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We earlier reported calcium-dependent, heparin-like L-selectin
ligands in cultured bovine endothelial cells (Norgard-Sumnicht, K. E.,
Varki, N. M., and Varki, A.(1993) Science 261,480-483).
Here we show that these are heparan sulfate proteoglycans (HSPGs)
associated either with the cultured cells or secreted into the medium
and extracellular matrix. Activation of the endothelial cells with
bacterial lipopolysaccharide (LPS) does not markedly alter the amount
or distribution of this material. A major portion of the
glycosaminoglycan (GAG) chains released from these HSPGs by alkaline
Current
understanding of the biosynthesis of heparan sulfate chains indicates
that all glucosamine amino groups must be either N-acetylated
or N-sulfated. However, nitrous acid deamination at pH 4.0
suggests the presence of some unsubstituted amino groups in these
L-selectin-binding GAG chains from endothelial cell HSPGs. This is
confirmed by chemical N-reacetylation and by reactivity with
sulfo-N-hydroxysuccinimide-biotin. These unsubstituted amino
groups are also found on HSPGs from human umbilical vein endothelial
cells, but are not detected in those from Chinese hamster ovary cells.
In both bovine and human endothelial cells, these novel groups are
enriched for in the HS-GAG chains which bind to L-selectin. Despite
this, studies with N-reacetylation and nitrous acid
deamination do not show conclusive evidence for the direct involvement
of the unsubstituted amino groups in L-selectin binding. This may be
because the chemical reactions used to modify the amino groups do not
go to completion. Alternatively, the unsubstituted amino groups may
only be indirectly involved in generating binding, by dictating the
biosynthesis of another critical group. Regardless, these studies shown
that HSPGs from cultured endothelial cells which can bind to L-selectin
are enriched with unsubstituted amino groups on their GAG chains. The
possible biochemical mechanisms for generation of these novel groups
are discussed.
Volume 270,
Number 20,
Issue of May 19, pp. 12012-12024, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
-elimination rebinds to L-selectin in the presence of calcium,
indicating that these saccharides alone can mediate the high affinity
recognition. Heparin lyase digestions indicate that these GAG chains
are enriched in heparan sulfate, not heparin sequences.
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