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J Biol Chem, Vol. 274, Issue 26, 18213-18217, June 25, 1999
From the The cell adhesion molecule L-selectin binds to
3'-sialyl-Lewis (Le)x and -Lea and to
3'-sulfo-Lex and -Lea sequences. The binding to
3'-sialyl-Lex is strongly affected by the presence of
6-O-sulfate as found on oligosaccharides of the counter
receptor, GlyCAM-1; 6-O-sulfate on the
N-acetylglucosamine (6-sulfation) enhances, whereas
6-O-sulfate on the galactose (6'-sulfation) virtually
abolishes binding. To extend knowledge on the specificity of
L-selectin, we have investigated interactions with novel
sulfo-oligosaccharides based on the Lex pentasaccharide
sequence. We observe that, also with 3'-sulfo-Lex, the
6-sulfation enhances and 6'-sulfation suppresses L-selectin binding.
The 6'-sulfation without 3'-sialyl or 3'-sulfate gives no binding
signal with L-selectin. Where the 6-sulfo,3'-sialyl-Lex is
on an extended di-N-acetyllactosamine backbone, additional 6-O-sulfates on the inner galactose and inner
N-acetylglucosamine do not influence the binding. Although
binding to the 6,3'-sulfo-Lex and
6-sulfo,3'-sialyl-Lex sequences is comparable, the former
is a more effective inhibitor of L-selectin binding. This difference is
most apparent when L-selectin is in paucivalent form (predominantly di-
and tetramer) rather than multivalent. Indeed, as inhibitors of the
paucivalent L-selectin, the 3'-sulfo-Lex series are more
potent than the corresponding 3'-sialyl-Lex series. Thus,
for synthetic strategies to design therapeutic oligosaccharide analogs
as antagonists of L-selectin binding, those based on the simpler
3'-sulfo-Lex (and also the 3'-sulfo-Lea) would
seem most appropriate.
L-selectin, a carbohydrate-binding adhesion molecule on leukocytes
that binds to saccharide ligands on high endothelial cells in
post-capillary venules of lymph nodes, has a key role in the initial
stages of leukocyte extravasation into peripheral lymph nodes and areas
of acute and chronic inflammation (1, 2). Previous work with
structurally defined oligosaccharides has shown that L-selectin binds
to Lewisa
(Lea)1 and
Lex sequences sialylated or sulfated at position 3 of outer
galactose with a preference for binding to 3'-sialyl-Lea
over 3'-sialyl-Lex (3) and a preference of
3'-sulfo-Lea and 3'-sulfo-Lex over the sialyl
forms (4-6). The occurrence of 3'-sulfated forms of Lex
and Lea has been documented on epithelial glycoproteins,
and this led to the demonstration that sulfate can substitute
effectively for sialic acid in ligands for the E- and L-selectins (4,
7, 8). Among these four sequences, the strongest binding signal is with
the 3'-sulfo-Lea (6). These findings are important for the
design of synthetic, potentially therapeutic analogs of the selectin
ligands, as chemical synthesis of sulfated oligosaccharides is far more
facile than of sialyl-oligosaccharides. O-glycosidic
oligosaccharides with other sulfation patterns have been isolated from
one of the counter-receptors of L-selectin, GlyCAM-1; these are
heptasaccharides with 3'-sialyl-Lex capping groups
containing 6-O-sulfate at the outer galactose (referred to
as 6'-O-sulfation), at the penultimate
N-acetylglucosamine (6-O-sulfation), or at both
of these positions (6',6-O-sulfation) (9). We have
demonstrated that the 6-sulfo,3'-sialyl-Lex sequence
constitutes a strong ligand for L-selectin, particularly where the
N-acetylneuraminic acid is de-N-acetylated,
whereas the 6'-sulfated analog is not bound (10, 24). Indeed, the addition of 6'-O-sulfate to the
6-sulfo,3'-sialyl-Lex sequence impairs the L-selectin binding.
