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J. Biol. Chem., Vol. 277, Issue 36, 32830-32836, September 6, 2002
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From the Despite numerous reports suggesting that
Hyposialylation of Integrins Stimulates the Activity of Myeloid
Fibronectin Receptors*
,,,
Department of Physiology and Biophysics,
University of Alabama at Birmingham, Birmingham, Alabama, 35294, the § Lakeside Veterans Administration Hospital,
Northwestern University Medical School and the Robert H. Lurie
Comprehensive Cancer Center, Chicago, Illinois, 60611, and the
¶ Department of Biochemistry and Molecular Biology, University of
Illinois College of Medicine, Chicago, Illinois, 60612
1 integrin receptors undergo differential
glycosylation, the potential role of N-linked carbohydrates
in modulating integrin function has been largely ignored. In the
present study, we find that 1 integrins are
differentially glycosylated during phorbol ester (PMA)-stimulated
differentiation of myeloid cells along the monocyte/macrophage lineage.
PMA treatment of two myeloid cell lines, U937 and THP-1, induces a
down-regulation in expression of the ST6Gal I sialyltransferase.
Correspondingly, the 1 integrin subunit becomes
hyposialylated, suggesting that the 1 integrin is a
substrate for this enzyme. The expression of hyposialylated
1 integrin isoforms is temporally correlated with
enhanced binding of myeloid cells to fibronectin, and, importantly, fibronectin binding is inhibited when the Golgi disrupter, brefeldin A,
is used to block the expression of the hyposialylated form. Consistent
with the observation that cells with hyposialylated integrins are more
adhesive to fibronectin, we demonstrate that the enzymatic removal of
sialic acid residues from purified 
51 integrins stimulates fibronectin binding by these integrins. These data
support the hypothesis that unsialylated 1 integrins are more adhesive to fibronectin, although desialylation of
5 subunits could also contribute to increased
fibronectin binding. Collectively our results suggest a novel mechanism
for regulation of the 1 integrin family of cell adhesion receptors.
*
This work was supported by National Institutes of Health
Grants RO1 CA84248 (to S. L. B.), 5 P60 AR 20614-23 (to S. L. B.), Hl5400 (to E. A. E.), and RO1 GM48134 (to K. J. C.), by a Veterans Administration Merit Review (to E. A. E.), and by a grant from the
University of Alabama Cell Adhesion and Matrix Research Center (to
S. L. B.).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: Dept. of
Physiology and Biophysics, Rm. 982A McCallum Building, 1918 University Blvd., Birmingham, AL 35294. Tel.: 205-934-3441; Fax:
205-975-9028; E-mail: bellis@ physiology.uab.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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