Laminin-dependent and laminin-independent adhesion of human melanoma cells to sulfatides

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Standard

Laminin-dependent and laminin-independent adhesion of human melanoma cells to sulfatides. / Roberts, D D; Wewer, U M; Liotta, L A; Ginsburg, V.

I: Cancer Research, Bind 48, Nr. 12, 15.06.1988, s. 3367-73.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Roberts, DD, Wewer, UM, Liotta, LA & Ginsburg, V 1988, 'Laminin-dependent and laminin-independent adhesion of human melanoma cells to sulfatides', Cancer Research, bind 48, nr. 12, s. 3367-73.

APA

Roberts, D. D., Wewer, U. M., Liotta, L. A., & Ginsburg, V. (1988). Laminin-dependent and laminin-independent adhesion of human melanoma cells to sulfatides. Cancer Research, 48(12), 3367-73.

Vancouver

Roberts DD, Wewer UM, Liotta LA, Ginsburg V. Laminin-dependent and laminin-independent adhesion of human melanoma cells to sulfatides. Cancer Research. 1988 jun. 15;48(12):3367-73.

Author

Roberts, D D ; Wewer, U M ; Liotta, L A ; Ginsburg, V. / Laminin-dependent and laminin-independent adhesion of human melanoma cells to sulfatides. I: Cancer Research. 1988 ; Bind 48, Nr. 12. s. 3367-73.

Bibtex

@article{7e2eed5b34c545ec8654cdb377a93836,
title = "Laminin-dependent and laminin-independent adhesion of human melanoma cells to sulfatides",
abstract = "Sulfatides (galactosylceramide-I3-sulfate) but not neutral glycolipids or gangliosides adsorbed on plastic promote adhesion of the human melanoma cell line G361. Direct adhesion of G361 cells requires densities of sulfatide greater than 1 pmol/mm2. In the presence of laminin, however, specific adhesion of G361 cells to sulfatide or seminolipid (galactosylalkylacyl-glycerol-I3-sulfate) but not to other lipids is strongly stimulated and requires only 25 fmol/mm2 of adsorbed lipid. The effects of laminin and sulfatide on adhesion are synergistic, suggesting that laminin is mediating adhesion by cross-linking receptors on the melanoma cell surface to sulfatide adsorbed on the plastic. Although thrombospondin binds to sulfatides and G361 cells, it does not enhance, but rather inhibits direct and laminin-dependent G361 cell adhesion to sulfatide. In contrast, C32 melanoma cells also adhere specifically to sulfatide, but adhesion of these cells is not enhanced by laminin or inhibited by antibodies to laminin that block laminin-dependent adhesion of G361 cells. Thrombospondin is a potent inhibitor of C32 cell adhesion to sulfatide. Fucoidan, which inhibits laminin binding to sulfatide, inhibits laminin-dependent adhesion of G361 cells by 50% at 0.2 micrograms/ml. Several other tumor cell lines also attach directly on sulfatide-coated surfaces. Laminin stimulates adhesion to sulfatide of three of the six cell lines tested. The ability of laminin to promote adhesion of tumor cells to sulfatide suggests that binding to sulfatide could participate in laminin-mediated cell-cell adhesion. Thus, many tumor cell lines can attach on sulfatide substrates using endogenous sulfatide binding proteins, and in some cells laminin but not thrombospondin can promote tumor cell adhesion to sulfatide.",
keywords = "Adsorption, Cell Adhesion, Glycoproteins, Humans, Laminin, Lipid Metabolism, Melanoma, Polysaccharides, Receptors, Immunologic, Receptors, Laminin, Sulfoglycosphingolipids, Thrombospondins, Tumor Cells, Cultured",
author = "Roberts, {D D} and Wewer, {U M} and Liotta, {L A} and V Ginsburg",
year = "1988",
month = jun,
day = "15",
language = "English",
volume = "48",
pages = "3367--73",
journal = "Cancer Research",
issn = "0008-5472",
publisher = "American Association for Cancer Research",
number = "12",

}

RIS

TY - JOUR

T1 - Laminin-dependent and laminin-independent adhesion of human melanoma cells to sulfatides