Knowing that 3-O-sulfation at galactose of Lex
or Lea can substitute for 3'-sialylation in the formation
of saccharide motifs recognized by the selectins, we have explored in
the present study the reactivities of human L-selectin with a novel
series of mono- and multisulfated Lex sequences in which
the 3'-sialyl residue on Lex is replaced by
3'-O-sulfate, and we make a comparison with reactivity toward the 3'-sulfo-Lea sequence, which is among the most
potent L-selectin ligands thus far described, and also with reactivity
toward the 6'-sulfo-Lex. We report here results that reveal
an advantage of 3'-sulfation over 3'-sialylation of Lex
with respect to inhibitory activity toward L-selectin binding and the
deleterious effect of 6'-sulfation of Lex with respect both
to binding and inhibitory activity toward L-selectin binding. We also
examine L-selectin binding to a novel trisulfated sequence,
3'-sialyl,6-sulfo-di-N-acetyl lactosamine, with two additional sulfates, one at the inner galactose and another at the
inner N-acetylglucosamine residue (both at position 6). We show that the additional sulfates along the extended backbone do not
influence the binding signal.
Oligosaccharides, Neoglycolipids, and Glycosylceramides--
The
carbohydrate sequences investigated are shown in Table
I. The following were synthesized
chemically: the 3'-sulfo-Lea (11); the
3'-sulfo-Lex, the 6',3'-sulfo-Lex;
the 6,3'-sulfo-Lex; the 6'-sulfo-Lex (12); and
also the 3'-sialyl-Lex
pentasaccharide,2 GSC151,
(13). These were purified by high pressure liquid chromatography using
a TSK-Gel® amide 80 column (Tosohaas) (6).
Lacto-N-tetraose and lacto-N-neo-tetraose were
purchased from Dextra. The oligosaccharide designated C4U was prepared
by keratanase II digestion of bovine articular keratan sulfate
essentially as described by Brown et al. (14). The
oligosaccharide designated Fuc-C4U was derived from C4U by fucosylation
using milk Recombinant Soluble L-selectins--
A soluble form of
human-L-selectin fused to the human immunoglobulin (IgG) Fc domain and
expressed in transfected Chinese hamster ovary cells (provided by G. Shaw, Genetics Institute Inc., Cambridge, Massachusetts) was isolated
from tissue culture supernatant as described previously (6). This
preparation consisted predominantly of tetramers of L-selectin as
assessed by gel filtration analysis (6) and is referred to here as
paucivalent. For binding experiments, where indicated, preparations of
the multivalent L-selectin were made by incubating for 1 h with
goat anti-human immunoglobulin heavy and light chains (Vector) at a
selectin:antibody ratio of 1:3 by weight. This ratio was selected from
a range, 1:0.5 to 1:10, as it gave the highest binding signal with
immobilized reference compounds 3'-sulfo-Lea and
3'-sialyl-Lea.
L-selectin Binding and Inhibition Assays--
For direct binding
experiments (10), purified lipid-linked oligosaccharides (glycolipids
and neoglycolipids) were immobilized on microwells (Falcon 3912). About
30% of the lipid-linked oligosaccharides added were retained in the
microwells under the binding assay conditions (6). Fifty ng of
multivalent L-selectin IgG chimera was applied per well using as
diluent 10 mM Tris buffer, pH 7.4, containing 150 mM NaCl and 2 mM Ca2+. As in
previous experiments with E-selectin (7), binding intensity of
L-selectin was of the same order to the 3'-sialyl-Lex
sequence in the form of a glycosylceramide or a neoglycolipid (not
shown). For inhibition experiments, the immobilized oligosaccharides used were either the lipid-linked 6-sulfo,3'-sialyl-Lex or
6,3'-sulfo-Lex (100 pmol added per well) and 10 ng of the multivalent L-selectin or 50 ng of the paucivalent L-selectin
were added per well. These levels of L-selectin were used in the
inhibition experiments as they gave comparable binding signals with the
two immobilized ligands. Serial dilutions of liposomes containing
lipid-linked oligosaccharides were used as inhibitors. These consisted
of cholesterol:lecithin:lipid-linked oligosaccharides at ratios of
0.4:0.4:1 by weight.
