Structural requirements for the carbohydrate ligand of E-selectin.

Tyrrell, D J; James, Paul G.; Rao, Narasinga B.N.; Foxall, Carrol; Abbas, Saeed A.; Dasgupta, Falguni; Nashed, Mina A.; Hasegawa, Akira; Kiso, Makoto; Asa, Darwin

doi:10.1073/pnas.88.22.10372

Cited by 230 publications

(102 citation statements)

References 28 publications

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“…3). This is not unexpected, because the carboxyl group at C-1 position of sialic acid is known to be important in binding to selectins (24,25), and this compound lacks the group.…”

Section: Resultsmentioning

confidence: 99%

Regulation of selectin binding activity by cyclization of sialic acid moiety of carbohydrate ligands on human leukocytes

Mitsuoka

Ohmori

Kimura

et al. 1999

Proc. Natl. Acad. Sci. U.S.A.

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We provide here evidence that supports the occurrence of a biologically dormant form of selectin ligand carbohydrate, the sialyl 6-sulfo Lewis X containing modified sialic acid, in human leukocytes. The modification of sialic acid involves first de-N-acetylation of sialic acid moiety through ubiquitous de-N-acetylation͞re-N-acetylation cycle, followed by the dehydrative cyclization of de-N-acetyl sialic acid to form ''cyclic sialic acid.'' The enzyme involved in the dehydration of de-N-acetyl sialic acid is a calcium-dependent enzyme having neutral-alkaline pH optimum. De-N-acetyl sialyl 6-sulfo Lewis X retained selectin binding activity as well as parental sialyl 6-sulfo Lewis X, but cyclic sialyl 6-sulfo Lewis X was devoid of selectin binding activity. Sialyl 6-sulfo Lewis X carrying the cyclic sialic acid is specifically recognized by the newly generated mAb, G159. The determinant was distributed widely among normal human leukocytes, especially on monocytes and subsets of lymphocytes including NK cells, helper memory T cells, Tcr-␥␦ T cells, and a part of B cells. The determinant was detected also on several cultured lymphocytic leukemia cell lines and O-tetradecanoylphorbol 13-acetate-activated lymphoid cells. Cyclic sialyl 6-sulfo Lewis X is efficiently formed by the action of the partly membranebound calcium-dependent enzyme, tentatively called ''sialic acid cyclase,'' and a possible physiological significance of this reaction could be a rapid inactivation of selectin binding activity at the cell surface. Conversely, the accumulated intracellular cyclic sialyl 6-sulfo Lewis X determinant may function as a dormant pool of selectin ligands, which, on appropriate stimulation, is hydrolyzed and becomes active in selectin-dependent cell adhesion.

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“…3). This is not unexpected, because the carboxyl group at C-1 position of sialic acid is known to be important in binding to selectins (24,25), and this compound lacks the group.…”

Section: Resultsmentioning

confidence: 99%

Regulation of selectin binding activity by cyclization of sialic acid moiety of carbohydrate ligands on human leukocytes

Mitsuoka

Ohmori

Kimura

et al. 1999

Proc. Natl. Acad. Sci. U.S.A.

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“…So far, the GalNAc variant of Le x, carried on oligosaccharide alditols, released from sea squirt H-antigen [1], has been shown to induce allergic skin reactions in humans [26]. However, no role in interaction processes, as found for Le x [27] and carbohydrate ligands having the Le x epitope as structural element (sialyl-Le x, VIM-2 structure, sulfoLe x) [28][29][30], has been reported. In this context, it should be mentioned that comparison of the time-averaged conformations of G(F)Gn and GN(F)Gn shows that Gal OH-2 and GalNAc NAc are oriented to the outside of the models.…”

Section: Discussionmentioning

confidence: 99%

Conversion of GalNAcβ(1–4)GlcNAcβ‐OMe into GalNAcβ(1–4)‐[Fucα(1–3)]GlcNAcβ‐OMe using human milk α3/4‐fucosyltransferase synthesis of a novel terminal element in glycoprotein glycans

et al. 1993

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Incubation of GalNAcβ(1–4)GlcNAcβ‐OMe with GDP‐Fuc in the presence of human milk α3/4‐fucosyltransferase resulted in the formation of GalNAcβ(1–4)[Fucα(1–3)]GlcNAcβ‐OMe. Under conditions that led to complete α3‐fucosylation of Galβ(1–4)GlcNAcβ‐OEt, GalNAcβ(1–4)GlcNAcβ‐OMe was fucosylated for more than 85%. For the identification of the isolated fucosylated products one‐ and two‐ dimensional 1H‐NMR spectroscopy was applied. In vacuo molecular dynamics simulations of Galβ(1–4)[Fucα(1–3)]GlcNAcβ‐OEt and GalNAcβ(1–4)[Fucα(1–3)]GlcNAcβ‐OMe using the CHARMm based force field CHEAT, demonstrated only small differences between the conformations of these compounds. This illustrates the minor conformational influence of the substituent at C‐2′, i.e. a hydroxyl function versus a N‐acetyl group.

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“…Obviously, the determination of the monosaccharide specificities is only a step in the right direction towards fully understanding the interaction between collectins and their biologically relevant targets. The well-defined groups of oligosaccharide ligands, like the sialyl Lewis x family of carbohydrate structures (Tyrrell et al, 1991), were available in the study of selectin mediated cell adhesion, but no such well-defined groups of oligosaccharide ligands have yet been identified to allow study of collectin function. It is important t o characterize the natural oligosaccharide ligands for the collectins to allow assessment of collectin-mediated reactions, such as complement activation or opsonization.…”

Section: Perspectivesmentioning

confidence: 99%

Collectins — soluble proteins containing collagenous regions and lectin domains — and their roles in innate immunity

1994

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The collectins are a group of mammalian lectins containing collagen-like regions. They include mannan binding protein, bovine conglutinin, lung surfactant protein A, lung surfactant protein D, and a newly discovered bovine protein named collectin-43. These proteins share a very similar modular domain composition and overall 3-dimensional structure. They also appear to play similar biological roles in the preimmune defense against microorganisms in both serum and lung surfactant. The close evolutionary relationship between the collectins is further emphasized by a common pattern of exons in their genomic structures and the presence of a gene cluster on chromosome 10 in humans that contains the genes known for the human collectins. Studies on the structure/function relationships within the collectins could provide insight into the properties of a growing number of proteins also containing collagenous regions such as Clq, the hibernation protein, the a-and 0-ficolins, as well as the membrane acetylcholinesterase and the macrophage scavenger receptor.

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Structural requirements for the carbohydrate ligand of E-selectin.

Cited by 230 publications

References 28 publications

Regulation of selectin binding activity by cyclization of sialic acid moiety of carbohydrate ligands on human leukocytes

Regulation of selectin binding activity by cyclization of sialic acid moiety of carbohydrate ligands on human leukocytes

Conversion of GalNAcβ(1–4)GlcNAcβ‐OMe into GalNAcβ(1–4)‐[Fucα(1–3)]GlcNAcβ‐OMe using human milk α3/4‐fucosyltransferase synthesis of a novel terminal element in glycoprotein glycans

Collectins — soluble proteins containing collagenous regions and lectin domains — and their roles in innate immunity

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