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Expression on blood cells of sialophorin, the surface glycoprotein that is
defective in Wiskott-Aldrich syndrome
E Remold-O'Donnell, C Zimmerman, D Kenney and FS Rosen
Sialophorin, previously called gpL115, is the heavily sialylated surface
protein that is defective in lymphocytes of Wiskott-Aldrich syndrome
patients. Using the monoclonal antibody L10 as a probe, sialophorin
expression was detected on isolated T lymphocytes and thymocytes, B cell
lines, monocytes, neutrophils, and platelets, but not on erythrocytes,
fibroblasts, and glioblastoma cells. This unusual distribution pattern
suggests that sialophorin is expressed on all circulating cells except
erythrocytes. Trace amounts of the sialophorin molecules on lymphocytes are
incompletely sialylated, but significant amounts of the molecules on
thymocytes are incompletely sialylated. The molecular form of sialophorin
on T lymphocytes, thymocytes, and monocytes is the previously characterized
species of apparent mol wt 115,000. A newly described sialophorin species
of apparent mol wt 135,000 was found on neutrophils and platelets. The
115,000 lymphocyte/monocyte form and the 135,000 platelet/neutrophil form
were shown to be substantially similar. The two forms have approximately
the same content of sialylated O-linked carbohydrate units since both
undergo the same atypical shift in electrophoretic mobility on
desialylation. Both contain the epitope recognized by the monoclonal
antibody L2 and the epitope recognized by L10 antibody. Moreover, evidence
from another study indicates that the polypeptide portions are identical,
cumulatively suggesting that 115,000 sialophorin and 135,000 sialophorin
are identical except for the presence on the latter of additional neutral
saccharide residues.
Volume 70,
Issue 1,
pp. 104-109,
07/01/1987
Copyright © 1987 by The American Society of Hematology
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