Binding of Multivalent L-selectin to Mono- and Multisulfated
Sequences--
In accord with earlier observations (6), the
3'-sulfo-Lex sequence was bound by human L-selectin but
less strongly than 3'-sulfo-Lea. However, the
6'-sulfo-Lex was not bound (Fig.
1A). The
6-O-sulfation of 3'-sulfo-Lex to give
6,3'-sulfo-Lex elicited enhanced L-selectin binding,
whereas the 6'-sulfated analog (6',3'-sulfo-Lex)
consistently showed some diminution of binding. The binding signal
observed with the 6,3'-sulfo-Lex sequence was of the same
order as that observed with the 6-sulfo,3'-sialyl-Lex (Fig.
1C). Thus, 6-sulfation, but not 6'-sulfation, has a
potentiating effect on human L-selectin binding not only to the
3'-sialyl-Lex, as shown previously (Ref. 10 and Fig.
1B), but also to the 3'-sulfo-Lex sequence. The
hindering effect of the 6'-O-sulfation was less pronounced
on 3'-sulfo-Lex than on the 3'-sialyl-Lex
analog investigated previously (Fig. 1B) (10).
Binding experiments with the oligosaccharide C4U and its 3'-fucosylated
analog, Fuc-C4U, clearly showed that the presence of the fucose residue
is essential for L-selectin binding to the 3'-sialyl,6-sulfated
di-N-acetyllactosamine backbone (Fig. 1D). The
binding signals with the Fuc-C4U and the
6-sulfo,3'-sialyl-Lex were similar, indicating that the
additional sulfates on the internal galactose and
N-acetylglucosamine residues do not influence the L-selectin
binding signal.
Inhibition of the Binding of Multivalent
L-selectin--
Inhibition experiments were performed with the
multivalent L-selectin using as immobilized ligands the
6-sulfo,3'-sialyl-Lex or the 6,3'-sulfo-Lex
(Figs. 2 and
3, A and B); all of
the acidic compounds of the Lex series tested gave some
inhibition of binding. The nonsulfated lacto-N-tetraose gave
no inhibition. The 6,3'-sulfo-Lex (IC50
1.4 × 10 Inhibition of the Binding of Paucivalent
L-selectin--
Inhibition of binding experiments using the
paucivalent L-selectin was performed (Figs. 3, C and
D, and 4) to discriminate more
clearly (6) between relatively high and low affinity inhibitors and
under conditions that may possibly simulate situations in vivo where L-selectin is relatively sparsely expressed. The degree of inhibition of selectin binding depended on the immobilized ligand
used; binding to the 6,3'sulfo-Lex was harder to inhibit
than to the 6-sulfo,3'-sialyl-Lex (Fig. 3, C and
D). Here the 3'-sialyl-Lex series were poorer
inhibitors overall than the corresponding 3'-sulfo-Lex
analogs and gave no significant inhibition when the
6,3'-sulfo-Lex was used as the immobilized ligand (Fig.
3D); when the 6-sulfo,3'-sialyl-Lex was used as
the immobilized ligand (Fig. 3C), only the homologous oligosaccharide sequence showed reasonable inhibition (IC50
1.6 × 10 It is clear from the binding experiments described here, first,
that, in contrast to 3'-sulfation of Lex, which supports
L-selectin reactivity, the 6'-sulfation does not elicit a detectable
binding signal. Second, the L-selectin reactivities of 3'-sulfo- and
3'-sialyl-Lex are similarly influenced by the addition of
6'-sulfate or 6-sulfate. Whereas 6'-sulfation has a negative effect,
6-sulfation has an enhancing effect on L-selectin binding to the
clustered, immobilized 3'-sulfo- and 3'-sialyl-Lex series.
