cell adhesion to type
I collagen
RC Ridley, H Xiao, H Hata, J Woodliff, J Epstein and RD Sanderson
Department of Pathology, University of Arkansas for Medical Sciences,
Little Rock 72205.
The syndecans comprise a family of integral membrane proteoglycans that
regulate cell behaviors by binding to extracellular matrix and binding
growth factors. In mouse blood cells, syndecan expression is restricted to
cells of the B-cell lineage where it is expressed by pre-B cells and plasma
cells, but is absent from circulating B cells. In the present study, we
examined the expression, structure, and function of syndecan on human
myeloma cell lines and myeloma patient bone marrow cells. On myeloma cells,
syndecan is a small (modal relative molecular mass [M(r)] = 120 Kd) heparan
sulfate proteoglycan localized at the cell surface. Syndecan was detected
by immunodot blotting on 7 of 10 human myeloma cell lines and by reverse
transcriptase polymerase chain reaction on 10 of 14 patient samples. Cell
binding assays show that myeloma cells expressing syndecan bind to type I
collagen via heparan sulfate chains, while those cell lines not expressing
syndecan do not bind to collagen. Furthermore, the cell lines expressing
syndecan were negative for CD19 and CD45 staining, indicating that syndecan
expression is restricted to tumors having a well-differentiated phenotype.
We conclude that syndecan acts as a matrix receptor on human myeloma cells
but is not expressed by all tumors, suggesting that syndecan may
participate in regulating myeloma cell adhesion to the bone marrow stromal
matrix.
Volume 81,
Issue 3,
pp. 767-774,
02/01/1993
Copyright © 1993 by The American Society of Hematology
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