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J. Biol. Chem., Vol. 276, Issue 20, 17101-17105, May 18, 2001
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From the Center for Reproductive Sciences, Department of
Obstetrics, Gynecology and Reproductive Sciences, University of
California, San Francisco, California 94143-0556
Human glycodelin is synthesized by
endometrial cells in the late secretory phase and early pregnancy under
hormonal regulation. Whereas the precise physiological functions of
glycodelin are unknown, its expression during embryonic nidation and
its inhibition of T cell proliferation suggest an immunomodulatory
role. We purified human glycodelin from first trimester human decidual
cytosol by using a rapid two-step high-performance liquid
chromatography method and investigated its effects on human monocyte
migration. Human U937 cells were used as a model of monocyte chemotaxis
in Boyden chamber migration assays. N-Formyl-Met-Leu-Phe
and the
Purification and Characterization of an Immunomodulatory
Endometrial Protein, Glycodelin*
-chemokine RANTES (regulated on activation normal T cell
expressed and secreted) were used as monocyte chemoattractants.
Purified glycodelin inhibited monocyte migration in a
dose-dependent fashion (IC50 = 550 nM). Glycodelin activity was totally reversed by heat inactivation (95 °C × 15 min) and neutralized by pretreatment with specific anti-glycodelin antibodies. Deglycosylated glycodelin was
equipotent to intact glycodelin in the monocyte migration assay.
125I-Glycodelin binding to whole U937 cells revealed
a single, saturable site with a Kd = 48 ± 21 nM by Scatchard analysis. Cross-linking studies indicated
that glycodelin binds to a high molecular mass (~250 kDa)
protein complex at the monocyte cell surface. Our findings support the
hypothesis that glycodelin reduces the local maternal inflammatory
response toward the implantation of a semiallogeneic conceptus.
*
This work was supported by the Philippe Foundation
(Paris, France) and a National Institutes of Health grant from the
NICHD, through cooperative agreement U54-HD37321, as part of the
Specialized Cooperative Centers Program in Reproduction Research.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Director, Center for
Reproductive Sciences, HSE 1689, Dept. of Obstetrics, Gynecology and
Reproductive Sciences, University of California, San Francisco, CA
94143-0556. Tel.: 415-476-9214; Fax: 415-753-3271; E-mail: rtaylor@socrates.ucsf.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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