Thus the 6-sulfate seems to be a part of the recognition motif for
L-selectin, whereas 6'-sulfate is not. Moreover, its presence partially
hinders the recognition of the 3'-sialyl- or 3'-sulfo-Lex
by the selectin. The enhancement of L-selectin binding in the presence
of 6-sulfation was substantial for both the 3'-sulfo- and the
3'-sialyl-Lex sequences, but the negative effect of
6'-sulfation was less pronounced with the 3'-sulfo-Lex than
with the 3'-sialyl-Lex sequence investigated previously
(10). Third, whereas the 6-sulfate on the subterminal
N-acetylglucosamine of the Lex sequence is
clearly a part of the recognition sequence for L-selectin, additional
sulfates along the di-N-acetyllactosamine backbone are not
recognized. Fourth, the presence of the 3'-linked fucose on
6-sulfo,3'-sialyl-Lex is essential for L-selectin binding.
In accord with this finding is an earlier report that L-selectin
binding is abolished by modification of the fucose in the
3'-sialyl-Lex sequence by removal of oxygen at position 2, 3, or 5 (18). The presence of the fucose is apparently less critical in
the 3'-sulfo-Lex sequence as it has been observed that the
defucosylated 3'-sulfo-Lex tri- and tetrasaccharides are
bound by L-selectin, albeit less strongly than the
3'-fucosyl analogs (4, 5).
The inhibition experiments described here reveal subtle differences in
L-selectin reactivities that are not apparent in the binding
experiments, namely a slightly greater binding affinity toward the
3'-sulfo than the 3'-sialyl-Lex. The 6-sulfated
3'-sulfo-Lex sequence had a greater inhibitory activity
than the 6-sulfated 3'-sialyl-Lex, although the binding
signals they elicited were similar. The differences were more apparent
in inhibition experiments where the paucivalent L-selectin was used;
these experiments clearly showed differences in the ease of inhibition
of L-selectin binding depending on the immobilized ligand used, and
they showed that inhibitory activities of the 3'-sulfo-Lex
series were greater than those of the 3'-sialyl-Lex series.
Collectively, these data, together with the earlier finding (4) that
the 3'-sulfo- but not the 3'-sialyl-lactosamine backbone (in the
absence of fucose) elicits a binding signal with L-selectin, indicate
that the 3'-sulfation at the galactose of Lex creates a
higher affinity ligand than the 3'-sialylation and that L-selectin has
overall a higher affinity toward the 3'-sulfo- and
6,3'-sulfo-Lex sequences than the corresponding
3'-sialyl-Lex analogs.
The inhibition experiments were performed here using as inhibitors
oligosaccharides linked to a lipid and displayed on liposomes as it was
found earlier that about 10,000-fold less oligosaccharide material is
required compared with the free oligosaccharides (6); the
IC50 values are in the nanomolar range (30-50
nM with the best inhibitors) when displayed on liposomes
and millimolar with the free oligosaccharides. This is in accord with
results from other groups who have examined free oligosaccharides as
inhibitors of L-selectin binding; the reported IC50 values
range from 0.2 to 6 mM (19-22). When examined in the
oligomeric state on dendrimers, IC50 values in the 1-10
µM range were reported (23). A general feature that
emerges from our inhibition experiments using L-selectin in the
multivalent state and those of other groups who have used the
multivalent L-selectin is that differences in inhibitory activities of
the various acidic Lex and Lea oligosaccharides
are less marked. Also, in the multivalent assay, the differing ease of
inhibition of L-selectin binding to different immobilized ligands is
less readily discernible.
The modification to the inhibition assay that we have introduced serves
to establish a hierarchy of inhibitory activities that may be relevant
in in vivo situations where the display of L-selectin is
relatively sparse. Thus, the inhibition assay with paucivalent
L-selectin establishes that the 3'-sulfo-Lex series and
also the 3'-sulfo-Lea are more effective inhibitors of the
L-selectin binding than the 3'-sialyl-Lex
analogs. Among these, the 6,3'-sulfo-Lex and the
monosulfated 3'-sulfo-Lea are the most potent inhibitors of
L-selectin binding among the oligosaccharide sequences so far tested.
The former is only marginally better. Therefore, from the point of view
of synthetic strategies for the design of therapeutic oligosaccharide
analogs, those based on the relatively simple structure
3-sulfo-Lex and -Lea would seem the most appropriate.
