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Sialyl-Lewis X Sale

(Synonyms: 唾液酸化酶X,sLeX) 目录号 : GC63191

Sialyl-Lewis X (sLeX) 是一种唾液酶酸化的聚四糖,是一种内源性抗原 (antigen)。Sialyl-Lewis X 是选择素 E-、P- 和 L- 的高亲和力配体 (ligand)。Sialyl-Lewis X 与 ELAM-1 和 CD62 结合,具有抑制 CD62 介导的炎症部位中性粒细胞募集的能力。

Sialyl-Lewis X Chemical Structure

Cas No.:98603-84-0

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产品描述

Sialyl-Lewis X (sLeX) is a sialylated fucosylated tetrasaccharide, an endogenous antigen. Sialyl-Lewis X is a high-affinity ligand for selectins (E-, P-, and L-selectin)[1]. Sialyl-Lewis X binds to ELAM-1 and CD62 and has the ability to inhibits CD62-mediated neutrophil recruitment to sites of inflammation[2].

Sialyl-Lewis X is a high-affinity ligand of CD62, Antibodies [mAb CSLEX (IgM; anti-sLeX)] to sLeX inhibit CD62-mediated binding of HL-60 cells to activated platelets[1].Liposomes containing glycolipids with the sLeX structure prevents adhesion of HL-60 cells and human neutrophils. HL-60 cell adhesion is partially inhibited (50%) by liposomes containing Lex at 5 μg/ml. However, sLeX liposomes give maximal inhibition at only 1 ug/ml. sLeX liposomes inhibits adhesion with a 10-fold higher affinity than Lex liposomes[1].CD62 binding of neutrophils to activated platelets is inhibited a soluble human milk oligosaccharide that contains the LeX structure. the sLeX sugar is a 30-fold more potent inhibitor than the nonsialylated Lex sugar, which requires 2 μg/ml and 54 μg/ml to achieve 50% inhibition of neutrophil adhesion, respectively[1].

[1]. M J Polley, et al. CD62 and Endothelial Cell-Leukocyte Adhesion Molecule 1 (ELAM-1) Recognize the Same Carbohydrate Ligand, sialyl-Lewis X. Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):6224-8.
[2]. L A Lasky, et al. Selectins: Interpreters of Cell-Specific Carbohydrate Information During Inflammation. Science

Chemical Properties

Cas No. 98603-84-0 SDF
别名 唾液酸化酶X,sLeX
分子式 C31H52N2O23 分子量 820.74
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5 mM 0.2437 mL 1.2184 mL 2.4368 mL
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Research Update

Microfibril associated protein 4 (MFAP4) is a carrier of the tumor associated carbohydrate Sialyl-Lewis X (sLex) in pancreatic adenocarcinoma

J Proteomics 2021 Jan 16;231:104004.PMID:33038510DOI:10.1016/j.jprot.2020.104004.

Late diagnosis of pancreatic ductal adenocarcinoma (PDA) is one of the reasons of its low 5-year survival rate and it is due to its unspecific symptoms during the first stages of the disease and the lack of reliable serological markers. Since PDA shows an altered glycan expression, here we have focused on finding novel potential biomarkers, namely glycoproteins that express the tumor associated carbohydrate structure Sialyl-Lewis X (sLex), which is described in PDA. Through a glycoproteomic approach, we have analyzed target proteins containing sLex from PDA tissues by 2DE and immunodetection techniques, and have identified by mass spectrometry the protein MFAP4 as a carrier of sLex in PDA. MFAP4 showed a higher expression in PDA tissues compared with pancreatic control tissues. In addition, the colocalization of sLex over MFAP4 was found only in PDA and not in control pancreatic tissues. The analysis of MFAP4 expression in PDA cell lines and their secretome, in combination with immunohistochemistry of pancreatic tissues, revealed that MFAP4 was not produced by PDA cells, but it was found in the pancreatic extracellular matrix. The specificity of MFAP4 glycoform containing sLex in PDA tissues shows its relevance as a potential PDA biomarker. SIGNIFICANCE: Despite advances in the field of cancer research, pancreatic ductal adenocarcinoma (PDA) lacks of a specific and sensitive biomarker for its early detection, when curative resection is still possible before metastases arise. Thus, efforts to discover new PDA biomarkers represent the first line in the fight against the increase of its incidence reported in recent years. Glycan alterations on glycoconjugates, such as glycoproteins have emerged as a rich source for the identification of novel cancer markers. In the present work, we aimed to shed light on novel biomarkers based on altered glycosylation in PDA, in particular those glycoproteins of PDA tissues carrying the tumor carbohydrate antigen Sialyl-Lewis X (sLex). Through a glycoproteomic approach, we have shown that the glycoprotein MFAP4 carries sLex in PDA tissues and not in control pancreatic tissues. MFAP4 is found in the extracellular matrix in PDA and although its role in cancer progression is unclear, its sLex glycoform could be a potential biomarker in pancreatic ductal adenocarcinoma.

