Galectin-8 Functions as a Matricellular Modulator of Cell Adhesion

Levy, Yinon; Arbel-Goren, Rinat; Hadari, Yaron R.; Eshhar, Sharon; Ronen, Denise; Elhanany, Eythan; Geiger, Benjamin; Zick, Yehiel

doi:10.1074/jbc.m100340200

Cited by 156 publications

(197 citation statements)

References 54 publications

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“…The inhibitory effects of lectins on cell adhesion are a widespread phenomenon observed in a number of cell lines and involve protein sugar interactions. For example, galectin-8 inhibited the growth of three cell lines including Hela [7]. Didemnum ternatanum lectin (DTL) also inhibits the proliferative activity of Hela cells grown on solid substrate and acts to slow cell growth, interfering in cell attachment and spreading [1].…”

Section: Xcl Induces Actin Cytoskeleton Modificationsmentioning

confidence: 99%

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Inhibitory action of a new lectin from Xerocomus chrysenteron on cell-substrate adhesion

Marty-Detraves¹,

Francis²,

Baricault³

et al. 2004

Mol Cell Biochem

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Lectins are carbohydrate-binding proteins which potentially link to cell surface glycoconjugates and affect cell proliferation. We investigated the effect of a new lectin from the mushroom Xerocomus chrysenteron (XCL) on cell proliferation using adherent and suspension cell lines. XCL caused a dose-dependent inhibition of proliferation of the adherent cell lines NIH-3T3 and HeLa. Several experiments suggest that disruption of cell-substrate adhesion is the main factor affecting cell growth inhibition. (i) No antiproliferative effect was observed on the SF9 cell line, which does not require to be attached to grow. (ii) XCL was shown to affect the adherence of cells following their suspension by trypsin treatment. (iii) XCL was localized on the cell surface where it would act as a coating agent. (iv) XCL induced morphological changes from well spread to rounded cells and disrupted the actin cytoskeleton. By contrast, flow cytometric analysis showed that XCL does not interfere with the cell cycle, and does not induce apoptosis. (Mol Cell Biochem 258: [49][50][51][52][53][54][55] 2004)

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Section: Xcl Induces Actin Cytoskeleton Modificationsmentioning

confidence: 99%

“…From 1-2 h, cells which were able to adhere were spread. Whereas most of cell lines are commonly spread after 2 h at 37°C [7], the early phases of cell adhesion occurred in the first 30 min. At this time, early focal contacts are present at the edges of the cells.…”

Section: Xcl Induces Actin Cytoskeleton Modificationsmentioning

confidence: 99%

Inhibitory action of a new lectin from Xerocomus chrysenteron on cell-substrate adhesion

Marty-Detraves¹,

Francis²,

Baricault³

et al. 2004

Mol Cell Biochem

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“…Inhibition of ERK1/2 Phosphorylation and DNA Synthesis by Thiodigalactoside-Thiodigalactoside (TDG) is one of the potent hapten inhibitors of ␤-galactoside binding (46,47). Preliminary studies were performed to ensure that TDG has no stimulatory effect on both ERK1/2 activation and DNA synthesis in HSCs.…”

Section: Effects Of Inhibitors Of Pkc and Pka On Erk1/2 Phosphorylatimentioning

confidence: 99%

Stimulation of Proliferation of Rat Hepatic Stellate Cells by Galectin-1 and Galectin-3 through Different Intracellular Signaling Pathways

Maeda

Kawada

Seki

et al. 2003

Journal of Biological Chemistry

138

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We found that the expression of galectin-1 and galectin-3 was significantly up-regulated in hepatic stellate cells (HSCs) both in the course of their transdifferentiation into myofibroblasts, a process of "self-activation," and in the fibrosis of liver tissues. Recombinant galectin-1 and galectin-3 stimulated the proliferation of cultured HSCs via the MEK1/2-ERK1/2 signaling pathway. However, galectin-3 utilized protein kinases C and A to induce this process, whereas galectin-1 did not. We also found that thiodigalactoside, a potent inhibitor of ␤-galactoside binding, attenuated the effects of both galectins. In addition, galectin-1, but not galectin-3, promoted the migration of HSCs. Thus, it appears that galectin-1 and galectin-3, generated by activated HSCs, could participate in ␤-galactoside binding and induce different intracellular signaling pathways leading to the proliferation of HSCs.

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“…Galectin-8 is also reported to be a physiological modulator of cell adhesion. When immobilized, it functions as a matrix protein equipotent to fibronectin in promoting cell adhesion by ligation and clustering of cell surface integdn receptors (77).…”

Section: The Galectin Family Of Proteins and Metagenesismentioning

confidence: 99%

Characterization of lectins and their specificity in carcinomas—An appraisal

Sherwani

Mohmood

Khan

et al. 2003

Indian J Clin Biochem

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Lectins, a group of specific glycoproteins present in animal as well as plant cells, are used as differentiating markers to study cancers and metastatic cell lines. This property of lectins depends on the process of cellular glycosylation. Glycosylation of some of the extracellular membrane proteins and lipids maintains the cell/cell and cell/matrix interactions. Chemical alterations in glycosylation play an important role in the metastatic behavior of tumor cells. Carbohydrate residues of the membrane glycoproteins can be detected using lectins due to their binding specificity to carbohydrates. Lectins, therefore have gained an importance in the field of cancer research. Galectins, a specialized group of lectin like proteins that are Ca+ independent and galactoside binding, are also considered as differentiation markers in some specific cancers like the carcinomas of thyroid.Thus the use of lectins and galectins to identify specific carbohydrates present on cell surface help in invasion and metastasis processes.

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Galectin-8 Functions as a Matricellular Modulator of Cell Adhesion

Cited by 156 publications

References 54 publications

Inhibitory action of a new lectin from Xerocomus chrysenteron on cell-substrate adhesion

Inhibitory action of a new lectin from Xerocomus chrysenteron on cell-substrate adhesion

Stimulation of Proliferation of Rat Hepatic Stellate Cells by Galectin-1 and Galectin-3 through Different Intracellular Signaling Pathways

Characterization of lectins and their specificity in carcinomas—An appraisal

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