We thank Dr. Chun-Ting Yuen and Dr. Colin
Herbert for preparation of the neoglycolipids and the purification of
the glycosylceramides, Dr. Gray Shaw for the
L-selectin-transfected Chinese hamster ovary cell line, Dr.
Robert Childs for helpful discussions, and Margaret Runnicles for help
in preparation of the manuscript.
*
This work was supported by program Grants E400/622 and
G9601454 from the Medical Research Council.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. Tel.:
44-181-869-3460/3461; Fax: 44-181-869-3455; E-mail:
t.feizi{at}ic.ac.uk.
2
For ease of comparison of the
sialyl-Lex and -Lea with the
sulfo-Lex and -Lea oligosaccharides, the term
pentasaccharide is used to denote the fucosyl tetrasaccharide backbones
that they share.
3
G. M. Brown, manuscript in preparation.
The abbreviation used is:
Lea and
Lex, Lewisa and Lewisx.
L-selectin Interactions with Novel Mono- and Multisulfated
Lewisx Sequences in Comparison with the Potent Ligand
3'-Sulfated Lewisa*
,
, and**
Glycosciences Laboratory, Imperial College
School of Medicine, Northwick Park Hospital, Watford Road, Harrow,
Middlesex HA1 3UJ, United Kingdom, § Laboratoire de
Chimie Organique Multifunctionelle, Universite du Paris Sud, Orsay,
Cedex 91405, France, ¶ Department of Applied Bioorganic
Chemistry, Gifu Universisty, Gifu, 501-11, Japan, and the
Department of Biological Sciences, Institute of Environmental
and Natural Sciences, Lancaster University, Lancaster,
LA1 4YQ, United Kingdom
ABSTRACT
TOP
ABSTRACT
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
INTRODUCTION
TOP
ABSTRACT
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
MATERIALS AND METHODS
TOP
ABSTRACT
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
-(1-3/4)-fucosyltransferase; oligosaccharide identity was
corroborated by 1H NMR spectroscopy, and purity was
established using high pH anion exchange
chromatography.3
Neoglycolipids (15) were prepared by conjugation of the above oligosaccharides to the amino phospholipid
L-1,2-dihexadecyl-sn-glycerol-3-phosphoethanolamine and purified, and their composition and sequences were corroborated by
liquid secondary ion mass spectroscopy as described previously (16).
The following were chemically synthesized glycosylceramides: the
3'-sialyl-Lex (13); the 6'-sulfo,3'-sialyl-Lex;
the 6-sulfo,3'-sialyl-Lex; and the
6',6-sulfo,3'-sialyl-Lex (17) designated GSC64, GSC268,
GSC269, and GSC270, respectively. These were purified by preparative
TLC as described previously (10).
Carbohydrate sequences investigated
RESULTS
TOP
ABSTRACT
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
View larger version (36K):
[in a new window]
Fig. 1.
Binding of multivalent human L-selectin to
immobilized lipid-linked oligosaccharides. Varying amounts of
(neo)glycolipids in a solution of carrier lipids were applied onto the
microwells, and 50 ng of L-selectin/well, in the presence
of anti-immunoglobulins, was added. Binding was detected by a
biotin-streptavidin-horseradish peroxidase system as described
previously (6). Results are expressed as means in duplicate wells with
the range indicated by error bars. The results in
B are taken from Ref. 10. See Table I for
abbreviations.
7 and 1.5 × 107
M with the two immobilized ligands) was approximately 3 and
5 times more active as an inhibitor than the
6-sulfo,3'-sialyl-Lex (5.1 × 107 and
6.9 × 107 M). The least active
inhibitors were the nonsulfated 3'-sialyl-Lex
(IC50 3.7 × 106 and 6.8 × 106 M), the 6'-sulfo-Lex
(3.1 × 106 and 2.0 × 106
M) and the 6'-sulfo,3'-sialyl-Lex (7.4 × 106 and 1.0 × 106 M).
Fine comparisons of the inhibitory activities of the relatively potent
sequences were difficult as inhibition curves were often closely spaced
or partially overlapping as in Fig. 2B.
