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(Received for publication, July 5,
1995; and in revised form, August 4, 1995) P-selectin glycoprotein ligand-1 (PSGL-1) is a mucin-like
glycoprotein on leukocytes that is a high affinity ligand for
P-selectin. Previous studies have shown that sialylation and
fucosylation of PSGL-1 are required for its binding to P-selectin, but
other post-translational modifications of PSGL-1 may also be important.
We demonstrate that PSGL-1 synthesized in human HL-60 cells can be
metabolically labeled with [
Volume 270,
Number 39,
Issue of September 29, pp. 22677-22680, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
S]sulfate that is
incorporated primarily into tyrosine sulfate. Treatment of PSGL-1 with
a bacterial arylsulfatase releases sulfate from tyrosine, resulting in
a concordant decrease in binding to P-selectin. These studies
demonstrate that tyrosine sulfate on PSGL-1 functions in conjunction
with sialylated and fucosylated glycans to mediate high affinity
binding to P-selectin.
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