Enforced sialyl-Lewis-X (sLeX) display in E-selectin ligands by exofucosylation is dispensable for CD19-CAR T-cell activity and bone marrow homing

Clin Transl Med 2021 Feb;11(2):e280.PMID:33634970DOI:10.1002/ctm2.280.

CD19-directed chimeric antigen receptors (CAR) T cells induce impressive rates of complete response in advanced B-cell malignancies, specially in B-cell acute lymphoblastic leukemia (B-ALL). However, CAR T-cell-treated patients eventually progress due to poor CAR T-cell persistence and/or disease relapse. The bone marrow (BM) is the primary location for acute leukemia. The rapid/efficient colonization of the BM by systemically infused CD19-CAR T cells might enhance CAR T-cell activity and persistence, thus, offering clinical benefits. Circulating cells traffic to BM upon binding of tetrasaccharide Sialyl-Lewis X (sLeX)-decorated E-selectin ligands (sialofucosylated) to the E-selectin receptor expressed in the vascular endothelium. sLeX-installation in E-selectin ligands is achieved through an ex vivo fucosylation reaction. Here, we sought to characterize the basal and cell-autonomous display of sLeX in CAR T-cells activated using different cytokines, and to assess whether exofucosylation of E-selectin ligands improves CD19-CAR T-cell activity and BM homing. We report that cell-autonomous sialofucosylation (sLeX display) steadily increases in culture- and in vivo-expanded CAR T cells, and that, the cytokines used during T-cell activation influence both the degree of such endogenous sialofucosylation and the CD19-CAR T-cell efficacy and persistence in vivo. However, glycoengineered enforced sialofucosylation of E-selectin ligands was dispensable for CD19-CAR T-cell activity and BM homing in multiple xenograft models regardless the cytokines employed for T-cell expansion, thus, representing a dispensable strategy for CD19-CAR T-cell therapy.

FUT6 deficiency compromises basophil function by selectively abrogating their Sialyl-Lewis X expression

Commun Biol 2021 Jul 2;4(1):832.PMID:34215830DOI:10.1038/s42003-021-02295-8.

Sialyl-Lewis X (sLex, CD15s) is a tetra-saccharide on the surface of leukocytes required for E-selectin-mediated rolling, a prerequisite for leukocytes to migrate out of the blood vessels. Here we show using flow cytometry that sLex expression on basophils and mast cell progenitors depends on fucosyltransferase 6 (FUT6). Using genetic association data analysis and qPCR, the cell type-specific defect was associated with single nucleotide polymorphisms (SNPs) in the FUT6 gene region (tagged by rs17855739 and rs778798), affecting coding sequence and/or expression level of the mRNA. Heterozygous individuals with one functional FUT6 gene harbor a mixed population of sLex+ and sLex- basophils, a phenomenon caused by random monoallelic expression (RME). Microfluidic assay demonstrated FUT6-deficient basophils rolling on E-selectin is severely impaired. FUT6 null alleles carriers exhibit elevated blood basophil counts and a reduced itch sensitivity against insect bites. FUT6-deficiency thus dampens the basophil-mediated allergic response in the periphery, evident also in lower IgE titers and reduced eosinophil counts.