View larger version (33K):
[in a new window]
Fig. 2.
Inhibition of the binding of the multivalent
human L-selectin by lipid-linked oligosaccharides of the
3'-sulfo-Lex and the 3'-sialyl-Lex series
displayed on liposomes. The inhibition of the binding of
L-selectin (10 ng/well) was assayed as described under
"Materials and Methods." For clarity, results with selected
compounds are shown; the IC50 values for all of the tested
compounds are shown in Fig. 3. The immobilized ligand in A
and C was the 6-sulfo,3'-sialyl-Lex, and in
B and D it was 6,3'-sulfo-Lex.
Specific binding signals were 1.0-1.4
(A490 nm) in the absence of inhibitor after
subtracting the signals in control wells containing carrier lipid only.
Results are expressed as means in duplicate wells with the range
indicated by error bars. See Table I for
abbreviations.
View larger version (39K):
[in a new window]
Fig. 3.
Activities of lipid-linked oligosaccharides
of the 3'-sulfo-Lex and 3'-sialyl-Lex series as
inhibitors of the binding of human L-selectin to immobilized 6-sulfo,
3'-sialyl-Lex (A and C)
and 6,3'sulfo-Lex (B and
D). Results of inhibition experiments with the
multivalent selectin are shown in A and B and
with the paucivalent selectin in C and D. The
inhibitory activities are expressed as IC50 values and have
been assembled from experiments of which selected inhibition curves
only are shown in Figs. 2 and 4. Where results from two experiments are
assembled as in A (Fig. 2, taken from experiments 1 and 3)
and in C (Fig. 4, taken from experiments 4 and 6), the
IC50 values were normalized relative to that of
6,3'-sulfo-Lex, which was included as a reference compound.
See Table I for abbreviations.
6 M). In contrast, among the
oligosaccharides in which there was 3'-sulfate instead of 3'-sialyl,
all inhibited the selectin binding to the two immobilized ligands. The
6'-sulfo-Lex was not inhibitory. The
3'-sulfo-Lex and the 6,3'-sulfo-Lex stood out
as superior inhibitors with IC50 values of 1.4 × 107 and 5.0 × 107 M, and
5 × 108 and 2.7 × 107
M, respectively. Also included in the present inhibition
experiments for comparison was the 3'-sulfo-Lea sequence;
its potency was intermediate between that of 3'-sulfo-Lex
and 6,3'-sulfo-Lex (Fig. 3, C and
D).
View larger version (34K):
[in a new window]
Fig. 4.
Inhibition of the binding of the paucivalent
human L-selectin by lipid-linked oligosaccharides of the
3'-sulfo-Lex and 3'-sialyl-Lex series,
displayed on liposomes. The inhibition of the binding of 50 ng/well of the paucivalent L-selectin was assayed as
described under "Materials and Methods." For clarity, results with
selected compounds are shown; the IC50 values for all of
the tested compounds are shown in Fig. 3. The immobilized ligand in
A and C was the
6-sulfo,3'-sialyl-Lex, and in B and D
it was the 6,3'-sulfo-Lex. Specific binding signals were
0.8-1.2 (A490 nm) in the absence of inhibitor
after subtracting the signals in control wells containing carrier lipid
only. Results are expressed as means in duplicate wells with the range
indicated by error bars. See Table I for
abbreviations.
DISCUSSION
TOP
ABSTRACT
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
ACKNOWLEDGEMENTS
FOOTNOTES
ABBREVIATIONS
REFERENCES
TOP
ABSTRACT
INTRODUCTION
MATERIALS AND METHODS
RESULTS
DISCUSSION
REFERENCES
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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 P. Andre, O. Spertini, S. Guia, P. Rihet, F. Dignat-George, H. Brailly, J. Sampol, P. J. Anderson, and E. Vivier Modification of P-selectin glycoprotein ligand-1 with a natural killer cell-restricted sulfated lactosamine creates an alternate ligand for L-selectin PNAS, March 28, 2000; 97(7): 3400 - 3405. [Abstract] [Full Text] [PDF]
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