Carbohydrate-Protein Interactions in Vascular Biology

Nelson, Richard M.; Venot, André; Bevilacqua, Michael P.; Linhardt, R; Stamenkovic, Ivan

doi:10.1146/annurev.cb.11.110195.003125

Cited by 99 publications

(56 citation statements)

References 36 publications

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“…This interaction is the result of selectin and its carbohydrate ligand, either sLe x or HS. 13 When the rolling neutrophil stops, it anchors to the endothelium through integrin-based, strong proteinprotein interactions. The anchored neutrophil is now in a position to follow a chemotactic signal through the endothelium to the underlying tissue site of inflammation.…”

Section: Cell Adhesionmentioning

confidence: 99%

Role of Glycosaminoglycans in Cellular Communication

2004

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Glycosaminoglycans are of critical importance in intercellular communication in organisms. This ubiquitous class of linear polyanions interacts with a wide variety of proteins, including growth factors and chemokines, which regulate important physiological processes. The presence of glycosaminoglycans on cell membranes and in the extracellular matrix also has resulted in their exploitation by infectious pathogens to gain access and entry into animal cells. This Account examines the structural and physical characteristics of these molecules responsible for their interaction with proteins important in cell-cell communication.

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Section: Cell Adhesionmentioning

confidence: 99%

Role of Glycosaminoglycans in Cellular Communication

2004

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“…3,4 Although adhesion pathways utilized by tumor cells show considerable diversity, members of the selectin family of molecules and numerous neolactoseries antigens highly expressed on the tumor cell surface are involved in tumor metastasis by mediating binding of blood-borne tumor cells via E-and/or P-selectin to vascular endothelium. [5][6][7][8][9][10] Much of what we know about selectin interactions comes from studies of leukocytes. 11,12 Functionally, the binding of selectins to leukocytes requires sialylated and fucosylated carbohydrate structures; their prototypes are SAa2-3Galb1-4(Fuca1-3)GlcNAc and SAa2-3Galb1-3(Fuca1-4)GlcNAc, referred to as sLe x and sLe a , respectively.…”

mentioning

confidence: 99%

Deficiency in surface expression of E‐selectin ligand promotes lung colonization in a mouse model of breast cancer

Monzavi‐Karbassi

Whitehead

Jousheghany

et al. 2005

Intl Journal of Cancer

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Expression of sialyl Lewis x (sLe x ) and sLe a on tumor cells is thought to facilitate metastasis by promoting cell adhesion to selectins on vascular endothelial cells. Experiments supporting this concept usually bypass the early steps of the metastatic process by employing tumor cells that are injected directly into the blood. We investigated the relative role of sLe x oligosaccharide in the dissemination of breast carcinoma, employing a spontaneous murine metastasis model. An sLe x deficient subpopulation of the 4T1 mammary carcinoma cell line was produced by negative selection using the sLe x -reactive KM93 MAb. This subpopulation was negative for E-selectin binding but retained P-selectin binding. Both sLe x -negative and -positive cells grew at the same rate; however, sLe x -negative cells spread more efficiently on plates and had greater motility in wound-scratch assays. Mice inoculated in the mammary fat pad with sLe x -negative and -positive variants produced lung metastases. However, the number of lung metastases was significantly increased in the group inoculated with the sLe x -negative variant (p 5 0.0031), indicating that negative selection for the sLe x epitope resulted in enrichment for a subpopulation of cells with a high metastatic phenotype. Cell variants demonstrated significant differences in cellular morphology and pattern of tumor growth in primary and secondary tumor sites. These results strongly suggest that loss of sLe x may facilitate the metastatic process by contributing to escape from the primary tumor mass. ' 2005 Wiley-Liss, Inc.Key words: sialyl Lewis x antigen; metastasis; 4T1 cells; breast cancer Tumor metastasis is a multistep process requiring detachment of malignant cells from the primary tumor, penetration of blood or lymph vessels, attachment to endothelium of distant organs and formation of new tumor foci. 1,2 Tissue invasion and metastasis of tumor cells are highly dependent on cell-cell interactions, many of which involve alterations in cell surface glycosylation patterns. 3,4 Although adhesion pathways utilized by tumor cells show considerable diversity, members of the selectin family of molecules and numerous neolactoseries antigens highly expressed on the tumor cell surface are involved in tumor metastasis by mediating binding of blood-borne tumor cells via E-and/or P-selectin to vascular endothelium. [5][6][7][8][9][10] Much of what we know about selectin interactions comes from studies of leukocytes. 11,12 Functionally, the binding of selectins to leukocytes requires sialylated and fucosylated carbohydrate structures; their prototypes are SAa2-3Galb1-4(Fuca1-3)GlcNAc and SAa2-3Galb1-3(Fuca1-4)GlcNAc, referred to as sLe x and sLe a , respectively. [13][14][15] Both sLe x and sLe a are involved in selectin-mediated adhesion of cancer cells to vascular endothelium, and these determinants are thought to be closely associated with hematogenous metastasis of cancers. [16][17][18][19] These determinants not only are markers for cancer but also are functionally implicated ...

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“…[1][2][3][4][5][6][7][8][9][10][11][12] The naturally occurring ligands for the three selectins are mostly mucin-type glycoproteins carrying sialylated, fucosylated glycans. [1][2][3]7,9,[11][12][13][14][15] Recent studies suggest that selectin interactions with carcinoma cells may play pathological roles in tumor biology.…”

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confidence: 99%

“…16,17 The interactions of selectins with O-glycan chains involves primarily their N-terminal lectin and epidermal growth factor-like domains. 2,4,5,11,18 Sialylated and/or sulfated Lewis x/a and related structures are the most common glycan recognition elements for the selectins. 2,7,9,11,12 However, monovalent oligosaccharide ligands such as Sialyl Lewis x (Sia␣2-3Gal␤1-4(Fuc␣1-3)GlcNAc) and Sialyl Lewis a (Sia␣2-3Gal␤1-3(Fuc␣1-4)GlcNAc) bind with low affinity to the selectins, and O-glycans released from the natural high-affinity ligands do not show easily detectable rebinding.…”

mentioning

confidence: 99%