AU - Roberts, D D

AU - Wewer, U M

AU - Liotta, L A

AU - Ginsburg, V

PY - 1988/6/15

Y1 - 1988/6/15

N2 - Sulfatides (galactosylceramide-I3-sulfate) but not neutral glycolipids or gangliosides adsorbed on plastic promote adhesion of the human melanoma cell line G361. Direct adhesion of G361 cells requires densities of sulfatide greater than 1 pmol/mm2. In the presence of laminin, however, specific adhesion of G361 cells to sulfatide or seminolipid (galactosylalkylacyl-glycerol-I3-sulfate) but not to other lipids is strongly stimulated and requires only 25 fmol/mm2 of adsorbed lipid. The effects of laminin and sulfatide on adhesion are synergistic, suggesting that laminin is mediating adhesion by cross-linking receptors on the melanoma cell surface to sulfatide adsorbed on the plastic. Although thrombospondin binds to sulfatides and G361 cells, it does not enhance, but rather inhibits direct and laminin-dependent G361 cell adhesion to sulfatide. In contrast, C32 melanoma cells also adhere specifically to sulfatide, but adhesion of these cells is not enhanced by laminin or inhibited by antibodies to laminin that block laminin-dependent adhesion of G361 cells. Thrombospondin is a potent inhibitor of C32 cell adhesion to sulfatide. Fucoidan, which inhibits laminin binding to sulfatide, inhibits laminin-dependent adhesion of G361 cells by 50% at 0.2 micrograms/ml. Several other tumor cell lines also attach directly on sulfatide-coated surfaces. Laminin stimulates adhesion to sulfatide of three of the six cell lines tested. The ability of laminin to promote adhesion of tumor cells to sulfatide suggests that binding to sulfatide could participate in laminin-mediated cell-cell adhesion. Thus, many tumor cell lines can attach on sulfatide substrates using endogenous sulfatide binding proteins, and in some cells laminin but not thrombospondin can promote tumor cell adhesion to sulfatide.

AB - Sulfatides (galactosylceramide-I3-sulfate) but not neutral glycolipids or gangliosides adsorbed on plastic promote adhesion of the human melanoma cell line G361. Direct adhesion of G361 cells requires densities of sulfatide greater than 1 pmol/mm2. In the presence of laminin, however, specific adhesion of G361 cells to sulfatide or seminolipid (galactosylalkylacyl-glycerol-I3-sulfate) but not to other lipids is strongly stimulated and requires only 25 fmol/mm2 of adsorbed lipid. The effects of laminin and sulfatide on adhesion are synergistic, suggesting that laminin is mediating adhesion by cross-linking receptors on the melanoma cell surface to sulfatide adsorbed on the plastic. Although thrombospondin binds to sulfatides and G361 cells, it does not enhance, but rather inhibits direct and laminin-dependent G361 cell adhesion to sulfatide. In contrast, C32 melanoma cells also adhere specifically to sulfatide, but adhesion of these cells is not enhanced by laminin or inhibited by antibodies to laminin that block laminin-dependent adhesion of G361 cells. Thrombospondin is a potent inhibitor of C32 cell adhesion to sulfatide. Fucoidan, which inhibits laminin binding to sulfatide, inhibits laminin-dependent adhesion of G361 cells by 50% at 0.2 micrograms/ml. Several other tumor cell lines also attach directly on sulfatide-coated surfaces. Laminin stimulates adhesion to sulfatide of three of the six cell lines tested. The ability of laminin to promote adhesion of tumor cells to sulfatide suggests that binding to sulfatide could participate in laminin-mediated cell-cell adhesion. Thus, many tumor cell lines can attach on sulfatide substrates using endogenous sulfatide binding proteins, and in some cells laminin but not thrombospondin can promote tumor cell adhesion to sulfatide.

KW - Adsorption

KW - Cell Adhesion

KW - Glycoproteins

KW - Humans

KW - Laminin

KW - Lipid Metabolism

KW - Melanoma

KW - Polysaccharides

KW - Receptors, Immunologic

KW - Receptors, Laminin

KW - Sulfoglycosphingolipids

KW - Thrombospondins

KW - Tumor Cells, Cultured

M3 - Journal article

C2 - 2967105

VL - 48

SP - 3367

EP - 3373

JO - Cancer Research

JF - Cancer Research

SN - 0008-5472

IS - 12

ER -

ID: 34330159