Galectin-3 Stimulates Cell Proliferation

Inohara, Hidenori; Akahani, Shiro; Raz, Avraham

doi:10.1006/excr.1998.4253

Cited by 177 publications

(146 citation statements)

References 37 publications

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“…In contrast, because galectin-3 was strongly present in ductular complexes and to a lesser extent in the degenerating acinar cells, it might exert paracrine effects on surrounding fibroblasts, including the modulation of their proliferative capacity. Similar mitogenic capabilities were reported for galectin-3 after fibroblast proliferation was stimulated in a paracrine fashion through interaction with cell-surface glycoconjugates of normal human IMR-90 lung fibroblasts (Inohara et al, 1998).…”

Section: Discussionsupporting

confidence: 81%

Galectin-1 and Galectin-3 in Chronic Pancreatitis

Wang

Frieß

Zhu

et al. 2000

Laboratory Investigation

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SUMMARY:Galectin-1 and galectin-3 have important functions in cell-cell interactions, cell adhesion to extracellular matrix, the organization of extracellular matrix, and tissue remodeling. To assess their potential role in chronic pancreatitis (CP), we examined their expression by Northern blot analysis, in situ hybridization, immunohistochemistry, and Western blot analysis in normal and CP pancreatic tissues. Northern blot analysis revealed a 4.5-fold increase of galectin-1 mRNA (p Ͻ 0.01) and a 3.8-fold increase of galectin-3 mRNA (p Ͻ 0.01) in CP samples compared with normal controls. In situ hybridization analysis of normal pancreas indicated low abundance of galectin-1 mRNA in fibroblasts, whereas galectin-3 mRNA was moderately present in ductal cells. CP samples exhibited moderate to intense galectin-1 mRNA signals in fibroblasts, whereas galectin-3 mRNA signals were intense in the cells of ductular complexes and weak in the degenerating acinar cells. In addition, intense galectin-1 and galectin-3 mRNA signals were present in nerves of normal and CP samples. Immunohistochemistry showed a distribution pattern of galectin-1 and galectin-3 similar to that described for in situ hybridization. Relative quantification of galectin-1 and galectin-3 protein by immunoblotting revealed an increase of 3.2-fold and 3.0-fold, respectively, in CP compared with normal controls. There was a significant correlation between galectin-1 and fibrosis and between galectin-3 and fibrosis and the density of ductular complexes. Up-regulation of galectin-1 in fibroblasts and galectin-3 in ductular complexes suggests a role of these lectins in tissue remodeling in CP. Galectin-1 might participate in ECM changes, whereas galectin-3 seems to be involved in both ECM changes and ductular complex formation. (Lab Invest 2000, 80:1233-1241.

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Section: Discussionsupporting

confidence: 81%

Galectin-1 and Galectin-3 in Chronic Pancreatitis

Wang

Frieß

Zhu

et al. 2000

Laboratory Investigation

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“…There have been reports that galectin-3 can also modulate the growth of fibroblasts by interacting with their surface glycoconjugates (17). Our present study revealed that both galectin-1 and galectin-3 promote the proliferation of HSCs.…”

Section: Discussionsupporting

confidence: 70%

“…Galectin-1 and galectin-3 are present intracellularly (both in the cytoplasm and the nucleus), extracellularly, and at the cell surface (10 -14). Galectin-1 and galectin-3 play roles in cell proliferation (15)(16)(17), differentiation (18,19), adhesion (20, 21), neoplastic transformation (22,23), and apoptosis (24 -26), and in the interaction of neoplastic cells with ECMs (27)(28)(29). Over such a wide range of influences, galectins are thought to modulate cell signaling by cross-linking with target molecules through their ␤-galactoside-containing glycoconjugates (30,31).…”

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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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“…1B). At this time, 18.5% of all glomeruli were still negative, but 81.5% were positive, although most of them (48.3% of total) were positive in ≤25% of glomerular area ( Table 2). Expression of Gal-3 was already observed in glomeruli from diabetic rats at 2 months of disease duration (Fig.…”

Section: Resultsmentioning

confidence: 91%

“…Intracellularly, it acts as a pre-mRNA-splicing factor (16) and participates in the regulation of cell proliferation and death, the latter due to its sequence homology and association with bcl-2 (17). By virtue of its proproliferative (17,18) and antiapoptotic (17) actions, it is considered as an immediate early gene (19) possibly implicated in tumor growth.…”

mentioning

confidence: 99%

The diabetic milieu modulates the advanced glycation end product-receptor complex in the mesangium by inducing or upregulating galectin-3 expression.

et al. 2000

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Nonenzymatic glycation has been implicated in the pathogenesis of the dysregulated tissue remodeling that characterizes diabetic glomerulopathy, via the formation of advanced glycation end products (AGEs) and their binding to cell surface receptors. Several AGEbinding proteins have been identified so far, including p60, p90, and the adhesive and growth-regulating lectin galectin-3 (Gal-3), the components of the so-called AGEreceptor complex. This study aimed to evaluate the mesangial expression of the AGE-receptor complex and its modulation by the diabetic milieu, both in vivo, in nondiabetic versus streptozotocin-induced diabetic rats, and in vitro, in mesangial cells exposed to either normal glucose (NG) levels (5.5 mmol/l), as compared with high glucose (HG) levels (30 mmol/l) and iso-osmolar mannitol (M), or to native bovine serum albumin (BSA), as compared with glycated BSA with AGE formation (BSA-AGE) and glycated BSA in which AGE formation was prevented by aminoguanidine (BSA-AM). In vivo, Gal-3 protein and mRNA were not detectable in glomeruli from nondiabetic rats until 12 months after initiating the study. On the contrary, in diabetic rats, Gal-3 expression was observed at 2 months of disease duration, and it increased thereafter. Both p60 and p90 immunoreactivities were observed at the glomerular level with slightly increased expression of p90, but not p60, in diabetic versus nondiabetic animals. In vitro, Gal-3 was not detectable in mesangial cells cultured in NG (although it became evident after a certain number of passages in culture), whereas Gal-3 was detectable in cells grown on BSA. Prolonged exposure (2-4 weeks) of mesangial cells to HG but not to M, as well as growing cells on BSA-AGE and, to a lesser extent, BSA-AM, induced or significantly increased the expression of Gal-3, both protein (up to 2.65-fold) and mRNA (up to 3.10-fold) and its secretion in the medium (by ~50%). Both p60 and p90 were demonstrated in mesangial cells under NG conditions, and the expression of p90, but not p60, was upregulated by ~20% by HG or BSA-AGE. These results indicate that 1) under basal conditions, Gal-3, unlike p90 and p60, is not detectable in the mesangium but becomes expressed with aging and 2) the diabetic milieu induces or upregulates Gal-3 production, whereas it increases only slightly the expression of p90, but not p60. Gal-3 expression or overexpression may modulate the AGE-receptor-mediated events by modifying the function of the AGE-receptor complex. Additionally, it may exert direct effects on tissue remodeling by virtue of its adhesive and growthregulating properties.

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Galectin-3 Stimulates Cell Proliferation

Cited by 177 publications

References 37 publications

Galectin-1 and Galectin-3 in Chronic Pancreatitis

Galectin-1 and Galectin-3 in Chronic Pancreatitis

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

The diabetic milieu modulates the advanced glycation end product-receptor complex in the mesangium by inducing or upregulating galectin-3 expression.

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