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Blood, 1 October 2001, Vol. 98, No. 7, pp. 2160-2165
IMMUNOBIOLOGY
Sperm protein 17 is expressed on normal and malignant lymphocytes
and promotes heparan sulfate-mediated cell-cell adhesion
H. Marie Lacy and
Ralph D. Sanderson
From the Arkansas Cancer Research Center, Departments
of Pathology and Anatomy, University of Arkansas for Medical Sciences,
Little Rock.
Sperm protein 17 (Sp17) is a highly conserved mammalian protein
present on acrosome-reacted sperm that is thought to promote fertilization by binding sulfated carbohydrates of the oocyte zona
pellucida. Although Sp17 was originally described as a testis-specific antigen, emerging evidence indicates that it may be more ubiquitously expressed than was previously thought. With the use of a
specific antiserum, Sp17 was found to be present on the surface
of malignant lymphoid cells, including B- and T-lymphoid cell lines,
and on the surface of primary cells isolated from 2 patients having
B-lymphoid tumors. Surprisingly, circulating B lymphocytes isolated
from healthy volunteers also expressed Sp17, while circulating T
lymphocytes exhibited only very weak expression. The role of Sp17 in
promoting lymphoid cell adhesion was addressed with the use of
recombinant Sp17 (rSp17). The rSp17 binds to the surface of
myeloma cells but not to cells pretreated with heparitinase, an enzyme
that removes heparan sulfate from the cell surface. Moreover, rSp17 promotes extensive aggregation of cells that express the
syndecan-1 heparan sulfate proteoglycan, but in contrast, cells lacking
syndecan-1 expression fail to aggregate in the presence of rSp17. These
findings suggest that Sp17 promotes heparan sulfate-mediated cell
aggregation and thereby plays a role in regulating adhesion and
migration of normal and malignant lymphocytes.
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